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Showing drug card for Acarbose (DB00284)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:47:36
Primary Accession Number DB00284
Secondary Accession Number
  • APRD00656
Name Acarbose
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description An inhibitor of alpha glucosidase that retards the digestion and absorption of carbohydrates in the small intestine and hence reduces the increase in blood-glucose concentrations after a carbohydrate load. It is given orally to non-insulin dependent diabetes mellitus patients where diet modification or oral hypoglycemic agents do not control their condition. (From Martindale The Extra Pharmacopoeia, 31st ed)
Synonyms Not Available
Brand Names
  1. Glucobay
  2. Prandase
  3. Precose
Brand Mixtures Not Available
Chemical IUPAC Name (2R,3R,4R,5S,6R)-5-[(2R,3R,4R,5S,6R)-5-[(2R,3R,4S,5S,6R)-3,4-dihydroxy-6-methyl-5-[[(1S,4S,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)-1-cyclohex-2-enyl]amino]oxan-2-yl]oxy-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-6-(hydroxymethyl)oxane-2,3,4-triol
Chemical Formula C25H43NO18
Chemical Structure Structure
CAS Registry Number 56180-94-0
InChI Identifier InChI=1/C25H43NO18/c1-6-11(26-8-2-7(3-27)12(30)15(33)13(8)31)14(32)19(37)24(40-6)43-22-10(5-29)42-25(20(38)17(22)35)44-21-9(4-28)41-23(39)18(36)16(21)34/h2,6,8-39H,3-5H2,1H3/t6-,8+,9-,10-,11-,12+,13+,14+,15+,16-,17-,18-,19-,20-,21-,22-,23-,24-,25-/m1/s1
InChI Key XUFXOAAUWZOOIT-JMPDRRIHBD
KEGG Drug D00216 Link Image
KEGG Compound C06802 Link Image
PubChem Compound 441184 Link Image
PubChem Substance 7847283 Link Image
ChEBI ID 2376 Link Image
PharmGKB ID PA448010 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02190893 Link Image
RxList Link http://www.rxlist.com/cgi/generic/acarbose.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Acarbose Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 645.6048
Monoisotopic Molecular Weight 645.2480
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.48e+02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -6.8 Source: PhysProp
Predicted LogP -2.65 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -0.64 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES C[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@H](O[C@@H]3[C@@H](CO)O[C@@H](O)[C@H](O)[C@H]3O)[C@H](O)[C@H]2O)[C@H](O)[C@@H](O)[C@@H]1N[C@H]1C=C(CO)[C@H](O)[C@H](O)[C@H]1O
Canonical SMILES CC1OC(OC2C(CO)OC(OC3C(CO)OC(O)C(O)C3O)C(O)C2O)C(O)C(O)C1NC1C=C(CO)C(O)C(O)C1O
Drug Category
  • Enzyme Inhibitors
  • Hypoglycemic Agents
ATC Codes
AHFS Codes
  • 68:20.02
Indication For treatment and management of diabetes type II (used in combination therapy as a second or third line agent)
Pharmacology Used to reduce blood gluose in patients with type 2 diabetes. Acarbose is a complex oligosaccharide that delays the digestion of ingested carbohydrates, thereby resulting in a smaller rise in blood glucose concentration following meals. Acarbose binds to and inhibits alpha amylase and alpha-gluocside hydrolases. In diabetic patients, this enzyme inhibition results in a delayed glucose absorption and a lowering of postprandial hyperglycemia.
Mechanism of Action Acarbose reversibly bind to pancreatic alpha-amylase and membrane-bound intestinal alpha-glucoside hydrolases. These enzymes inhibit hydrolysis of complex starches to oligosaccharides in the lumen of the small intestine and hydrolysis of oligosaccharides, trisaccharides, and disaccharides to glucose and other monosaccharides in the brush border of the small intestine.
Absorption Extremely low bioavailability.
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life 2 hours
Dosage Forms
Form Route
Tablet Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Digoxin Decreased serum levels of digoxin, it is thought that acarbose reduces digoxin absorption.
Food Interactions
  • Take with food, at beginning of each meal.
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Maltase-glucoamylase, intestinal
  2. Lysosomal alpha-glucosidase
  3. Sucrase-isomaltase, intestinal
  4. Pancreatic alpha-amylase
Drug Target 1 [top]
Target 1 ID 929
Target 1 Name Maltase-glucoamylase, intestinal
Target 1 Synonyms
  1. Alpha-glucosidase
  2. EC 3.2.1.20
  3. EC 3.2.1.3
  4. Glucoamylase
Target 1 Gene Name MGAM
Target 1 Protein Sequence >Maltase-glucoamylase, intestinal 
ARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTPD
PGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWNP
QGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTSN
RFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSS
IGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYG
AQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQ
EYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDERR
DFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSS
DGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSV
SGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTV
FPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICGF
ALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLP
YLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYV
PDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLI
IALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFNE
IKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWSIKIRDE
EKIDCYPDENGASAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADISL
KSSVYANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNKNRYEVPVPLNIPSMPSSTPEGQ
LYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFSDMFIRISTRLPSKYLYGFGETEHRS
YRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPLP
ALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEIAS
LYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAIS
GNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYVA
FPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDASL
NHPPYMPHLESRDRGLSSKTLCMESQQILPDGSLVQHYNVHNLYGWSQTRPTYEAVQEVT
GQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFFQ
DAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDVAFVNISRTVLQTRYTLLPYLYT
LMHKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRAR
WYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRQKFMGFKIALD
DEGTAGGWLFWDDGQSIDTYGKGLYYLASFSASQNTMQSHIIFNNYITGTNPLKLGYIEI
WGVGSVPVTSVSISVSGMVITPSFNNDPTTQVLSIDVTDRNISLHNFTSLTWISTL
Target 1 Number of Residues 1886
Target 1 Molecular Weight 209724
Target 1 Theoretical pI 5.14
Target 1 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
Process
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
Component
Not Available
Target 1 General Function Carbohydrate transport and metabolism
Target 1 Specific Function May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing
Target 1 Pathways
Name SMPDB Link KEGG Link
Galactose metabolism SMP00043 Link Image map00052 Link Image
Target 1 Reactions
  • Hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose ALL_REAC (other) R01790 R01791 R06199(G)
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 13-33
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 17648144 Link Image
Target 1 UniProtKB/Swiss-Prot ID O43451 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name MGA_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Cell membrane
  • apical cell membrane
  • single- pass type II membrane protein. Brush border
Target 1 Gene Sequence >5574 bp 
ATGGCAAGAAAGAAGCTGAAAAAATTTACTACTTTGGAGATTGTGCTCAGTGTTCTTCTG
CTTGTGTTGTTTATCATCAGTATTGTTCTAATTGTGCTTTTAGCCAAAGAGTCACTGAAA
TCAACAGCCCCAGATCCTGGGACAACTGGTACCCCAGATCCTGGGACAACTGGTACCCCA
GATCCTGGAACAACTGGTACCACACATGCTAGGACAACGGGTCCCCCAGATCCTGGAACA
ACTGGTACCACTCCTGTTTCTGCTGAATGTCCAGTGGTAAATGAATTGGAACGAATTAAT
TGCATCCCTGACCAGCCGCCAACAAAGGCCACATGTGACCAACGTGGCTGTTGCTGGAAT
CCCCAGGGAGCTGTAAGTGTTCCCTGGTGCTACTATTCCAAGAATCATAGCTACCATGTA
GAGGGCAACCTTGTCAACACAAATGCAGGATTCACAGCCCGGTTGAAAAATCTGCCTTCT
TCACCAGTGTTTGGAAGCAATGTTGACAATGTTCTTCTCACAGCAGAATATCAGACATCT
AATCGTTTCCACTTTAAGTTGACTGACCAAACCAATAACAGGTTTGAAGTGCCCCACGAA
CACGTGCAGTCCTTCAGTGGAAATGCTGCTGCTTCTTTGACCTACCAAGTTGAAATCTCC
AGACAGCCATTTAGCATCAAAGTGACCAGAAGAAGCAACAATCGTGTTTTGTTTGACTCG
AGCATTGGGCCCCTACTGTTTGCTGACCAGTTCTTGCAGCTCTCCACTCGACTGCCTAGC
ACTAACGTGTATGGCCTGGGAGAGCATGTGCACCAGCAGTATCGGCATGATATGAATTGG
AAGACCTGGCCCATATTTAACAGAGACACAACTCCCAATGGAAACGGAACTAATTTGTAT
GGTGCGCAGACATTCTTCTTGTGCCTTGAAGATGCTAGTGGATTGTCCTTTGGGGTGTTT
CTGATGAACAGCAATGCCATGGAGGTTGTCCTTCAGCCTGCGCCAGCCATCACTTACCGC
ACCATTGGGGGCATTCTCGACTTCTATGTGTTCTTGGGAAACACTCCAGAGCAAGTTGTT
CAAGAATATCTAGAGCTCATTGGGCGGCCAGCCCTTCCCTCCTACTGGGCGCTTGGATTT
CACCTCAGTCGTTACGAATATGGAACCTTAGACAACATGAGGGAAGTCGTGGAGAGAAAT
CGCGCAGCACAGCTCCCTTATGATGTTCAGCATGCTGATATTGATTATATGGATGAGAGA
AGGGACTTCACTTATGATTCAGTGGATTTTAAAGGCTTCCCTGAATTTGTCAACGAGTTA
CACAATAATGGACAGAAGCTTGTCATCATTGTGGATCCAGCCATCTCCAACAACTCTTCC
TCAAGTAAACCCTATGGCCCATATGACAGGGGTTCAGATATGAAGATATGGGTGAATAGT
TCAGATGGAGTGACTCCACTCATTGGGGAGGTCTGGCCTGGACAAACTGTGTTTCCTGAT
TATACCAATCCCAACTGTGCTGTTTGGTGGACAAAGGAATTTGAGCTTTTTCACAATCAA
GTAGAGTTTGATGGAATCTGGATTGATATGAATGAAGTCTCCAACTTTGTTGATGGTTCG
GTCTCAGGATGTTCCACAAACAACCTAAATAATCCCCCATTCACTCCCAGAATCCTGGAT
GGGTACCTGTTCTGCAAGACTCTCTGTATGGATGCAGTGCAGCACTGGGGCAAGCAGTAT
GACATTCACAATCTGTATGGCTACTCCATGGCGGTCGCCACAGCAGAAGCTGCCAAGACT
GTGTTCCCTAATAAGAGAAGCTTCATTCTGACCCGTTCTACCTTTGCGGGCTCTGGCAAG
TTTGCAGCACATTGGTTAGGAGACAACACTGCCACCTGGGATGACCTGAGATGGTCCATC
CCTGGCGTGCTTGAGTTCAACCTTTTTGGCATCCCAATGGTGGGTCCTGACATATGTGGC
TTTGCTTTGGACACCCCTGAGGAGCTCTGTAGGCGGTGGATGCAGTTGGGTGCATTTTAT
CCGTTTTCTAGAAATCACAATGGCCAAGGCTACAAGGACCAGGATCCTGCCTCCTTTGGA
GCTGACTCCCTGCTGTTGAATTCCTCCAGGCACTACCTTAACATCCGCTATACTCTATTG
CCCTACCTATACACCCTTTTCTTCCGTGCTCACAGCCGAGGGGACACGGTGGCCAGGCCC
CTTTTGCATGAGTTCTACGAGGACAACAGCACTTGGGATGTGCACCAACAGTTCTTATGG
GGGCCCGGCCTCCTCATCACTCCAGTTCTGGATGAAGGTGCAGAGAAAGTGATGGCATAT
GTGCCTGATGCTGTCTGGTATGACTACGAGACTGGGAGCCAAGTGAGATGGAGGAAGCAA
AAAGTCGAGATGGAACTTCCTGGAGACAAAATTGGACTTCACCTTCGAGGAGGCTACATC
TTCCCCACACAGCAGCCAAATACAACCACTCTGGCCAGTCGAAAGAACCCTCTTGGTCTT
ATCATTGCCCTAGATGAGAACAAAGAAGCAAAAGGAGAACTTTTCTGGGATGATGGGGAA
ACGAAGGATACTGTGGCCAATAAAGTGTATCTTTTATGTGAGTTTTCTGTCACTCAAAAC
CGCTTGGAGGTGAATATTTCACAATCAACCTACAAGGACCCCAATAATTTAGCATTTAAT
GAGATTAAAATTCTTGGGACGGAGGAACCTAGCAATGTTACAGTGAAACACAATGGTGTC
CCAAGTCAGACTTCTCCTACAGTCACTTATGATTCTAACCTGAAGGTTGCCATTATCACA
GATATTGATCTTCTCCTGGGAGAAGCATACACAGTGGAATGGAGCATAAAGATAAGGGAT
GAAGAAAAAATAGACTGTTACCCTGATGAGAATGGTGCTTCTGCCGAAAACTGCACTGCC
CGTGGCTGTATCTGGGAGGCATCCAATTCTTCTGGAGTCCCTTTTTGCTATTTTGTCAAC
GACCTATACTCTGTCAGTGATGTTCAGTATAATTCCCATGGGGCCACAGCTGACATCTCC
TTAAAGTCTTCCGTTTATGCCAATGCCTTCCCCTCCACACCCGTGAACCCCCTTCGCCTG
GATGTCACTTACCATAAGAATGAAATGCTGCAGTTCAAGATTTATGATCCCAACAAGAAT
CGGTATGAAGTTCCAGTCCCTCTGAACATACCCAGCATGCCATCCAGCACCCCTGAGGGT
CAACTCTATGATGTGCTCATTAAGAAGAATCCATTTGGGATTGAAATTCGCCGGAAGAGT
ACAGGCACTATAATTTGGGACTCTCAGCTCCTTGGCTTTACCTTCAGTGACATGTTTATC
CGCATCTCCACCCGCCTTCCCTCCAAGTACCTCTATGGCTTTGGGGAAACTGAGCACAGG
TCCTATAGGAGAGACTTGGAGTGGCACACTTGGGGGATGTTCTCCCGAGACCAGCCCCCA
GGGTACAAGAAGAATTCCTATGGTGTCCACCCCTACTACATGGGGCTGGAGGAGGACGGC
AGTGCCCATGGAGTGCTCCTGCTGAACAGCAATGCCATGGATGTGACGTTCCAGCCCCTG
CCTGCCTTGACATACCGCACCACAGGGGGAGTTCTGGACTTTTATGTGTTCTTGGGGCCG
ACTCCAGAGCTTGTCACCCAGCAGTACACTGAGTTGATTGGCCGGCCTGTGATGGTACCT
TACTGGTCTTTGGGGTTCCAGCTGTGTCGCTATGGCTACCAGAATGACTCTGAGATCGCC
AGCTTGTATGATGAGATGGTGGCTGCCCAGATCCCTTATGATGTGCAGTACTCAGACATC
GACTACATGGAGCGGCAGCTGGACTTCACCCTCAGCCCCAAGTTTGCTGGGTTTCCAGCT
CTGATCAATCGCATGAAGGCTGATGGGATGCGGGTCATCCTCATTCTGGATCCAGCCATT
TCTGGCAATGAGACACAGCCTTATCCTGCCTTCACTCGGGGCGTGGAGGATGACGTCTTC
ATCAAATACCCAAATGATGGAGACATTGTCTGGGGAAAGGTCTGGCCTGATTTTCCTGAT
GTTGTTGTGAATGGGTCTCTAGACTGGGACAGCCAAGTGGAGCTATATCGAGCTTATGTG
GCCTTCCCAGACTTTTTCCGTAATTCAACTGCCAAGTGGTGGAAGAGGGAAATAGAAGAA
CTATACAACAATCCACAGAATCCAGAGAGGAGCTTGAAGTTTGATGGCATGTGGATTGAT
ATGAATGAACCATCAAGCTTCGTGAATGGGGCAGTTTCTCCAGGCTGCAGGGACGCCTCT
CTGAACCACCCTCCCTACATGCCACATTTGGAGTCCAGGGACAGGGGCCTGAGCAGCAAG
ACCCTTTGTATGGAGAGTCAGCAGATCCTCCCAGACGGCTCCCTGGTGCAGCACTACAAC
GTGCACAACCTGTATGGGTGGTCCCAGACCAGACCCACATACGAAGCCGTGCAGGAGGTG
ACGGGACAGCGAGGGGTCGTCATCACCCGCTCCACATTTCCCTCTTCTGGCCGCTGGGCA
GGACATTGGCTGGGAGACAACACGGCCGCATGGGATCAGCTGAAGAAGTCTATCATTGGC
ATGATGGAGTTCAGCCTCTTCGGCATATCCTATACGGGAGCAGATATCTGTGGGTTCTTT
CAAGATGCTGAATATGAGATGTGTGTTCGCTGGATGCAGCTGGGGGCCTTTTACCCCTTC
TCAAGAAACCACAACACCATTGGGACCAGGAGACAAGACCCTGTGTCCTGGGATGTTGCT
TTTGTGAATATTTCCAGAACTGTCCTGCAGACCAGATACACCCTGTTGCCATATCTGTAT
ACCTTGATGCATAAGGCCCACACGGAGGGCGTCACTGTTGTGCGGCCTCTGCTCCATGAA
TTTGTGTCAGACCAGGTGACATGGGACATAGACAGTCAGTTCCTGCTGGGCCCAGCCTTC
CTGGTCAGCCCTGTCCTGGAGCGTAATGCCAGAAATGTCACTGCATATTTCCCTAGAGCC
CGCTGGTATGATTACTACACGGGTGTGGATATTAATGCAAGAGGAGAGTGGAAGACCTTG
CCAGCCCCTCTTGACCACATTAATCTTCATGTCCGTGGGGGCTACATCCTGCCCTGGCAA
GAGCCTGCACTGAACACCCACTTAAGCCGCCAGAAATTCATGGGCTTCAAAATTGCCTTG
GATGATGAAGGAACTGCTGGGGGCTGGCTCTTCTGGGATGATGGGCAAAGCATTGATACC
TATGGGAAAGGACTCTATTACTTGGCCAGCTTTTCTGCCAGCCAGAATACGATGCAAAGC
CATATAATTTTCAACAATTACATCACTGGTACAAATCCTTTGAAACTGGGCTACATTGAA
ATCTGGGGAGTGGGCAGTGTCCCCGTTACCAGTGTCAGCATCTCTGTGAGTGGCATGGTC
ATAACACCCTCCTTCAACAATGACCCCACGACACAGGTATTAAGCATCGATGTGACTGAC
AGAAACATCAGCCTACATAATTTTACTTCATTGACGTGGATAAGCACTCTGTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID MGAM Link Image
Target 1 GenAtlas ID MGAM Link Image
Target 1 HGNC ID HGNC:7043 Link Image
Target 1 Chromosome Location 7
Target 1 Locus 7q34
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Danielsen EM: Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte. EMBO J. 1987 Oct;6(10):2891-6. [PubMed Link Image]
  2. Naim HY, Sterchi EE, Lentze MJ: Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase. J Biol Chem. 1988 Dec 25;263(36):19709-17. [PubMed Link Image]
  3. Nichols BL, Eldering J, Avery S, Hahn D, Quaroni A, Sterchi E: Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase. J Biol Chem. 1998 Jan 30;273(5):3076-81. [PubMed Link Image]
Target 1 Drug References
  1. Okumiya T, Keulemans JL, Kroos MA, Van der Beek NM, Boer MA, Takeuchi H, Van Diggelen OP, Reuser AJ: A new diagnostic assay for glycogen storage disease type II in mixed leukocytes. Mol Genet Metab. 2006 May;88(1):22-8. Epub 2005 Dec 15. [PubMed Link Image]
  2. Zhang H, Kallwass H, Young SP, Carr C, Dai J, Kishnani PS, Millington DS, Keutzer J, Chen YT, Bali D: Comparison of maltose and acarbose as inhibitors of maltase-glucoamylase activity in assaying acid alpha-glucosidase activity in dried blood spots for the diagnosis of infantile Pompe disease. Genet Med. 2006 May;8(5):302-6. [PubMed Link Image]
  3. Gelb MH, Turecek F, Scott CR, Chamoles NA: Direct multiplex assay of enzymes in dried blood spots by tandem mass spectrometry for the newborn screening of lysosomal storage disorders. J Inherit Metab Dis. 2006 Apr-Jun;29(2-3):397-404. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 1016
Target 2 Name Lysosomal alpha-glucosidase
Target 2 Synonyms
  1. Acid maltase
  2. Aglucosidase alfa
  3. EC 3.2.1.20
  4. Lysosomal alpha-glucosidase precursor
Target 2 Gene Name GAA
Target 2 Protein Sequence >Lysosomal alpha-glucosidase precursor 
MGVRHPPCSHRLLAVCALVSLATAALLGHILLHDFLLVPRELSGSSPVLEETHPAHQQGA
SRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGA
QMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLH
FTIKDPANRRYEVPLETPRVHSRAPSPLYSVEFSEEPFGVIVHRQLDGRVLLNTTVAPLF
FADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLA
LEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGY
PFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDG
FRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKV
WPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELEN
PPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISR
STFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVR
WTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAG
ETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPI
EALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQP
MALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQ
LQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC
Target 2 Number of Residues 967
Target 2 Molecular Weight 105339
Target 2 Theoretical pI 5.91
Target 2 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
Process
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
Component
Not Available
Target 2 General Function Carbohydrate transport and metabolism
Target 2 Specific Function Essential for the degradation of glygogen to glucose in lysosomes
Target 2 Pathways
Name SMPDB Link KEGG Link
Galactose metabolism SMP00043 Link Image map00052 Link Image
Target 2 Reactions
  • Hydrolysis of terminal, non-reducing 1,4-linked alpha-D-glucose residues with release of alpha-D-glucose ALL_REAC (other) R00028 R00801 R00802 R01101 R06084(G) R06087(G) R06088(G) R06091(G) INHIBITOR Castanospermine
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-27
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 31608 Link Image
Target 2 UniProtKB/Swiss-Prot ID P10253 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name LYAG_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Lysosome
Target 2 Gene Sequence >2859 bp 
ATGGGAGTGAGGCACCCGCCCTGCTCCCACCGGCTCCTGGCCGTCTGCGCCCTCGTGTCC
TTGGCAACCGCTGCACTCCTGGGGCACATCCTACTCCATGATTTCCTGCTGGTTCCCCGA
GAGCTGAGTGGCTCCTCCCCAGTCCTGGAGGAGACTCACCCAGCTCACCAGCAGGGAGCC
AGCAGACCAGGGCCCCGGGATGCCCAGGCACACCCCGGCCGTCCCAGAGCAGTGCCCACA
CAGTGCGACGTCCCCCCCAACAGCCGCTTCGATTGCGCCCCTGACAAGGCCATCACCCAG
GAACAGTGCGAGGCCCGCGGCTGCTGCTACATCCCTGCAAAGCAGGGGCTGCAGGGAGCC
CAGATGGGGCAGCCCTGGTGCTTCTTCCCACCCAGCTACCCCAGCTACAAGCTGGAGAAC
CTGAGCTCCTCTGAAATGGGCTACACGGCCACCCTGACCCGTACCACCCCCACCTTCTTC
CCCAAGGACATCCTGACCCTGCGGCTGGACGTGATGATGGAGACTGAGAACCGCCTCCAC
TTCACGATCAAAGATCCAGCTAACAGGCGCTACGAGGTGCCCTTGGAGACCCCGCGTGTC
CACAGCCGGGCACCGTCCCCACTCTACAGCGTGGAGTTCTCCGAGGAGCCCTTCGGGGTG
ATCGTGCACCGGCAGCTGGACGGCCGCGTGCTGCTGAACACGACGGTGGCGCCCCTGTTC
TTTGCGGACCAGTTCCTTCAGCTGTCCACCTCGCTGCCCTCGCAGTATATCACAGGCCTC
GCCGAGCACCTCAGTCCCCTGATGCTCAGCACCAGCTGGACCAGGATCACCCTGTGGAAC
CGGGACCTTGCGCCCACGCCCGGTGCGAACCTCTACGGGTCTCACCCTTTCTACCTGGCG
CTGGAGGACGGCGGGTCGGCACACGGGGTGTTCCTGCTAAACAGCAATGCCATGGATGTG
GTCCTGCAGCCGAGCCCTGCCCTTAGCTGGAGGTCGACAGGTGGGATCCTGGATGTCTAC
ATCTTCCTGGGCCCAGAGCCCAAGAGCGTGGTGCAGCAGTACCTGGACGTTGTGGGATAC
CCGTTCATGCCGCCATACTGGGGCCTGGGCTTCCACCTGTGCCGCTGGGGCTACTCCTCC
ACCGCTATCACCCGCCAGGTGGTGGAGAACATGACCAGGGCCCACTTCCCCCTGGACGTC
CAATGGAACGACCTGGACTACATGGACTCCCGGAGGGACTTCACGTTCAACAAGGATGGC
TTCCGGGACTTCCCGGCCATGGTGCAGGAGCTGCACCAGGGCGGCCGGCGCTACATGATG
ATCGTGGATCCTGCCATCAGCAGCTCGGGCCCTGCCGGGAGCTACAGGCCCTACGACGAG
GGTCTGCGGAGGGGGGTTTTCATCACCAACGAGACCGGCCAGCCGCTGATTGGGAAGGTA
TGGCCCGGGTCCACTGCCTTCCCCGACTTCACCAACCCCACAGCCCTGGCCTGGTGGGAG
GACATGGTGGCTGAGTTCCATGACCAGGTGCCCTTCGACGGCATGTGGATTGACATGAAC
GAGCCTTCCAACTTCATCAGAGGCTCTGAGGACGGCTGCCCCAACAATGAGCTGGAGAAC
CCACCCTACGTGCCTGGGGTGGTTGGGGGGACCCTCCAGGCGGCCACCATCTGTGCCTCC
AGCCACCAGTTTCTCTCCACACACTACAACCTGCACAACCTCTACGGCCTGACCGAAGCC
ATCGCCTCCCACAGGGCGCTGGTGAAGGCTCGGGGGACACGCCCATTTGTGATCTCCCGC
TCGACCTTTGCTGGCCACGGCCGATACGCCGGCCACTGGACGGGGGACGTGTGGAGCTCC
TGGGAGCAGCTCGCCTCCTCCGTGCCAGAAATCCTGCAGTTTAACCTGCTGGGGGTGCCT
CTGGTCGGGGCCGACGTCTGCGGCTTCCTGGGCAACACCTCAGAGGAGCTGTGTGTGCGC
TGGACCCAGCTGGGGGCCTTCTACCCCTTCATGCGGAACCACAACAGCCTGCTCAGTCTG
CCCCAGGAGCCGTACAGCTTCAGCGAGCCGGCCCAGCAGGCCATGAGGAAGGCCCTCACC
CTGCGCTACGCACTCCTCCCCCACCTCTACACACTGTTCCACCAGGCCCACGTCGCGGGG
GAGACCGTGGCCCGGCCCCTCTTCCTGGAGTTCCCCAAGGACTCTAGCACCTGGACTGTG
GACCACCAGCTCCTGTGGGGGGAGGCCCTGCTCATCACCCCAGTGCTCCAGGCCGGGAAG
GCCGAAGTGACTGGCTACTTCCCCTTGGGCACATGGTACGACCTGCAGACGGTGCCAATA
GAGGCCCTTGGCAGCCTCCCACCCCCACCTGCAGCTCCCCGTGAGCCAGCCATCCACAGC
GAGGGGCAGTGGGTGACGCTGCCGGCCCCCCTGGACACCATCAACGTCCACCTCCGGGCT
GGGTACATCATCCCCCTGCAGGGCCCTGGCCTCACAACCACAGAGTCCCGCCAGCAGCCC
ATGGCCCTGGCTGTGGCCCTGACCAAGGGTGGAGAGGCCCGAGGGGAGCTGTTCTGGGAC
GATGGAGAGAGCCTGGAAGTGCTGGAGCGAGGGGCCTACACACAGGTCATCTTCCTGGCC
AGGAATAACACGATCGTGAATGAGCTGGTACGTGTGACCAGTGAGGGAGCTGGCCTGCAG
CTGCAGAAGGTGACTGTCCTGGGCGTGGCCACGGCGCCCCAGCAGGTCCTCTCCAACGGT
GTCCCTGTCTCCAACTTCACCTACAGCCCCGACACCAAGGTCCTGGACATCTGTGTCTCG
CTGTTGATGGGAGAGCAGTTTCTCGTCAGCTGGTGTTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID GAA Link Image
Target 2 GenAtlas ID GAA Link Image
Target 2 HGNC ID HGNC:4065 Link Image
Target 2 Chromosome Location 17
Target 2 Locus 17q25.2-q25.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Raben N, Lee E, Lee L, Hirschhorn R, Plotz PH: Novel mutations in African American patients with glycogen storage disease Type II. Mutations in brief no. 209. Online. Hum Mutat. 1999;13(1):83-4. [PubMed Link Image]
  2. Ko TM, Hwu WL, Lin YW, Tseng LH, Hwa HL, Wang TR, Chuang SM: Molecular genetic study of Pompe disease in Chinese patients in Taiwan. Hum Mutat. 1999;13(5):380-4. [PubMed Link Image]
  3. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  4. Zhong N, Martiniuk F, Tzall S, Hirschhorn R: Identification of a missense mutation in one allele of a patient with Pompe disease, and use of endonuclease digestion of PCR-amplified RNA to demonstrate lack of mRNA expression from the second allele. Am J Hum Genet. 1991 Sep;49(3):635-45. [PubMed Link Image]
  5. Martiniuk F, Mehler M, Bodkin M, Tzall S, Hirschhorn K, Zhong N, Hirschhorn R: Identification of a missense mutation in an adult-onset patient with glycogenosis type II expressing only one allele. DNA Cell Biol. 1991 Nov;10(9):681-7. [PubMed Link Image]
  6. Hermans MM, Kroos MA, van Beeumen J, Oostra BA, Reuser AJ: Human lysosomal alpha-glucosidase. Characterization of the catalytic site. J Biol Chem. 1991 Jul 25;266(21):13507-12. [PubMed Link Image]
  7. Hermans MM, de Graaff E, Kroos MA, Wisselaar HA, Oostra BA, Reuser AJ: Identification of a point mutation in the human lysosomal alpha-glucosidase gene causing infantile glycogenosis type II. Biochem Biophys Res Commun. 1991 Sep 16;179(2):919-26. [PubMed Link Image]
  8. Martiniuk F, Mehler M, Tzall S, Meredith G, Hirschhorn R: Sequence of the cDNA and 5'-flanking region for human acid alpha-glucosidase, detection of an intron in the 5' untranslated leader sequence, definition of 18-bp polymorphisms, and differences with previous cDNA and amino acid sequences. DNA Cell Biol. 1990 Mar;9(2):85-94. [PubMed Link Image]
  9. Martiniuk F, Bodkin M, Tzall S, Hirschhorn R: Identification of the base-pair substitution responsible for a human acid alpha glucosidase allele with lower "affinity" for glycogen (GAA 2) and transient gene expression in deficient cells. Am J Hum Genet. 1990 Sep;47(3):440-5. [PubMed Link Image]
  10. Hoefsloot LH, Hoogeveen-Westerveld M, Reuser AJ, Oostra BA: Characterization of the human lysosomal alpha-glucosidase gene. Biochem J. 1990 Dec 1;272(2):493-7. [PubMed Link Image]
  11. 3049072 Hoefsloot LH, Hoogeveen-Westerveld M, Kroos MA, van Beeumen J, Reuser AJ, Oostra BA: Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrase-isomaltase complex. EMBO J. 1988 Jun;7(6):1697-704.
  12. 7603530 Reuser AJ, Kroos MA, Hermans MM, Bijvoet AG, Verbeet MP, Van Diggelen OP, Kleijer WJ, Van der Ploeg AT: Glycogenosis type II (acid maltase deficiency). Muscle Nerve. 1995;3:S61-9.
  13. 7695647 Lin CY, Shieh JJ: Identification of a de novo point mutation resulting in infantile form of Pompe's disease. Biochem Biophys Res Commun. 1995 Mar 17;208(2):886-93.
  14. 7717400 Boerkoel CF, Exelbert R, Nicastri C, Nichols RC, Miller FW, Plotz PH, Raben N: Leaky splicing mutation in the acid maltase gene is associated with delayed onset of glycogenosis type II. Am J Hum Genet. 1995 Apr;56(4):887-97.
  15. 7866409 Huie ML, Hirschhorn R, Chen AS, Martiniuk F, Zhong N: Mutation at the catalytic site (M519V) in glycogen storage disease type II (Pompe disease). Hum Mutat. 1994;4(4):291-3.
  16. 7881422 Hermans MM, De Graaff E, Kroos MA, Mohkamsing S, Eussen BJ, Joosse M, Willemsen R, Kleijer WJ, Oostra BA, Reuser AJ: The effect of a single base pair deletion (delta T525) and a C1634T missense mutation (pro545leu) on the expression of lysosomal alpha-glucosidase in patients with glycogen storage disease type II. Hum Mol Genet. 1994 Dec;3(12):2213-8.
  17. 7981676 Huie ML, Chen AS, Brooks SS, Grix A, Hirschhorn R: A de novo 13 nt deletion, a newly identified C647W missense mutation and a deletion of exon 18 in infantile onset glycogen storage disease type II (GSDII). Hum Mol Genet. 1994 Jul;3(7):1081-7.
  18. 8094613 Hermans MM, de Graaff E, Kroos MA, Wisselaar HA, Willemsen R, Oostra BA, Reuser AJ: The conservative substitution Asp-645-->Glu in lysosomal alpha-glucosidase affects transport and phosphorylation of the enzyme in an adult patient with glycogen-storage disease type II. Biochem J. 1993 Feb 1;289 ( Pt 3):687-93.
  19. 8401535 Hermans MM, Kroos MA, de Graaff E, Oostra BA, Reuser AJ: Two mutations affecting the transport and maturation of lysosomal alpha-glucosidase in an adult case of glycogen storage disease type II. Hum Mutat. 1993;2(4):268-73.
  20. 8435067 Hermans MM, Wisselaar HA, Kroos MA, Oostra BA, Reuser AJ: Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites. Biochem J. 1993 Feb 1;289 ( Pt 3):681-6.
  21. 8486380 Hermans MM, Svetkey LP, Oostra BA, Chen YT, Reuser AJ: The loss of a polymorphic glycosylation site caused by Thr-927-->Ile is linked to a second polymorphic Val-816-->Ile substitution in lysosomal alpha-glucosidase of American blacks. Genomics. 1993 Apr;16(1):300-1.
  22. 8834250 Tsunoda H, Ohshima T, Tohyama J, Sasaki M, Sakuragawa N, Martiniuk F: Acid alpha-glucosidase deficiency: identification and expression of a missense mutation (S529V) in a Japanese adult phenotype. Hum Genet. 1996 Apr;97(4):496-9.
  23. 8912788 Huie ML, Menaker M, McAlpine PJ, Hirschhorn R: Identification of an E689K substitution as the molecular basis of the human acid alpha-glucosidase type 4 allozyme (GAA*4). Ann Hum Genet. 1996 Sep;60(Pt 5):365-8.
  24. 9521422 Hermans MM, Kroos MA, Smeitink JA, van der Ploeg AT, Kleijer WJ, Reuser AJ: Glycogen Storage Disease type II: genetic and biochemical analysis of novel mutations in infantile patients from Turkish ancestry. Hum Mutat. 1998;11(3):209-15.
  25. 9535769 Huie ML, Tsujino S, Sklower Brooks S, Engel A, Elias E, Bonthron DT, Bessley C, Shanske S, DiMauro S, Goto YI, Hirschhorn R: Glycogen storage disease type II: identification of four novel missense mutations (D645N, G648S, R672W, R672Q) and two insertions/deletions in the acid alpha-glucosidase locus of patients of differing phenotype. Biochem Biophys Res Commun. 1998 Mar 27;244(3):921-7.
  26. 9660056 Kroos MA, van Leenen D, Verbiest J, Reuser AJ, Hermans MM: Glycogen storage disease type II: identification of a dinucleotide deletion and a common missense mutation in the lysosomal alpha-glucosidase gene. Clin Genet. 1998 May;53(5):379-82.
Target 2 Drug References
  1. Salehi A, Fan BG, Ekelund M, Nordin G, Lundquist I: TPN-evoked dysfunction of islet lysosomal activity mediates impairment of glucose-stimulated insulin release. Am J Physiol Endocrinol Metab. 2001 Jul;281(1):E171-9. [PubMed Link Image]
  2. Li Y, Scott CR, Chamoles NA, Ghavami A, Pinto BM, Turecek F, Gelb MH: Direct multiplex assay of lysosomal enzymes in dried blood spots for newborn screening. Clin Chem. 2004 Oct;50(10):1785-96. Epub 2004 Aug 3. [PubMed Link Image]
  3. Lundquist I, Panagiotidis G: The relationship of islet amyloglucosidase activity and glucose-induced insulin secretion. Pancreas. 1992;7(3):352-7. [PubMed Link Image]
  4. Zhang H, Kallwass H, Young SP, Carr C, Dai J, Kishnani PS, Millington DS, Keutzer J, Chen YT, Bali D: Comparison of maltose and acarbose as inhibitors of maltase-glucoamylase activity in assaying acid alpha-glucosidase activity in dried blood spots for the diagnosis of infantile Pompe disease. Genet Med. 2006 May;8(5):302-6. [PubMed Link Image]
  5. Gelb MH, Turecek F, Scott CR, Chamoles NA: Direct multiplex assay of enzymes in dried blood spots by tandem mass spectrometry for the newborn screening of lysosomal storage disorders. J Inherit Metab Dis. 2006 Apr-Jun;29(2-3):397-404. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 2129
Target 3 Name Sucrase-isomaltase, intestinal
Target 3 Synonyms
  1. EC 3.2.1.10]
  2. EC 3.2.1.48
  3. Isomaltase
Target 3 Gene Name SI
Target 3 Protein Sequence >Sucrase-isomaltase, intestinal 
MARKKFSGLEISLIVLFVIVTIIAIALIVVLATKTPAVDEISDSTSTPATTRVTTNPSDS
GKCPNVLNDPVNVRINCIPEQFPTEGICAQRGCCWRPWNDSLIPWCFFVDNHGYNVQDMT
TTSIGVEAKLNRIPSPTLFGNDINSVLFTTQNQTPNRFRFKITDPNNRRYEVPHQYVKEF
TGPTVSDTLYDVKVAQNPFSIQVIRKSNGKTLFDTSIGPLVYSDQYLQISARLPSDYIYG
IGEQVHKRFRHDLSWKTWPIFTRDQLPGDNNNNLYGHQTFFMCIEDTSGKSFGVFLMNSN
AMEIFIQPTPIVTYRVTGGILDFYILLGDTPEQVVQQYQQLVGLPAMPAYWNLGFQLSRW
NYKSLDVVKEVVRRNREAGIPFDTQVTDIDYMEDKKDFTYDQVAFNGLPQFVQDLHDHGQ
KYVIILDPAISIGRRANGTTYATYERGNTQHVWINESDGSTPIIGEVWPGLTVYPDFTNP
NCIDWWANECSIFHQEVQYDGLWIDMNEVSSFIQGSTKGCNVNKLNYPPFTPDILDKLMY
SKTICMDAVQNWGKQYDVHSLYGYSMAIATEQAVQKVFPNKRSFILTRSTFAGSGRHAAH
WLGDNTASWEQMEWSITGMLEFSLFGIPLVGADICGFVAETTEELCRRWMQLGAFYPFSR
NHNSDGYEHQDPAFFGQNSLLVKSSRQYLTIRYTLLPFLYTLFYKAHVFGETVARPVLHE
FYEDTNSWIEDTEFLWGPALLITPVLKQGADTVSAYIPDAIWYDYESGAKRPWRKQRVDM
YLPADKIGLHLRGGYIIPIQEPDVTTTASRKNPLGLIVALGENNTAKGDFFWDDGETKDT
IQNGNYILYTFSVSNNTLDIVCTHSSYQEGTTLAFQTVKILGLTDSVTEVRVAENNQPMN
AHSNFTYDASNQVLLIADLKLNLGRNFSVQWNQIFSENERFNCYPDADLATEQKCTQRGC
VWRTGSSLSKAPECYFPRQDNSYSVNSARYSSMGITADLQLNTANARIKLPSDPISTLRV
EVKYHKNDMLQFKIYDPQKKRYEVPVPLNIPTTPISTYEDRLYDVEIKENPFGIQIRRRS
SGRVIWDSWLPGFAFNDQFIQISTRLPSEYIYGFGEVEHTAFKRDLNWNTWGMFTRDQPP
GYKLNSYGFHPYYMALEEEGNAHGVFLLNSNAMDVTFQPTPALTYRTVGGILDFYMFLGP
TPQVATKQYHEVIGHPVMPAYWALGFQLCRYGYANTSEVRELYDAMVAANIPYDVQYTDI
DYMERQLDFTIGEAFQDLPQFVDKIRGEGMRYIIILDPAISGNETKTYPAFERGQQNDVF
VKWPNTNDICWAKVWPDLPNITIDKTLTEDEAVNASRAHVAFPDFFRTSTAEWWAREIVD
FYNEKMKFDGLWIDMNEPSSFVNGTTTNQCRNDELNYPPYFPELTKRTDGLHFRTICMEA
EQILSDGTSVLHYDVHNLYGWSQMKPTHDALQKTTGKRGIVISRSTYPTSGRWGGHWLGD
NYARWDNMDKSIIGMMEFSLFGISYTGADICGFFNNSEYHLCTRWMQLGAFYPYSRNHNI
ANTRRQDPASWNETFAEMSRNILNIRYTLLPYFYTQMHEIHANGGTVIRPLLHEFFDEKP
TWDIFKQFLWGPAFMVTPVLEPYVQTVNAYVPNARWFDYHTGKDIGVRGQFQTFNASYDT
INLHVRGGHILPCQEPAQNTFYSRQKHMKLIVAADDNQMAQGSLFWDDGESIDTYERDLY
LSVQFNLNQTTLTSTILKRGYINKSETRLGSLHVWGKGTTPVNAVTLTYNGNKNSLPFNE
DTTNMILRIDLTTHNVTLEEPIEINWS
Target 3 Number of Residues 1857
Target 3 Molecular Weight 209406
Target 3 Theoretical pI 5.39
Target 3 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
Process
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
Component
Not Available
Target 3 General Function Carbohydrate transport and metabolism
Target 3 Specific Function Plays an important role in the final stage of carbohydrate digestion
Target 3 Pathways
Name SMPDB Link KEGG Link
Starch and sucrose metabolism SMP00058 Link Image map00500 Link Image
Target 3 Reactions
  • Hydrolysis of 1,6-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by internal_xref(ec_num(3,2,1,1)) (alpha-amylase), and in isomaltose ALL_REAC (other) R01718 R01791 R06080(G) R06199(G)
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • 13-32
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 36645 Link Image
Target 3 UniProtKB/Swiss-Prot ID P14410 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name SUIS_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Cell membrane
  • apical cell membrane
  • single- pass type II membrane protein. Note=Brush border
Target 3 Gene Sequence >5484 bp 
ATGGCAAGAAAGAAATTTAGTGGATTGGAAATCTCTCTGATTGTCCTTTTTGTCATAGTT
ACTATAATAGCTATTGCCTTAATTGTTGTTTTAGCAACTAAGACACCTGCTGTTGATGAA
ATTAGTGATTCTACTTCAACTCCAGCTACTACTCGTGTGACTACAAATCCTTCTGATTCA
GGAAAATGTCCAAATGTGTTAAATGATCCTGTCAATGTGAGAATAAACTGCATTCCAGAA
CAATTCCCAACAGAGGGAATTTGTGCACAGAGAGGCTGCTGCTGGAGGCCGTGGAATGAC
TCTCTTATTCCTTGGTGCTTCTTCGTTGATAATCATGGTTATAACGTTCAAGACATGACA
ACAACAAGTATTGGAGTTGAAGCCAAATTAAACAGGATACCTTCACCTACACTATTTGGA
AATGACATCAACAGTGTTCTCTTCACAACTCAAAATCAGACACCCAATCGTTTCCGGTTC
AAGATTACTGATCCAAATAATAGAAGATATGAAGTTCCTCATCAGTATGTAAAAGAGTTT
ACTGGACCCACAGTTTCTGATACGTTGTATGATGTGAAGGTTGCCCAAAACCCATTTAGC
ATCCAAGTTATTAGGAAAAGCAACGGTAAAACTTTGTTTGACACCAGCATTGGTCCCTTA
GTGTACTCTGACCAGTACTTACAGATCTCAGCCCGTCTTCCAAGTGATTATATTTATGGT
ATTGGAGAACAAGTTCATAAGAGATTTCGTCATGATTTATCCTGGAAAACATGGCCAATT
TTTACTCGAGACCAACTTCCTGGTGATAATAATAATAATTTATACGGCCATCAAACATTC
TTTATGTGTATTGAAGATACATCTGGAAAGTCATTCGGTGTTTTTTTAATGAATAGCAAT
GCAATGGAGATTTTTATCCAGCCTACTCCAATAGTAACATATAGAGTTACCGGTGGCATT
CTGGATTTTTACATCCTTCTAGGAGATACACCAGAACAAGTAGTTCAACAGTATCAACAG
CTTGTTGGACTACCAGCAATGCCAGCATATTGGAATCTTGGATTCCAACTAAGTCGCTGG
AATTATAAGTCACTAGATGTAGTGAAAGAAGTGGTAAGGAGAAACCGGGAAGCTGGCATA
CCATTTGATACACAGGTCACTGATATTGACTACATGGAAGACAAGAAAGACTTTACTTAT
GATCAAGTTGCGTTTAACGGACTCCCTCAATTTGTGCAAGATTTGCATGACCATGGACAG
AAATATGTCATCATCTTGGACCCTGCAATTTCCATAGGTCGACGTGCCAATGGAACAACA
TATGCAACCTATGAGAGGGGAAACACACAACATGTGTGGATAAATGAGTCAGATGGAAGT
ACACCAATTATTGGAGAGGTATGGCCAGGATTAACAGTATACCCTGATTTCACTAATCCA
AACTGCATTGATTGGTGGGCAAATGAATGCAGTATTTTCCATCAAGAAGTGCAATATGAT
GGACTTTGGATTGACATGAATGAAGTTTCCAGCTTTATTCAAGGTTCAACAAAAGGATGT
AATGTAAACAAATTGAATTATCCACCGTTTACTCCTGATATTCTTGACAAACTCATGTAT
TCCAAAACAATTTGCATGGATGCTGTGCAGAACTGGGGTAAACAGTATGATGTTCATAGC
CTCTATGGATACAGCATGGCTATAGCCACAGAGCAAGCTGTACAAAAAGTTTTTCCTAAT
AAGAGAAGCTTCATTCTTACCCGCTCAACATTTGCTGGATCTGGAAGACATGCTGCTCAT
TGGTTAGGAGACAATACTGCTTCATGGGAACAAATGGAATGGTCTATAACTGGAATGCTG
GAGTTCAGTTTGTTTGGAATACCTTTGGTTGGAGCAGACATCTGTGGATTTGTGGCTGAA
ACCACAGAAGAACTTTGCAGAAGATGGATGCAACTTGGGGCATTTTATCCATTTTCCAGA
AACCATAATTCTGACGGATATGAACATCAGGATCCTGCATTTTTTGGGCAGAATTCACTT
TTGGTTAAATCATCAAGGCAGTATTTAACTATTCGCTACACCTTATTACCCTTCCTCTAC
ACTCTGTTTTATAAAGCCCATGTGTTTGGAGAAACAGTAGCAAGACCAGTTCTTCATGAG
TTTTATGAGGATACGAACAGCTGGATTGAGGACACTGAGTTTTTGTGGGGCCCTGCATTA
CTTATTACTCCTGTTCTAAAACAGGGAGCAGATACTGTGAGTGCCTACATCCCTGATGCT
ATTTGGTATGATTATGAATCTGGTGCAAAAAGGCCATGGAGGAAACAACGGGTTGATATG
TATCTTCCAGCAGACAAAATAGGATTACATCTTAGAGGAGGTTATATCATCCCCATTCAA
GAACCAGATGTAACAACAACAGCAAGCCGTAAGAATCCTCTAGGACTTATAGTCGCATTA
GGTGAAAACAACACAGCCAAAGGAGACTTTTTCTGGGATGATGGAGAAACTAAAGATACA
ATACAAAATGGCAACTACATATTATATACATTTTCAGTTTCTAATAACACATTAGATATT
GTGTGCACACATTCATCATATCAGGAAGGAACTACCTTAGCATTTCAGACTGTAAAAATC
CTTGGGTTGACAGACAGTGTTACAGAAGTTAGAGTGGCGGAAAATAATCAACCAATGAAC
GCTCATTCCAATTTCACTTATGATGCTTCTAACCAGGTTCTCCTAATTGCAGATCTCAAA
CTTAATCTTGGAAGAAACTTTAGTGTTCAATGGAATCAAATTTTCTCAGAAAATGAAAGA
TTTAATTGTTATCCAGATGCAGATTTGGCAACTGAACAAAAGTGCACACAACGTGGCTGT
GTATGGAGAACGGGTTCTTCTCTATCCAAAGCACCTGAGTGTTACTTTCCCAGACAAGAT
AACTCTTATTCAGTCAACTCAGCTCGCTATTCATCCATGGGTATAACAGCTGACCTCCAA
CTAAATACTGCAAATGCCAGAATAAAGTTACCTTCTGACCCCATCTCAACTCTTCGTGTG
GAGGTGAAATATCACAAAAATGATATGTTGCAGTTTAAGATTTATGATCCCCAAAAGAAG
AGATATGAAGTACCAGTACCGTTAAACATTCCAACCACCCCAATAAGTACTTATGAAGAC
AGACTTTATGATGTGGAAATCAAGGAAAATCCTTTTGGCATCCAGATTCGACGGAGAAGC
AGTGGAAGAGTCATTTGGGATTCTTGGCTGCCTGGATTTGCTTTTAATGACCAGTTCATT
CAAATATCGACTCGCCTGCCATCAGAATATATATATGGTTTTGGGGAAGTGGAACATACA
GCATTTAAGCGAGATCTGAACTGGAATACTTGGGGAATGTTCACAAGAGACCAACCCCCT
GGTTACAAACTTAATTCCTATGGATTTCATCCCTATTACATGGCTCTGGAAGAGGAGGGC
AATGCTCATGGTGTTTTCTTACTCAACAGCAATGCAATGGATGTTACATTCCAGCCAACT
CCTGCTCTAACTTACCGTACAGTTGGAGGGATCTTGGATTTTTATATGTTTTTGGGCCCA
ACTCCACAAGTTGCAACAAAGCAATACCATGAAGTAATTGGCCATCCAGTCATGCCAGCT
TATTGGGCTTTGGGATTCCAATTATGTCGTTATGGATATGCAAATACTTCAGAGGTTCGG
GAATTATATGACGCTATGGTGGCTGCTAACATCCCCTATGATGTTCAGTACACAGACATT
GACTACATGGAAAGGCAGCTAGACTTTACAATTGGTGAAGCATTCCAGGACCTTCCTCAG
TTTGTTGACAAAATAAGAGGAGAAGGAATGAGATACATTATTATCCTGGATCCAGCAATT
TCAGGAAATGAAACAAAGACTTACCCTGCATTTGAAAGAGGACAGCAGAATGATGTCTTT
GTCAAATGGCCAAACACCAATGACATTTGTTGGGCAAAGGTTTGGCCAGATTTGCCCAAC
ATAACAATAGATAAAACTCTAACGGAAGATGAAGCTGTTAATGCTTCCAGAGCTCATGTA
GCTTTCCCAGATTTCTTCAGGACTTCCACAGCAGAGTGGTGGGCCAGAGAAATTGTGGAC
TTTTACAATGAAAAGATGAAGTTTGATGGTTTGTGGATTGATATGAATGAGCCATCAAGT
TTTGTAAATGGAACAACTACTAATCAATGCAGAAATGACGAACTAAATTATCCACCTTAT
TTCCCAGAACTCACAAAAAGAACTGATGGATTACATTTCAGAACAATTTGCATGGAAGCT
GAGCAGATTCTTAGTGATGGAACATCAGTTTTGCATTACGATGTTCACAATCTCTATGGA
TGGTCACAGATGAAACCTACTCATGATGCATTGCAAAAGACAACTGGAAAAAGAGGGATT
GTAATTTCTCGTTCCACGTATCCTACTAGTGGACGATGGGGAGGACACTGGCTTGGAGAC
AACTATGCACGATGGGACAACATGGACAAATCAATCATTGGTATGATGGAATTTAGTCTG
TTTGGAATATCATATACTGGAGCAGACATCTGTGGTTTTTTCAACAACTCAGAATATCAT
CTCTGTACCCGCTGGATGCAACTTGGAGCATTTTATCCATACTCAAGGAATCACAACATT
GCAAATACTAGAAGACAAGATCCCGCTTCCTGGAATGAAACTTTTGCTGAAATGTCAAGG
AATATTCTAAATATTAGATACACCTTATTGCCCTATTTTTACACACAAATGCATGAAATT
CATGCTAATGGTGGCACTGTTATCCGACCCCTTTTGCATGAGTTCTTTGATGAAAAACCA
ACCTGGGATATATTCAAGCAGTTCTTATGGGGTCCAGCATTTATGGTTACCCCAGTACTG
GAACCTTATGTTCAAACTGTAAATGCCTACGTCCCCAATGCTCGGTGGTTTGACTACCAT
ACAGGCAAAGATATTGGCGTCAGAGGACAATTTCAAACATTTAATGCTTCTTATGACACA
ATAAACCTACATGTCCGTGGTGGTCACATCCTACCATGTCAAGAGCCAGCTCAAAACACA
TTTTACAGTCGACAAAAACACATGAAGCTCATTGTTGCTGCAGATGATAATCAGATGGCA
CAGGGTTCTCTGTTTTGGGATGATGGAGAGAGTATAGACACCTATGAAAGAGACCTATAT
TTATCTGTACAATTTAATTTAAACCAGACCACCTTAACAAGCACTATATTGAAGAGAGGT
TACATAAATAAAAGTGAAACGAGGCTTGGATCCCTTCATGTATGGGGGAAAGGAACTACT
CCTGTCAATGCAGTTACTCTAACGTATAACGGAAATAAAAATTCGCTTCCTTTTAATGAA
GACACTACCAACATGATATTACGTATTGATCTGACCACACACAATGTTACTCTAGAAGAA
CCAATAGAAATCAACTGGTCATGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID SI Link Image
Target 3 GenAtlas ID SI Link Image
Target 3 HGNC ID HGNC:10856 Link Image
Target 3 Chromosome Location 3
Target 3 Locus 3q25.2-q26.2
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Chantret I, Lacasa M, Chevalier G, Ruf J, Islam I, Mantei N, Edwards Y, Swallow D, Rousset M: Sequence of the complete cDNA and the 5' structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase. Biochem J. 1992 Aug 1;285 ( Pt 3):915-23. [PubMed Link Image]
  2. Gorvel JP, Ferrero A, Chambraud L, Rigal A, Bonicel J, Maroux S: Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon. Gastroenterology. 1991 Sep;101(3):618-25. [PubMed Link Image]
  3. Green F, Edwards Y, Hauri HP, Povey S, Ho MW, Pinto M, Swallow D: Isolation of a cDNA probe for a human jejunal brush-border hydrolase, sucrase-isomaltase, and assignment of the gene locus to chromosome 3. Gene. 1987;57(1):101-10. [PubMed Link Image]
  4. Ouwendijk J, Moolenaar CE, Peters WJ, Hollenberg CP, Ginsel LA, Fransen JA, Naim HY: Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment. J Clin Invest. 1996 Feb 1;97(3):633-41. [PubMed Link Image]
Target 3 Drug References
  1. Juretic D, Bernik S, Cop L, Hadzija M, Petlevski R, Lukac-Bajalo J: Short-term effect of acarbose on specific intestinal disaccharidase activities and hyperglycaemia in CBA diabetic mice. J Anim Physiol Anim Nutr (Berl). 2003 Aug;87(7-8):263-8. [PubMed Link Image]
  2. Meyer H, Wieczorek H, Zeiske W: K+ transport in the caterpillar intestine epithelium: role of osmolytes for the K+-secretory capacity of the tobacco hornworm midgut. J Comp Physiol [B]. 2004 Oct;174(7):527-39. Epub 2004 Aug 20. [PubMed Link Image]
  3. Karley AJ, Ashford DA, Minto LM, Pritchard J, Douglas AE: The significance of gut sucrase activity for osmoregulation in the pea aphid, Acyrthosiphon pisum. J Insect Physiol. 2005 Dec;51(12):1313-9. Epub 2005 Sep 15. [PubMed Link Image]
  4. Samulitis BK, Goda T, Lee SM, Koldovsky O: Inhibitory mechanism of acarbose and 1-deoxynojirimycin derivatives on carbohydrases in rat small intestine. Drugs Exp Clin Res. 1987;13(8):517-24. [PubMed Link Image]
  5. Newbrun E, Hoover CI, Walker GJ: Inhibition by acarbose, nojirimycin and 1-deoxynojirimycin of glucosyltransferase produced by oral streptococci. Arch Oral Biol. 1983;28(6):531-6. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 4513
Target 4 Name Pancreatic alpha-amylase
Target 4 Synonyms
  1. 1,4-alpha-D- glucan glucanohydrolase
  2. EC 3.2.1.1
  3. PA
  4. Pancreatic alpha-amylase precursor
Target 4 Gene Name AMY2A
Target 4 Protein Sequence >Pancreatic alpha-amylase 
MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPP
NENVAIYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGN
AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLTGL
LDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAG
SKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWG
FVPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWP
RQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNVVDGQP
FTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYCDVISGDKINGNCTGI
KIYVSDDGKAHFSISNSAEDPFIAIHAESKL
Target 4 Number of Residues 519
Target 4 Molecular Weight 57707
Target 4 Theoretical pI 7.05
Target 4 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
amylase activity
alpha-amylase activity
Process
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
Component
Not Available
Target 4 General Function Involved in alpha-amylase activity
Target 4 Specific Function Endohydrolysis of 1,4-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-15
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non Essential
Target 4 GenBank ID Protein Not Available
Target 4 UniProtKB/Swiss-Prot ID P04746 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name AMYP_HUMAN Link Image
Target 4 PDB ID 1B2Y Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Secreted protein
Target 4 Gene Sequence >1536 bp 
ATGAAGTTCTTTCTGTTGCTTTTCACCATTGGGTTCTGCTGGGCTCAGTATTCCCCAAAT
ACACAACAAGGACGGACATCTATTGTTCATCTGTTTGAATGGCGATGGGTTGATATTGCT
CTTGAATGTGAGCGATATTTAGCTCCGAAGGGATTTGGAGGGGTTCAGGTCTCTCCACCA
AATGAAAATGTTGCAATTTACAACCCTTTCAGACCTTGGTGGGAAAGATACCAACCAGTT
AGCTATAAATTATGCACAAGATCTGGAAATGAAGATGAATTTAGAAACATGGTGACTAGA
TGTAACAATGTTGGGGTTCGTATTTATGTGGATGCTGTAATTAATCATATGTGTGGTAAC
GCTGTGAGTGCAGGAACAAGCAGTACCTGTGGAAGTTACTTCAACCCTGGAAGTAGGGAC
TTTCCAGCAGTCCCATATTCTGGATGGGATTTCAATGATGGTAAATGTAAAACTGGAAGT
GGAGATATCGAGAACTACAATGATGCTACTCAGGTCAGAGATTGTCGTCTGACTGGTCTT
CTTGATCTTGCACTGGAGAAGGATTACGTGCGTTCTAAGATTGCCGAATATATGAACCAT
CTCATTGACATTGGTGTTGCAGGGTTCAGACTTGATGCTTCCAAGCACATGTGGCCTGGA
GACATAAAGGCAATTTTGGACAAACTGCATAATCTAAACAGTAACTGGTTCCCTGCAGGA
AGTAAACCTTTCATTTACCAGGAGGTAATTGATCTGGGTGGTGAGCCAATTAAAAGCAGT
GACTACTTTGGTAATGGCCGGGTGACAGAATTCAAGTATGGTGCAAAACTCGGCACAGTT
ATTCGCAAGTGGAATGGAGAGAAGATGTCTTACTTAAAGAACTGGGGAGAAGGTTGGGGT
TTCGTACCTTCTGACAGAGCGCTTGTCTTTGTGGATAACCATGACAATCAACGAGGACAT
GGGGCTGGAGGAGCCTCTATTCTTACCTTCTGGGATGCTAGGCTGTACAAAATGGCAGTT
GGATTTATGCTTGCTCATCCTTACGGATTTACACGAGTAATGTCAAGCTACCGTTGGCCA
AGACAGTTTCAAAATGGAAACGATGTTAATGATTGGGTTGGGCCACCAAATAATAATGGA
GTAATTAAAGAAGTTACTATTAATCCAGACACTACTTGTGGCAATGACTGGGTCTGTGAA
CATCGATGGCGCCAAATAAGGAACATGGTTATTTTCCGCAATGTAGTGGATGGCCAGCCT
TTTACAAATTGGTATGATAATGGGAGCAACCAAGTGGCTTTTGGGAGAGGAAACAGAGGA
TTCATTGTTTTCAACAATGATGACTGGTCATTTTCTTTAACTTTGCAAACTGGTCTTCCT
GCTGGCACATACTGTGATGTCATTTCTGGAGATAAAATTAATGGCAATTGCACAGGCATT
AAAATTTACGTTTCTGATGATGGCAAAGCTCATTTTTCTATTAGTAACTCTGCTGAAGAT
CCATTTATTGCAATTCATGCTGAATCTAAATTGTAA
Target 4 GenBank Gene ID
Target 4 GeneCard ID Not Available
Target 4 GenAtlas ID AMY2A Link Image
Target 4 HGNC ID HGNC:477 Link Image
Target 4 Chromosome Location 1
Target 4 Locus 1p21
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Rydberg EH, Sidhu G, Vo HC, Hewitt J, Cote HC, Wang Y, Numao S, MacGillivray RT, Overall CM, Brayer GD, Withers SG: Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris. Protein Sci. 1999 Mar;8(3):635-43. [PubMed Link Image]
  2. Horii A, Emi M, Tomita N, Nishide T, Ogawa M, Mori T, Matsubara K: Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene. Gene. 1987;60(1):57-64. [PubMed Link Image]
  3. Gumucio DL, Wiebauer K, Caldwell RM, Samuelson LC, Meisler MH: Concerted evolution of human amylase genes. Mol Cell Biol. 1988 Mar;8(3):1197-205. [PubMed Link Image]
  4. Groot PC, Bleeker MJ, Pronk JC, Arwert F, Mager WH, Planta RJ, Eriksson AW, Frants RR: Human pancreatic amylase is encoded by two different genes. Nucleic Acids Res. 1988 May 25;16(10):4724. [PubMed Link Image]
  5. Wise RJ, Karn RC, Larsen SH, Hodes ME, Gardell SJ, Rutter WJ: A complementary DNA sequence that predicts a human pancreatic amylase primary structure consistent with the electrophoretic mobility of the common isozyme, Amy2 A. Mol Biol Med. 1984 Oct;2(5):307-22. [PubMed Link Image]
  6. Nishide T, Emi M, Nakamura Y, Matsubara K: Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected] Gene. 1984 May;28(2):263-70. [PubMed Link Image]
  7. Qian M, Haser R, Buisson G, Duee E, Payan F: The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution. Biochemistry. 1994 May 24;33(20):6284-94. [PubMed Link Image]
  8. Brayer GD, Luo Y, Withers SG: The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes. Protein Sci. 1995 Sep;4(9):1730-42. [PubMed Link Image]
Target 4 Drug References Not Available

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.