| Identification | |||||||||||||||||||||||||||||||||||||||||||
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| Name | Beta-D-Glucose | ||||||||||||||||||||||||||||||||||||||||||
| Accession Number | DB02379 (EXPT00455, EXPT00685, EXPT01603) | ||||||||||||||||||||||||||||||||||||||||||
| Type | small molecule | ||||||||||||||||||||||||||||||||||||||||||
| Groups | experimental | ||||||||||||||||||||||||||||||||||||||||||
| Description | A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement. [PubChem] |
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| Structure |
Download: MOL | SDF | SMILES | InChI Display: 2D Structure | 3D Structure |
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| Synonyms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Salts | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand names | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand mixtures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Categories |
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| CAS number | 50-99-7 | ||||||||||||||||||||||||||||||||||||||||||
| Weight |
Average: 180.1559 Monoisotopic: 180.063388116 |
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| Chemical Formula | C6H12O6 | ||||||||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=WQZGKKKJIJFFOK-QYESYBIKSA-N | ||||||||||||||||||||||||||||||||||||||||||
| InChI |
InChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6-/m0/s1
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| IUPAC Name |
(2S,3S,4R,5R,6S)-6-(hydroxymethyl)oxane-2,3,4,5-tetrol
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| SMILES |
OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@H]1O
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| Mass Spec | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Taxonomy | |||||||||||||||||||||||||||||||||||||||||||
| Kingdom | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Classes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Substructures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacology | |||||||||||||||||||||||||||||||||||||||||||
| Indication | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacodynamics | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Mechanism of action | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Absorption | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Volume of distribution | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Protein binding | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Metabolism |
Not Available
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| Route of elimination | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Half life | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Clearance | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Toxicity | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Affected organisms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pathways | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacoeconomics | |||||||||||||||||||||||||||||||||||||||||||
| Manufacturers | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Packagers | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Dosage forms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Prices | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Patents | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Properties | |||||||||||||||||||||||||||||||||||||||||||
| State | solid | ||||||||||||||||||||||||||||||||||||||||||
| Experimental Properties |
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| Predicted Properties |
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| Synthesis Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| General Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||
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| ATC Codes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| AHFS Codes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| PDB Entries | |||||||||||||||||||||||||||||||||||||||||||
| FDA label | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| MSDS | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Interactions | |||||||||||||||||||||||||||||||||||||||||||
| Drug Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Food Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Targets |
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1. Glycogen phosphorylase, muscle form Pharmacological action: unknownPhosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties Organism class: humanUniProt ID: P11217 ![]() Gene: PYGM ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Involved in D-xylose catabolism Organism class: bacterialUniProt ID: P15587 ![]() Gene: xylA Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 3. Glucokinase Pharmacological action: unknownCatalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage Organism class: humanUniProt ID: P35557 ![]() Gene: GCK ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
This receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin Organism class: bacterialUniProt ID: P06971 ![]() Gene: fhuA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q9ZB17 ![]() Gene: galM Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q79G13 ![]() Gene: celA1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 7. Glucokinase Pharmacological action: unknownNot highly important in E.coli as glucose is transported into the cell by the pts system already as glucose 6-phosphate Organism class: bacterialUniProt ID: P0A6V8 ![]() Gene: glk Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 8. Amylase Pharmacological action: unknownOrganism class: bacterial UniProt ID: O82839 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 9. Fucose-binding lectin PA-IIL Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9HYN5 ![]() Gene: lecB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 10. BH0236 protein Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9KG76 ![]() Gene: BH0236 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 11. Laminarinase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9WXN1 ![]() Gene: TM_0024 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Endoxylanase that degrades arabinoxylan and glucuronoxylan to xylobiose and xylotriose (in vitro) Organism class: bacterialUniProt ID: Q8GJ44 ![]() Gene: xynA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 13. Cellulase B Pharmacological action: unknownEndohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans Organism class: bacterialUniProt ID: O07653 ![]() Gene: celB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 14. Endoglucanase C Pharmacological action: unknownThe biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes:(1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the nonreducing end of the cellulose polymer chain; (3) Beta-1,4- glucosidases which hydrolyze the cellobiose and other short cello- oligosaccharides to glucose Organism class: bacterialUniProt ID: P14090 ![]() Gene: cenC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 15. Endoglucanase SS precursor Pharmacological action: unknownThis enzyme catalyzes the endohydrolysis of 1,4-beta- glucosidic linkages in cellulose, lichenin and cereal beta-D- glucans Organism class: bacterialUniProt ID: P0C2S5 ![]() Gene: celS Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 16. D-galactose-binding periplasmic protein precursor Pharmacological action: unknownThis protein is involved in the active transport of galactose and glucose. It plays a role in the chemotaxis towards the two sugars by interacting with the trg chemoreceptor Organism class: bacterialUniProt ID: P0AEE5 ![]() Gene: mglB Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 17. Glycosyltransferase 6 domain-containing protein 1 Pharmacological action: unknownOrganism class: human UniProt ID: Q7Z4J2 ![]() Gene: GLT6D1 SNPs: SNPJam Report ![]() References:
18. Glucosamine-6-phosphate isomerase Pharmacological action: unknownD-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3) Organism class: humanUniProt ID: P46926 ![]() Gene: GNPDA1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 19. Beta-amylase Pharmacological action: unknownHydrolysis of 1,4-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains Organism class: bacterialUniProt ID: P36924 ![]() Gene: spoII Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 20. ADP-ribose pyrophosphatase, mitochondrial Pharmacological action: unknownHydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'- phosphate Organism class: humanUniProt ID: Q9BW91 ![]() Gene: NUDT9 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 21. SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 Pharmacological action: unknownOrganism class: human UniProt ID: O60264 ![]() Gene: SMARCA5 SNPs: SNPJam Report ![]() References:
22. Cyclomaltodextrin glucanotransferase Pharmacological action: unknownDegrades starch to alpha-, beta-, and gamma- cyclodextrins, as well as linear sugars Organism class: bacterialUniProt ID: P26827 ![]() Gene: amyA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death Organism class: bacterialUniProt ID: P01552 ![]() Gene: entB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Endohydrolysis of 1,4-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides Organism class: humanUniProt ID: P04745 ![]() Gene: AMY1A ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 25. Maltodextrin phosphorylase Pharmacological action: unknownPhosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties Organism class: bacterialUniProt ID: P00490 ![]() Gene: malP Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
The B-chain is responsible for binding the holotoxin to specific receptors on the target cell surface Organism class: viralUniProt ID: P69178 ![]() Gene: stxB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: O14594 ![]() Gene: NCAN SNPs: SNPJam Report ![]() References:
28. Beta-glucanase Pharmacological action: unknownHydrolysis of 1,4-beta-D-glucosidic linkages in beta-D-glucans containing 1,3- and 1,4-bonds Organism class: bacterialUniProt ID: P23904 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References: 29. Quinoprotein glucose dehydrogenase-B Pharmacological action: unknownOxidizes glucose to gluconolactone Organism class: bacterialUniProt ID: P13650 ![]() Gene: gdhB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 30. Alpha-amylase Pharmacological action: unknownEndohydrolysis of 1,4-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides Organism class: bacterialUniProt ID: P00692 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References: 31. DNA Pharmacological action: unknownDNA is the molecule of heredity, as it is responsible for the genetic propagation of most inherited traits. It is a polynucleic acid that carries genetic information on cell growth, division, and function. DNA consists of two long strands of nucleotides twisted into a double helix and held together by hydrogen bonds. The sequence of nucleotides determines hereditary characteristics. Each strand serves as the template for subsequent DNA replication and as a template for mRNA production, leading to protein synthesis via ribosomes. Gene Sequence: FASTAReferences: 32. Alpha-amylase Pharmacological action: unknownEndohydrolysis of 1,4-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides Organism class: bacterialUniProt ID: P29957 ![]() Gene: amy Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q54331 ![]() Gene: celB Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 34. Chondroitinase B Pharmacological action: unknownCleaves the glycosaminoglycan, dermatan sulfate Organism class: bacterialUniProt ID: Q46079 ![]() Gene: cslB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
L-aspartate = fumarate + NH(3) Organism class: bacterialUniProt ID: P0AC38 ![]() Gene: aspA Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 36. Endoglucanase 5A Pharmacological action: unknownEndohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans Organism class: bacterialUniProt ID: O85465 ![]() Gene: cel5A Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: Q6UWM7 ![]() Gene: LCTL ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
38. Amylosucrase Pharmacological action: unknownCatalyzes the synthesis of alpha-glucan from sucrose. Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis, these two sucrose isomers being obtained by glucosyl transfer onto fructose Organism class: bacterialUniProt ID: Q9ZEU2 ![]() Gene: ams Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Endohydrolysis of 1,4-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides Organism class: humanUniProt ID: P04746 ![]() Gene: AMY2A Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 40. YtnJ Pharmacological action: unknownOrganism class: bacterial UniProt ID: O34974 ![]() Gene: moxC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 41. Endoglucanase E1 Pharmacological action: unknownHas a very high specific activity on carboxymethylcellulose Organism class: bacterialUniProt ID: P54583 ![]() Gene: Acel_0614 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 42. D-galactose-binding periplasmic protein Pharmacological action: unknownThis protein is involved in the active transport of galactose and glucose. It plays a role in the chemotaxis towards the two sugars by interacting with the trg chemoreceptor Organism class: bacterialUniProt ID: P23905 ![]() Gene: mglB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 43. Ecotin Pharmacological action: unknownGeneral inhibitor of pancreatic serine proteases:inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity Organism class: bacterialUniProt ID: P23827 ![]() Gene: eco Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 44. A/G-specific adenine glycosylase Pharmacological action: unknownAdenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past go lesions which are due to the oxidatively damaged form of guanine:7,8-dihydro-8- oxoguanine Organism class: bacterialUniProt ID: P17802 ![]() Gene: mutY Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 45. Keratin-associated protein 5-2 Pharmacological action: unknownOrganism class: human UniProt ID: Q701N4 ![]() Gene: KRTAP5-2 SNPs: SNPJam Report ![]() References:
46. Sialoadhesin Pharmacological action: unknownOrganism class: human UniProt ID: Q9BZZ2 ![]() Gene: SIGLEC1 SNPs: SNPJam Report ![]() References:
47. Neopullulanase Pharmacological action: unknownHydrolyzes pullulan efficiently but only a small amount of starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form maltotriose Organism class: bacterialUniProt ID: P38940 ![]() Gene: nplT Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans Organism class: bacterialUniProt ID: Q60037 ![]() Gene: xynA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 49. Maltoporin Pharmacological action: unknownInvolved in the transport of maltose and maltodextrins. Does not act as a receptor for phages Organism class: bacterialUniProt ID: P26466 ![]() Gene: lamB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 50. Hexokinase Pharmacological action: unknownATP + D-hexose = ADP + D-hexose 6-phosphate Organism class: parasiticUniProt ID: Q26609 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 51. Neopullulanase 1 Pharmacological action: unknownEndohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Also hydrolyzes cyclodextrins Organism class: bacterialUniProt ID: Q60053 ![]() Gene: tvaI Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans Organism class: bacterialUniProt ID: P40943 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 53. Cyclomaltodextrin glucanotransferase Pharmacological action: unknownCyclizes part of a 1,4-alpha-D-glucan chain by formation of a 1,4-alpha-D-glucosidic bond Organism class: bacterialUniProt ID: P43379 ![]() Gene: cgt Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 54. Maltoporin Pharmacological action: unknownInvolved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ("greasy slide") of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda Organism class: bacterialUniProt ID: P02943 ![]() Gene: lamB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 55. Myoglobin Pharmacological action: unknownOrganism class: human UniProt ID: P02144 ![]() Gene: MB SNPs: SNPJam Report ![]() References:
56. Galectin-2 Pharmacological action: unknownThis protein binds beta-galactoside. Its physiological function is not yet known Organism class: humanUniProt ID: P05162 ![]() Gene: LGALS2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
57. Prostaglandin G/H synthase 1 Pharmacological action: unknownMay play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells Organism class: humanUniProt ID: P23219 ![]() Gene: PTGS1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
58. Hexokinase-1 Pharmacological action: unknownATP + D-hexose = ADP + D-hexose 6-phosphate Organism class: humanUniProt ID: P19367 ![]() Gene: HK1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 59. Maltooligosyltrehalose trehalohydrolase, putative Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9RX51 ![]() Gene: treZ Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 60. Alpha-amylase Pharmacological action: unknownEndohydrolysis of 1,4-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides Organism class: bacterialUniProt ID: P00691 ![]() Gene: amyE Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 61. Inorganic polyphosphate/ATP-glucomannokinase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q7WT42 ![]() Gene: ppgmk Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 62. Exoglucanase/xylanase [Includes: Exoglucanase Pharmacological action: unknownThe biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes:(1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the nonreducing end of the cellulose polymer chain; (3) Beta-1,4- glucosidases which hydrolyze the cellobiose and other short cello- oligosaccharides to glucose Organism class: bacterialUniProt ID: P07986 ![]() Gene: cex Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 63. Acetoin(diacetyl) reductase Pharmacological action: unknownCatalyzes the reversible reduction of acetoin to 2,3- butanediol in the presence of NADH Organism class: bacterialUniProt ID: Q48436 ![]() Gene: budC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 64. Cyclomaltodextrin glucanotransferase Pharmacological action: unknownCyclizes part of a 1,4-alpha-D-glucan chain by formation of a 1,4-alpha-D-glucosidic bond Organism class: bacterialUniProt ID: P05618 ![]() Gene: cgt Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 65. Coat protein VP1 Pharmacological action: unknownOrganism class: viral UniProt ID: P49302 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 66. Endoglucanase G Pharmacological action: unknownThe biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes:(1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the nonreducing end of the cellulose polymer chain; (3) Beta-1,4- glucosidases which hydrolyze the cellobiose and other short cello- oligosaccharides to glucose Organism class: bacterialUniProt ID: P37700 ![]() Gene: celCCG Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 67. Hydrolase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q7SI98 ![]() Protein Sequence: FASTA 68. Galectin-7 Pharmacological action: unknownCould be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. Pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release Organism class: humanUniProt ID: P47929 ![]() Gene: LGALS7 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 69. Cholera enterotoxin subunit B Pharmacological action: unknownThe B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself Organism class: bacterialUniProt ID: P01556 ![]() Gene: ctxB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 70. Keratin-associated protein 5-3 Pharmacological action: unknownOrganism class: human UniProt ID: Q6L8H2 ![]() Gene: KRTAP5-3 SNPs: SNPJam Report ![]() References:
71. Dimethyl sulfoxide reductase Pharmacological action: unknownTerminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds Organism class: bacterialUniProt ID: Q57366 ![]() Gene: dmsA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
This enzyme catalyzes the endohydrolysis of 1,4-beta- glucosidic linkages in cellulose, lichenin and cereal beta-D- glucans Organism class: bacterialUniProt ID: P23340 ![]() Gene: celC307 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 73. Alpha-amylase 2B Pharmacological action: unknownOrganism class: human UniProt ID: P19961 ![]() Gene: AMY2B SNPs: SNPJam Report ![]() References:
74. Cyclomaltodextrin glucanotransferase Pharmacological action: unknownCyclizes part of a 1,4-alpha-D-glucan chain by formation of a 1,4-alpha-D-glucosidic bond Organism class: bacterialUniProt ID: P30920 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References: 75. Endo-1,4-beta glucanase EngF Pharmacological action: unknownEndohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans Organism class: bacterialUniProt ID: P94622 ![]() Gene: engF Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 76. Neopullulanase 2 Pharmacological action: unknownHydrolyzes pullulan efficiently but only a small amount of starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form maltotriose Organism class: bacterialUniProt ID: Q08751 ![]() Gene: tvaII Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans Organism class: bacterialUniProt ID: P26221 ![]() Gene: celD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 78. Botulinum neurotoxin type B Pharmacological action: unknownBotulinum toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that cleaves the '76-Gln-|-Phe-77' bond of synaptobrevin-2 Organism class: bacterialUniProt ID: P10844 ![]() Gene: botB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 79. Slt-IIvB Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q47644 ![]() Gene: stxB2e Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 80. Tetanus toxin Pharmacological action: unknownTetanus toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '76-Gln-|-Phe- 77' bond of synaptobrevin-2 Organism class: bacterialUniProt ID: P04958 ![]() Gene: tetX Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 81. Xylose isomerase Pharmacological action: unknownInvolved in D-xylose catabolism Organism class: bacterialUniProt ID: P24300 ![]() Gene: xylA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 82. Glucan 1,4-alpha-maltohexaosidase Pharmacological action: unknownHydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends Organism class: bacterialUniProt ID: P19571 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References: 83. Glucan 1,4-alpha-maltotetraohydrolase Pharmacological action: unknownHydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends Organism class: bacterialUniProt ID: P13507 ![]() Gene: amyP Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 84. Endoglucanase F Pharmacological action: unknownProbable endoglucanase involved in the degradation of cellulose or related beta-glucans Organism class: bacterialUniProt ID: P37698 ![]() Gene: celCCF Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 85. Glucose--fructose oxidoreductase Pharmacological action: unknownD-glucose + D-fructose = D-gluconolactone + D- glucitol Organism class: bacterialUniProt ID: Q07982 ![]() Gene: gfo Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Non-covalently bound to the neck of the phage capsid and essential for phage adsorption to the bacterial host. It displays endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O- glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide Organism class: viralUniProt ID: P12528 ![]() Gene: 9 Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 87. Glycogen phosphorylase, liver form Pharmacological action: unknownPhosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties Organism class: humanUniProt ID: P06737 ![]() Gene: PYGL ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 88. Pulmonary surfactant-associated protein D Pharmacological action: unknownContributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties Organism class: humanUniProt ID: P35247 ![]() Gene: SFTPD ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 89. Interferon beta Pharmacological action: unknownHas antiviral, antibacterial and anticancer activities Organism class: humanUniProt ID: P01574 ![]() Gene: IFNB1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 90. Maltose-binding periplasmic protein precursor Pharmacological action: unknownInvolved in the high-affinity maltose membrane transport system malEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides Organism class: bacterialUniProt ID: P0AEX9 ![]() Gene: malE Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 91. Enoyl-[acyl-carrier-protein] reductase [NADH] Pharmacological action: unknownAcyl-[acyl-carrier-protein] + NAD(+) = trans- 2,3-dehydroacyl-[acyl-carrier-protein] + NADH Organism class: bacterialUniProt ID: P0AEK4 ![]() Gene: fabI Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 92. Endoglucanase A Pharmacological action: unknownThis enzyme catalyzes the endohydrolysis of 1,4-beta- glucosidic linkages in cellulose, lichenin and cereal beta-D- glucans Organism class: bacterialUniProt ID: P0C2S2 ![]() Gene: celA Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: |
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Endohydrolysis of 1,4-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides UniProt ID: P04746![]() Gene: AMY2A Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() |
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