DrugBank: N-Acetyl-D-glucosamine (DB00141)

targets (8)

Identification

Name

N-Acetyl-D-glucosamine

Accession Number

DB00141 (NUTR00040)

Type

small molecule

Groups

approved, nutraceutical

Description

The N-acetyl derivative of glucosamine. [PubChem]

Structure

Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure

Synonyms

2-Acetamido-2-deoxy-D-glucose
GlcNAc
Glucosamine Complex
N-Acetylchitosamine

Synonyms

2-Acetamido-2-deoxy-D-glucose
GlcNAc
Glucosamine Complex
N-Acetylchitosamine

Salts

Not Available

Brand names

Name	Company
Aflexa
GS-500
Maxi GS
Natures Blend Glucosamine

Brand mixtures

Not Available

Categories

Dietary supplement
Micronutrient

CAS number

7512-17-6

Weight

Average: 221.2078
Monoisotopic: 221.089937217

Chemical Formula

C₈H₁₅NO₆

InChI Key

InChIKey=MBLBDJOUHNCFQT-LXGUWJNJSA-N

InChI

InChI=1S/C8H15NO6/c1-4(12)9-5(2-10)7(14)8(15)6(13)3-11/h2,5-8,11,13-15H,3H2,1H3,(H,9,12)/t5-,6+,7+,8+/m0/s1

Plain Text

IUPAC Name

N-[(2R,3R,4S,5R)-3,4,5,6-tetrahydroxy-1-oxohexan-2-yl]acetamide

SMILES

[H]C(=O)[C@H](NC(C)=O)[C@@H](O)[C@H](O)[C@H](O)CO

Plain Text

Mass Spec

Not Available

Taxonomy

Kingdom

Not Available

Classes

Not Available

Substructures

Not Available

Pharmacology

Indication

For the treatment and prevention of osteoarthritis, by itself or in combination with chondroitin sulfate.

Pharmacodynamics

Not Available

Mechanism of action

The mechanism of action in relieving arthritic pain and in repair of cartilage is a matter of speculation. Biochemically, glucosamine is involved in glycoprotein metabolism. Glycoproteins, known as proteoglycans, form the ground substance in the extra-cellular matrix of connective tissue. Proteoglycans are polyanionic substances of high-molecular weight and contain many different types of heteropolysaccharide side-chains covalently linked to a polypeptide-chain backbone. These polysaccharides make up to 95% of the proteoglycan structure. In fact, chemically, proteoglycans resemble polysaccharides more than they do proteins. The polysaccharide groups in proteoglycans are called glycosaminoglycans (GAGs). GAGs include hyaluronic acid, chondroitin sulfate, dermatan sulfate, keratan sulfate, heparin and heparan sulfate. All of the GAGs contain derivatives of glucosamine or galactosamine. Glucosamine derivatives are found in hyaluronic acid, keratan sulfate and heparan sulfate. Chondroitin sulfate contains derivatives of galactosamine. The glucosamine-containing glycosaminoglycan hyaluronic acid is vital for the function of articular cartilage. GAG chains are fundamental components of aggrecan found in articular cartilage. Aggrecan confers upon articular cartilage shock-absorbing properties. It does this by providing cartilage with a swelling pressure that is restrained by the tensile forces of collagen fibers. This balance confers upon articular cartilage the deformable resilience vital to its function. In the early stages of degenerative joint disease, aggrecan biosynthesis is increased. However, in later stages, aggrecan synthesis is decreased, leading eventually to the loss of cartilage resiliency and to most of the symptoms that accompany osteoarthritis. During the progression of osteoarthritis, exogenous glucosamine may have a beneficial role. It is known that, in vitro, chondrocytes do synthesize more aggregan when the culture medium is supplemented with glucosamine. N-acetylglucosamine is found to be less effective in these in vitro studies. Glucosamine has also been found to have antioxidant activity and to be beneficial in animal models of experimental arthritis. The counter anion of the glucosamine salt (i.e. chloride or sulfate) is unlikely to play any role in the action or pharmacokinetics of glucosamine. Further, the sulfate in glucosamine sulfate supplements should not be confused with the glucosamine sulfate found in such GAGs as keratan sulfate and heparan sulfate. In the case of the supplement, sulfate is the anion of the salt. In the case of the above GAGs, sulfate is present as an ester. Also, there is no glucosamine sulfate in chondroitin sulfate (source: PDRhealth).

Absorption

Approximately 90% of orally administered glucosamine (salt form) gets absorbed from the small intestine.

Volume of distribution

Not Available

Protein binding

Not Available

Metabolism

A significant fraction of ingested glucosamine is catabolized by first-pass metabolism in the liver.

Route of elimination

Not Available

Half life

Not Available

Clearance

Not Available

Toxicity

Mouse, intravenous LD₅₀ is 4170 mg/kg. Side effects that have been reported are mainly mild gastrointestinal complaints such as heartburn, epigastric distress and diarrhea. No allergic reactions have been reported including sulfa-allergic reactions to glucosamine sulfate.

Affected organisms

Humans and other mammals

Pathways

Not Available

Pharmacoeconomics

Manufacturers

Not Available

Packagers

Gallipot

Dosage forms

Not Available

Prices

Unit description	Cost	Unit
Acetyl-d-glucosamine powder	3.75 USD	g

Patents

Not Available

Properties

State

solid

Melting point

205 oC

Experimental Properties

Property	Value	Source
logP	-2.1	PhysProp

Predicted Properties

Property	Value	Source
water solubility	1.48e+02 g/l	ALOGPS
logP	-2.1	ALOGPS
logP	-3.9	ChemAxon Molconvert
logS	-0.18	ALOGPS
pKa	12.8	ChemAxon Molconvert
hydrogen acceptor count	6	ChemAxon Molconvert
hydrogen donor count	5	ChemAxon Molconvert
polar surface area	127.09	ChemAxon Molconvert
rotatable bond count	6	ChemAxon Molconvert
refractivity	48.45	ChemAxon Molconvert
polarizability	20.49	ChemAxon Molconvert

References

Synthesis Reference

Not Available

General Reference

Not Available

External Links

Resource	Link
KEGG Compound	C00140
BindingDB	50223349
ChEBI	17411
ChEMBL	17411
Therapeutic Targets Database	DAP000872
HET	NAG
PDRhealth	http://www.pdrhealth.com/drug_info/nmdrugprofiles/nutsupdrugs/glu_0122.shtml

ATC Codes

M01AX05

AHFS Codes

Not Available

PDB Entries

1XHG

FDA label

Not Available

MSDS

show (73.5 KB)

Interactions

Drug Interactions

Not Available

Food Interactions

Not Available

Targets
1. Beta-1,4-galactosyltransferase 3 Pharmacological action: unknown Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids Organism class: human UniProt ID: O60512 Gene: B4GALT3 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed 2. Beta-1,4-galactosyltransferase 4 Pharmacological action: unknown Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids Organism class: human UniProt ID: O60513 Gene: B4GALT4 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed Bulter T, Schumacher T, Namdjou DJ, Gutierrez Gallego R, Clausen H, Elling L: Chemoenzymatic synthesis of biotinylated nucleotide sugars as substrates for glycosyltransferases. Chembiochem. 2001 Dec 3;2(12):884-94. Pubmed 3. Beta-1,4-galactosyltransferase 2 Pharmacological action: unknown Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose Organism class: human UniProt ID: O60909 Gene: B4GALT2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed 4. N-acetylglucosamine kinase Pharmacological action: unknown Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Also has ManNAc kinase activity Organism class: human UniProt ID: Q9UJ70 Gene: NAGK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Weihofen WA, Berger M, Chen H, Saenger W, Hinderlich S: Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation. J Mol Biol. 2006 Dec 1;364(3):388-99. Epub 2006 Sep 3. Pubmed Uehara T, Park JT: The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling. J Bacteriol. 2004 Nov;186(21):7273-9. Pubmed An HJ, Kim DS, Park YK, Kim SK, Choi YP, Kang S, Ding B, Cho NH: Comparative proteomics of ovarian epithelial tumors. J Proteome Res. 2006 May;5(5):1082-90. Pubmed Yang C, Rodionov DA, Li X, Laikova ON, Gelfand MS, Zagnitko OP, Romine MF, Obraztsova AY, Nealson KH, Osterman AL: Comparative genomics and experimental characterization of N-acetylglucosamine utilization pathway of Shewanella oneidensis. J Biol Chem. 2006 Oct 6;281(40):29872-85. Epub 2006 Jul 20. Pubmed Nishimasu H, Fushinobu S, Shoun H, Wakagi T: Crystal structures of an ATP-dependent hexokinase with broad substrate specificity from the hyperthermophilic archaeon Sulfolobus tokodaii. J Biol Chem. 2007 Mar 30;282(13):9923-31. Epub 2007 Jan 17. Pubmed 5. N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase Pharmacological action: unknown Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P- mannose moieties, which are formed in the first step Organism class: human UniProt ID: Q9UK23 Gene: NAGPA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed Mullis KG, Huynh M, Kornfeld RH: Purification and kinetic parameters of bovine liver N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. J Biol Chem. 1994 Jan 21;269(3):1718-26. Pubmed Chavez CA, Bohnsack RN, Kudo M, Gotschall RR, Canfield WM, Dahms NM: Domain 5 of the Cation-Independent Mannose 6-Phosphate Receptor Preferentially Binds Phosphodiesters (Mannose 6-Phosphate N-Acetylglucosamine Ester). Biochemistry. 2007 Oct 10;. Pubmed Kornfeld R, Bao M, Brewer K, Noll C, Canfield WM: Purification and multimeric structure of bovine N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. J Biol Chem. 1998 Sep 4;273(36):23203-10. Pubmed 6. Alpha-N-acetylglucosaminidase Pharmacological action: unknown Actions: activator Involved in the degradation of heparan sulfate Organism class: human UniProt ID: P54802 Gene: NAGLU Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Spiro RG: Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation. Cell Mol Life Sci. 2004 May;61(9):1025-41. Pubmed Nogawa M, Takahashi H, Kashiwagi A, Ohshima K, Okada H, Morikawa Y: Purification and Characterization of Exo-beta-d-Glucosaminidase from a Cellulolytic Fungus, Trichoderma reesei PC-3-7. Appl Environ Microbiol. 1998 Mar;64(3):890-895. Pubmed Vishu Kumar AB, Varadaraj MC, Gowda LR, Tharanathan RN: Characterization of chito-oligosaccharides prepared by chitosanolysis with the aid of papain and Pronase, and their bactericidal action against Bacillus cereus and Escherichia coli. Biochem J. 2005 Oct 15;391(Pt 2):167-75. Pubmed Zou L, Yang S, Hu S, Chaudry IH, Marchase RB, Chatham JC: The protective effects of PUGNAc on cardiac function after trauma-hemorrhage are mediated via increased protein O-GlcNAc levels. Shock. 2007 Apr;27(4):402-8. Pubmed Shirazi F, Kulkarni M, Deshpande MV: A rapid and sensitive method for screening of chitinase inhibitors using Ostazin Brilliant Red labelled chitin as a substrate for chitinase assay. Lett Appl Microbiol. 2007 Jun;44(6):660-5. Pubmed Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. Pubmed 7. N-acylglucosamine 2-epimerase Pharmacological action: unknown Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity Organism class: human UniProt ID: P51606 Gene: RENBP Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Lee YC, Wu HM, Chang YN, Wang WC, Hsu WH: The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion. J Mol Biol. 2007 Mar 30;367(3):895-908. Epub 2006 Nov 6. Pubmed Lee YC, Chien HC, Hsu WH: Production of N-acetyl-D-neuraminic acid by recombinant whole cells expressing Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase and Escherichia coli N-acetyl-D-neuraminic acid lyase. J Biotechnol. 2007 May 1;129(3):453-60. Epub 2007 Feb 9. Pubmed Takahashi S, Ogasawara H, Hiwatashi K, Hata K, Hori K, Koizumi Y, Sugiyama T: Amino acid residues conferring the nucleotide binding properties of N-acetyl-D-glucosamine 2-epimerase (renin binding protein). Biomed Res. 2005 Jun;26(3):117-21. Pubmed Ferrero MA, Martinez-Blanco H, Lopez-Velasco FF, Ezquerro-Saenz C, Navasa N, Lozano S, Rodriguez-Aparicio LB: Purification and characterization of GlcNAc-6-P 2-epimerase from Escherichia coli K92. Acta Biochim Pol. 2007;54(2):387-99. Epub 2007 Jun 14. Pubmed 8. Beta-1,4-galactosyltransferase 1 Pharmacological action: unknown The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix Organism class: human UniProt ID: P15291 Gene: B4GALT1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Ramakrishnan B, Boeggeman E, Qasba PK: Mutation of arginine 228 to lysine enhances the glucosyltransferase activity of bovine beta-1,4-galactosyltransferase I. Biochemistry. 2005 Mar 8;44(9):3202-10. Pubmed Ramasamy V, Ramakrishnan B, Boeggeman E, Ratner DM, Seeberger PH, Qasba PK: Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety. J Mol Biol. 2005 Oct 14;353(1):53-67. Pubmed Boeggeman E, Ramakrishnan B, Kilgore C, Khidekel N, Hsieh-Wilson LC, Simpson JT, Qasba PK: Direct identification of nonreducing GlcNAc residues on N-glycans of glycoproteins using a novel chemoenzymatic method. Bioconjug Chem. 2007 May-Jun;18(3):806-14. Epub 2007 Mar 20. Pubmed Hidalgo A, Burgos V, Viola H, Medina J, Argibay P: Differential expression of glycans in the hippocampus of rats trained on an inhibitory learning paradigm. Neuropathology. 2006 Dec;26(6):501-7. Pubmed Ramakrishnan B, Boeggeman E, Qasba PK: Effect of the Met344His mutation on the conformational dynamics of bovine beta-1,4-galactosyltransferase: crystal structure of the Met344His mutant in complex with chitobiose. Biochemistry. 2004 Oct 5;43(39):12513-22. Pubmed

Targets

1. Beta-1,4-galactosyltransferase 3

Pharmacological action: unknown

Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids

Organism class: human
UniProt ID: O60512 Link_out

Gene: B4GALT3 Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed

2. Beta-1,4-galactosyltransferase 4

Pharmacological action: unknown

Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids

Organism class: human
UniProt ID: O60513 Link_out

Gene: B4GALT4 Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed
Bulter T, Schumacher T, Namdjou DJ, Gutierrez Gallego R, Clausen H, Elling L: Chemoenzymatic synthesis of biotinylated nucleotide sugars as substrates for glycosyltransferases. Chembiochem. 2001 Dec 3;2(12):884-94. Pubmed

3. Beta-1,4-galactosyltransferase 2

Pharmacological action: unknown

Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose

Organism class: human
UniProt ID: O60909 Link_out

Gene: B4GALT2 Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed

4. N-acetylglucosamine kinase

Pharmacological action: unknown

Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Also has ManNAc kinase activity

Organism class: human
UniProt ID: Q9UJ70 Link_out

Gene: NAGK Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Weihofen WA, Berger M, Chen H, Saenger W, Hinderlich S: Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation. J Mol Biol. 2006 Dec 1;364(3):388-99. Epub 2006 Sep 3. Pubmed
Uehara T, Park JT: The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling. J Bacteriol. 2004 Nov;186(21):7273-9. Pubmed
An HJ, Kim DS, Park YK, Kim SK, Choi YP, Kang S, Ding B, Cho NH: Comparative proteomics of ovarian epithelial tumors. J Proteome Res. 2006 May;5(5):1082-90. Pubmed
Yang C, Rodionov DA, Li X, Laikova ON, Gelfand MS, Zagnitko OP, Romine MF, Obraztsova AY, Nealson KH, Osterman AL: Comparative genomics and experimental characterization of N-acetylglucosamine utilization pathway of Shewanella oneidensis. J Biol Chem. 2006 Oct 6;281(40):29872-85. Epub 2006 Jul 20. Pubmed
Nishimasu H, Fushinobu S, Shoun H, Wakagi T: Crystal structures of an ATP-dependent hexokinase with broad substrate specificity from the hyperthermophilic archaeon Sulfolobus tokodaii. J Biol Chem. 2007 Mar 30;282(13):9923-31. Epub 2007 Jan 17. Pubmed

5. N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase

Pharmacological action: unknown

Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P- mannose moieties, which are formed in the first step

Organism class: human
UniProt ID: Q9UK23 Link_out

Gene: NAGPA Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed
Mullis KG, Huynh M, Kornfeld RH: Purification and kinetic parameters of bovine liver N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. J Biol Chem. 1994 Jan 21;269(3):1718-26. Pubmed
Chavez CA, Bohnsack RN, Kudo M, Gotschall RR, Canfield WM, Dahms NM: Domain 5 of the Cation-Independent Mannose 6-Phosphate Receptor Preferentially Binds Phosphodiesters (Mannose 6-Phosphate N-Acetylglucosamine Ester). Biochemistry. 2007 Oct 10;. Pubmed
Kornfeld R, Bao M, Brewer K, Noll C, Canfield WM: Purification and multimeric structure of bovine N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. J Biol Chem. 1998 Sep 4;273(36):23203-10. Pubmed

6. Alpha-N-acetylglucosaminidase

Pharmacological action: unknown
Actions: activator

Involved in the degradation of heparan sulfate

Organism class: human
UniProt ID: P54802 Link_out

Gene: NAGLU Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Spiro RG: Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation. Cell Mol Life Sci. 2004 May;61(9):1025-41. Pubmed
Nogawa M, Takahashi H, Kashiwagi A, Ohshima K, Okada H, Morikawa Y: Purification and Characterization of Exo-beta-d-Glucosaminidase from a Cellulolytic Fungus, Trichoderma reesei PC-3-7. Appl Environ Microbiol. 1998 Mar;64(3):890-895. Pubmed
Vishu Kumar AB, Varadaraj MC, Gowda LR, Tharanathan RN: Characterization of chito-oligosaccharides prepared by chitosanolysis with the aid of papain and Pronase, and their bactericidal action against Bacillus cereus and Escherichia coli. Biochem J. 2005 Oct 15;391(Pt 2):167-75. Pubmed
Zou L, Yang S, Hu S, Chaudry IH, Marchase RB, Chatham JC: The protective effects of PUGNAc on cardiac function after trauma-hemorrhage are mediated via increased protein O-GlcNAc levels. Shock. 2007 Apr;27(4):402-8. Pubmed
Shirazi F, Kulkarni M, Deshpande MV: A rapid and sensitive method for screening of chitinase inhibitors using Ostazin Brilliant Red labelled chitin as a substrate for chitinase assay. Lett Appl Microbiol. 2007 Jun;44(6):660-5. Pubmed
Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. Pubmed

7. N-acylglucosamine 2-epimerase

Pharmacological action: unknown

Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity

Organism class: human
UniProt ID: P51606 Link_out

Gene: RENBP Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Lee YC, Wu HM, Chang YN, Wang WC, Hsu WH: The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion. J Mol Biol. 2007 Mar 30;367(3):895-908. Epub 2006 Nov 6. Pubmed
Lee YC, Chien HC, Hsu WH: Production of N-acetyl-D-neuraminic acid by recombinant whole cells expressing Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase and Escherichia coli N-acetyl-D-neuraminic acid lyase. J Biotechnol. 2007 May 1;129(3):453-60. Epub 2007 Feb 9. Pubmed
Takahashi S, Ogasawara H, Hiwatashi K, Hata K, Hori K, Koizumi Y, Sugiyama T: Amino acid residues conferring the nucleotide binding properties of N-acetyl-D-glucosamine 2-epimerase (renin binding protein). Biomed Res. 2005 Jun;26(3):117-21. Pubmed
Ferrero MA, Martinez-Blanco H, Lopez-Velasco FF, Ezquerro-Saenz C, Navasa N, Lozano S, Rodriguez-Aparicio LB: Purification and characterization of GlcNAc-6-P 2-epimerase from Escherichia coli K92. Acta Biochim Pol. 2007;54(2):387-99. Epub 2007 Jun 14. Pubmed

8. Beta-1,4-galactosyltransferase 1

Pharmacological action: unknown

The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix

Organism class: human
UniProt ID: P15291 Link_out

Gene: B4GALT1 Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Ramakrishnan B, Boeggeman E, Qasba PK: Mutation of arginine 228 to lysine enhances the glucosyltransferase activity of bovine beta-1,4-galactosyltransferase I. Biochemistry. 2005 Mar 8;44(9):3202-10. Pubmed
Ramasamy V, Ramakrishnan B, Boeggeman E, Ratner DM, Seeberger PH, Qasba PK: Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety. J Mol Biol. 2005 Oct 14;353(1):53-67. Pubmed
Boeggeman E, Ramakrishnan B, Kilgore C, Khidekel N, Hsieh-Wilson LC, Simpson JT, Qasba PK: Direct identification of nonreducing GlcNAc residues on N-glycans of glycoproteins using a novel chemoenzymatic method. Bioconjug Chem. 2007 May-Jun;18(3):806-14. Epub 2007 Mar 20. Pubmed
Hidalgo A, Burgos V, Viola H, Medina J, Argibay P: Differential expression of glycans in the hippocampus of rats trained on an inhibitory learning paradigm. Neuropathology. 2006 Dec;26(6):501-7. Pubmed
Ramakrishnan B, Boeggeman E, Qasba PK: Effect of the Met344His mutation on the conformational dynamics of bovine beta-1,4-galactosyltransferase: crystal structure of the Met344His mutant in complex with chitobiose. Biochemistry. 2004 Oct 5;43(39):12513-22. Pubmed

Comments

Drug created on June 13, 2005 07:24 / Updated on April 19, 2012 13:03