UDP-3-O-acyl-N-acetylglucosamine deacetylase

UDP-3-O-acyl-N-acetylglucosamine deacetylase (EC 3.5.1.108, LpxC protein, LpxC enzyme, LpxC deacetylase, deacetylase LpxC, UDP-3-O-acyl-GlcNAc deacetylase, UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, UDP-(3-O-acyl)-N-acetylglucosamine deacetylase, UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase) is an enzyme with systematic name UDP-3-O-((3R)-3-hydroxymyristoyl)-N-acetylglucosamine amidohydrolase.^[1]^[2]^[3]^[4]^[5]^[6] This enzyme catalyses the following chemical reaction

UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine + H₂O

\rightleftharpoons

UDP-3-O-[(3R)-3-hydroxymyristoyl]-D-glucosamine + acetate

This zinc protein participates in biosynthesis of lipid A.

References

↑ Hernick, M.; Gennadios, H.A.; Whittington, D.A.; Rusche, K.M.; Christianson, D.W.; Fierke, C.A. (2005). "UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism". J. Biol. Chem. 280 (17): 16969–16978. doi:10.1074/jbc.M413560200. PMID 15705580.
↑ Jackman, J.E.; Raetz, C.R.; Fierke, C.A. (1999). "UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme". Biochemistry. 38 (6): 1902–1911. doi:10.1021/bi982339s. PMID 10026271.
↑ Hyland, S.A.; Eveland, S.S.; Anderson, M.S. (1997). "Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway". J. Bacteriol. 179 (6): 2029–2037. PMID 9068651.
↑ Wang, W.; Maniar, M.; Jain, R.; Jacobs, J.; Trias, J.; Yuan, Z. (2001). "A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase". Anal. Biochem. 290 (2): 338–346. doi:10.1006/abio.2000.4973. PMID 11237337.
↑ Whittington, D.A.; Rusche, K.M.; Shin, H.; Fierke, C.A.; Christianson, D.W. (2003). "Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis". Proc. Natl. Acad. Sci. USA. 100: 8146–8150. doi:10.1073/pnas.1432990100. PMC 166197. PMID 12819349.
↑ Mochalkin, I.; Knafels, J.D.; Lightle, S. (2008). "Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor". Protein Sci. 17 (3): 450–457. doi:10.1110/ps.073324108. PMID 18287278.

External links

UDP-3-O-acyl-N-acetylglucosamine deacetylase at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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