UDP-N-acetylglucosamine 1-carboxyvinyltransferase
| UDP-N-acetylglucosamine 1-carboxyvinyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 UDP-N-acetylglucosamine 1-carboxyvinyltransferase tetramer, Enterobacter cloacae | |||||||||
| Identifiers | |||||||||
| EC no. | 2.5.1.7 | ||||||||
| CAS no. | 9023-27-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an UDP-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) is an enzyme[1] that catalyzes the first committed step in peptidoglycan biosynthesis of bacteria:
- phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
Thus, the two substrates of this enzyme are phosphoenolpyruvate and UDP-N-acetyl-D-glucosamine, whereas its two products are phosphate and UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine. The pyruvate moiety provides the linker that bridges the glycan and peptide portion of peptidoglycan.[2]
The enzyme is inhibited by the antibiotic fosfomycin, which covalently modifies an active site cysteine residue.[3]
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine 1-carboxyvinyltransferase.[4] This enzyme participates in amino sugars metabolism and glycan biosynthesis.
Structural studies[edit]
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1A2N, 1DLG, 1EJC, 1EJD, 1EYN, 1NAW, 1Q3G, 1RYW, 1UAE, and 1YBG.
References[edit]
- ^ "Enolpyruvate transferase, EPT family". Retrieved 2008-11-23.
- ^ Brown ED, Vivas EI, Walsh CT, Kolter R (July 1995). "MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli". J. Bacteriol. 177 (14): 4194–7. doi:10.1128/jb.177.14.4194-4197.1995. PMC 177162. PMID 7608103.
- ^ King, Michael B. (2005). Lange Q & A. New York: McGraw-Hill, Medical Pub. Division. pp. 298. ISBN 0-07-144578-1.
- ^ Other names in common use include MurA transferase, UDP-N-acetylglucosamine 1-carboxyvinyl-transferase, UDP-N-acetylglucosamine enoylpyruvyltransferase, enoylpyruvate transferase, phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase, phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase, phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase, phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2-deoxyglucose 3-enolpyruvyltransferase, phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase, pyruvate-UDP-acetylglucosamine transferase, pyruvate-uridine diphospho-N-acetylglucosamine transferase, pyruvate-uridine diphospho-N-acetyl-glucosamine transferase, and pyruvic-uridine diphospho-N-acetylglucosaminyltransferase.
Literature[edit]
- Gunetileke KG, Anwar RA (1968). "Biosynthesis of uridine diphospho-N-acetylmuramic acid. II Purification and properties of pyruvate-uridine diphospho-N-acetylglucosamine transferase and characterization of uridine diphospho-N-acetylenopyruvylglucosamine". J. Biol. Chem. 243 (21): 5770–8. PMID 5699062.
- Zemell RI, Anwar RA (1975). "Pyruvate-uridine diphospho-N-acetylglucosamine transferase Purification to homogeneity and feedback inhibition". J. Biol. Chem. 250 (8): 3185–92. PMID 1123336.
- van Heijenoort J (2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Nat. Prod. Rep. 18 (5): 503–19. doi:10.1039/a804532a. PMID 11699883.
