UDP-N-acetylglucosamine 1-carboxyvinyltransferase explained

UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Ec Number:	2.5.1.7
Cas Number:	9023-27-2
Go Code:	0008760
Width:	270

In enzymology, an UDP-N-acetylglucosamine 1-carboxyvinyltransferase is an enzyme^[1] that catalyzes the first committed step in peptidoglycan biosynthesis of bacteria:

phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine

\rightleftharpoons 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

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes,,,,,,,,, and .

Literature

• 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 . 5770–8 . 5699062 . 21 .
• Zemell RI, Anwar RA . 1975 . Pyruvate-uridine diphospho-N-acetylglucosamine transferase Purification to homogeneity and feedback inhibition . J. Biol. Chem. . 250 . 3185–92 . 1123336 . 8 .
• van Heijenoort J . 2001 . Recent advances in the formation of the bacterial peptidoglycan monomer unit . Nat. Prod. Rep. . 18 . 503–19 . 11699883 . 10.1039/a804532a . 5 .

Notes and References

1. Web site: Enolpyruvate transferase, EPT family . 2008-11-23.
2. Brown ED, Vivas EI, Walsh CT, Kolter R . MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli . J. Bacteriol. . 177 . 14 . 4194–7 . July 1995 . 10.1128/jb.177.14.4194-4197.1995 . 7608103 . 177162 .
3. Book: King, Michael B. . Lange Q & A . McGraw-Hill, Medical Pub. Division . New York . 2005 . 298 . 0-07-144578-1 . registration .
4. 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.