| UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.191 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase ( EC 2.3.1.191, UDP-3-O-acyl-glucosamine N-acyltransferase, UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase, acyltransferase LpxD, acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase, firA (gene), lpxD (gene)) is an enzyme with systematic name (3R)-3-hydroxymyristoyl-(acyl-carrier protein):UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine N-acetyltransferase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction
- (3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + holo-[acyl-carrier protein]
The enzyme catalyses a step of lipid A biosynthesis.
References
- ^ Bartling CM, Raetz CR (September 2009). "Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry. 48 (36): 8672–83. doi: 10.1021/bi901025v. PMC 2748855. PMID 19655786.
- ^ Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN (March 2007). "Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis". Proceedings of the National Academy of Sciences of the United States of America. 104 (11): 4321–6. Bibcode: 2007PNAS..104.4321B. doi: 10.1073/pnas.0606356104. PMC 1810333. PMID 17360522.
- ^ Bartling CM, Raetz CR (May 2008). "Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry. 47 (19): 5290–302. doi: 10.1021/bi800240r. PMC 2435086. PMID 18422345.
- ^ Kelly TM, Stachula SA, Raetz CR, Anderson MS (September 1993). "The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis". The Journal of Biological Chemistry. 268 (26): 19866–74. doi: 10.1016/S0021-9258(19)36593-7. PMID 8366125.
- ^ Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP (July 2008). "Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis". Journal of Bacteriology. 190 (13): 4549–58. doi: 10.1128/jb.00234-08. PMC 2446808. PMID 18456814.
External links
- UDP-3-O-(3-hydroxymyristoyl)glucosamine+N-acyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.191 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase ( EC 2.3.1.191, UDP-3-O-acyl-glucosamine N-acyltransferase, UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase, acyltransferase LpxD, acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase, firA (gene), lpxD (gene)) is an enzyme with systematic name (3R)-3-hydroxymyristoyl-(acyl-carrier protein):UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine N-acetyltransferase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction
- (3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + holo-[acyl-carrier protein]
The enzyme catalyses a step of lipid A biosynthesis.
References
- ^ Bartling CM, Raetz CR (September 2009). "Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry. 48 (36): 8672–83. doi: 10.1021/bi901025v. PMC 2748855. PMID 19655786.
- ^ Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN (March 2007). "Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis". Proceedings of the National Academy of Sciences of the United States of America. 104 (11): 4321–6. Bibcode: 2007PNAS..104.4321B. doi: 10.1073/pnas.0606356104. PMC 1810333. PMID 17360522.
- ^ Bartling CM, Raetz CR (May 2008). "Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry. 47 (19): 5290–302. doi: 10.1021/bi800240r. PMC 2435086. PMID 18422345.
- ^ Kelly TM, Stachula SA, Raetz CR, Anderson MS (September 1993). "The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis". The Journal of Biological Chemistry. 268 (26): 19866–74. doi: 10.1016/S0021-9258(19)36593-7. PMID 8366125.
- ^ Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP (July 2008). "Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis". Journal of Bacteriology. 190 (13): 4549–58. doi: 10.1128/jb.00234-08. PMC 2446808. PMID 18456814.
External links
- UDP-3-O-(3-hydroxymyristoyl)glucosamine+N-acyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)