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UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
| Field | Value |
|---|---|
| Name | UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase |
| EC_number | 2.3.1.191 |
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (, 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. This enzyme catalyses the following chemical reaction
: (3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine \rightleftharpoons 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
References
- (September 2009). "Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry.
- (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.
- (May 2008). "Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis". Biochemistry.
- (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.
- (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.
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