PMID:8366125: Difference between revisions
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status | !|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status | ||
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LpxD | |||
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[[Category:GO:0009245_!_lipid_A_biosynthetic_process]][http://gowiki.tamu.edu/wiki/index.php/Category:GO:0009245_!_lipid_A_biosynthetic_process GO:0009245] | |||
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lipid A biosynthetic process | |||
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IMP: Inferred from Mutant Phenotype | |||
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P | |||
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A ts mutantion in the lpxD gene (firA200) is shown to decrease the rate of lipid A synthesis at the restrictive temperature (Figs. 2 and 3). | |||
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complete | |||
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LpxD | |||
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[[Category:GO:0016410_!_N-acyltransferase_activity]][http://gowiki.tamu.edu/wiki/index.php/Category:GO:0016410_!_N-acyltransferase_activity GO:0016410] | |||
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N-acyltransferase activity | |||
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IDA: Inferred from Direct Assay | |||
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F | |||
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The enzyme displays absolute specificity for the 3-OH group of R-3-hydroxymyristoyl-ACP (Fig. 9). | |||
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complete | |||
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Revision as of 15:48, 16 October 2008
Kelly, TM, Stachula, SA, Raetz, CR and Anderson, MS (1993) The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis.J. Biol. Chem. 268:19866-74
| Abstract | The possibility that the firA gene of Escherichia coli (Dicker, I. B., and Seetharam, S. (1991) Mol. Microbiol. 6, 817-823) might function in lipid A biosynthesis was examined based on its homology to the lpxA gene, which encodes UDP-N-acetylglucosamine O-acyl-transferase, the first enzyme in lipid A formation. Extracts of a temperature-sensitive firA mutant, RL-25, were assayed for their ability to acylate UDP-GlcNAc, using a coupled assay. The results suggested that extracts of RL-25 might be defective in the third enzyme of this pathway, the UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. Living cells of RL-25 also displayed a 5-fold decreased rate of lipid A biosynthesis at the nonpermissive temperature as judged by a 32Pi incorporation assay. In order to examine N-acyltransferase activity directly, the substrate [alpha-32P]UDP-3-O-(R-3-hydroxymyristoyl)-GlcN was synthesized enzymatically. N-Acyltransferase specific activity in RL-25 extracts was reduced to less than 10% of wild-type. When the wild-type firA gene was cloned into a T7-based expression vector, N-acyltransferase specific activity increased almost 360-fold relative to wild-type extracts, demonstrating that firA is the structural gene for the enzyme. The N-acyltransferase displays absolute specificity for the R-3-OH moiety of R-3-hydroxymyristoyl-ACP, as does the O-acyltransferase, consistent with the placement of R-3-hydroxymyristate in E. coli lipid A. |
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Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
LpxD |
GO:0009245 |
lipid A biosynthetic process |
IMP: Inferred from Mutant Phenotype |
P |
A ts mutantion in the lpxD gene (firA200) is shown to decrease the rate of lipid A synthesis at the restrictive temperature (Figs. 2 and 3). |
complete | ||
|
LpxD |
GO:0016410 |
N-acyltransferase activity |
IDA: Inferred from Direct Assay |
F |
The enzyme displays absolute specificity for the 3-OH group of R-3-hydroxymyristoyl-ACP (Fig. 9). |
complete | ||
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