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Activation of E. coli UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase by Fe(2+) yields a more efficient enzyme with altered ligand affinity
The metal-dependent deacetylase UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) catalyzes the first committed step in lipid A biosynthesis, the hydrolysis of UDP-3-O-myristoyl-N-acetyl-glucosamine to form UDP-3-O-myristoyl-glucosamine and acetate. Consequently, LpxC is a target...
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| Main Authors: | , , , |
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| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
2010
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| Teme: | |
| Online dostop: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2884013/ https://ncbi.nlm.nih.gov/pubmed/20136146 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi902066t |
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