role of motif iii in catalysis by acetyl-coa synthetase

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ID: 221213
2012
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Abstract
The acyl-adenylate-forming enzyme superfamily, consisting of acyl- and aryl-CoA synthetases, the adenylation domain of the nonribosomal peptide synthetases, and luciferase, has three signature motifs (I–III) and ten conserved core motifs (A1–A10), some of which overlap the signature motifs. The consensus sequence for signature motif III (core motif A7) in acetyl-CoA synthetase is Y-X-S/T/A-G-D, with an invariant fifth position, highly conserved first and fourth positions, and variable second and third positions. Kinetic studies of enzyme variants revealed that an alteration at any position resulted in a strong decrease in the catalytic rate, although the most deleterious effects were observed when the first or fifth positions were changed. Structural modeling suggests that the highly conserved Tyr in the first position plays a key role in active site architecture through interaction with a highly conserved active-site Gln, and the invariant Asp in the fifth position plays a critical role in ATP binding and catalysis through interaction with the 2′- and 3′-OH groups of the ribose moiety. Interactions between these Asp and ATP are observed in all structures available for members of the superfamily, consistent with a critical role in substrate binding and catalysis for this invariant residue.
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ingram-smith2012archaearole Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Cheryl Ingram-Smith;Jerry L. Thurman;Karen Zimowski;Kerry S. Smith
Journal annals of nuclear energy
Year 2012
DOI
10.1155/2012/509579
URL
http://dx.doi.org/10.1155/2012/509579
Keywords
Microbiology

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