AI Article Synopsis
- A comparison of active sites in beta-ketoacyl synthases (KAS) and similar enzymes shows significant differences in geometry and function of catalytic residues.
- A specific template derived from KAS I and II enzymes accurately identifies their family members without false positives.
- The catalytic roles of histidines vary between different KAS types and related enzymes, with a less specific template that includes only cysteine and one histidine yielding many irrelevant matches.
Article Abstract
A detailed comparison of the active sites in beta-ketoacyl synthases (KAS) and related enzymes has been made. Using three-dimensional templates of the three catalytic residues to scan the protein structural database reveals differences in both the geometry and the catalytic role of equivalent residues in different members of the family. The template based on the catalytic cysteine and two histidines in the KAS I and II is totally specific for this family, with no false hits. However, the role of the histidines in catalysis is different between KAS I/II and thiolase on the one hand and KAS III/chalcone synthase on the other. In contrast, a template comprising only cysteine and one histidine is not specific with many hits including members of the KAS family, metal binding sites, other active sites in nonhomologous proteins, and some "random" nonactive sites.
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| http://dx.doi.org/10.1002/prot.10421 | DOI Listing |
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