3zyt
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Structure Determination of EstA from Arthrobacter nitroguajacolicus Rue61a
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Structural highlights
FunctionPublication Abstract from PubMedIn this article we analyze the reasons for catalytic promiscuity of a type VIII esterase with beta-lactamase fold and the ability to cleave beta-lactams. We compared the structure of this enzyme to those of an esterase of the same type without any lactamase ability, an esterase with moderate lactamase ability, and a class C beta-lactamase with similar fold. Our results show that for these enzymes, the difference in the substrate specificity is sterically driven. Crystal structure analysis of EstA from Arthrobacter sp. Rue61a--an insight into catalytic promiscuity.,Wagner UG, DiMaio F, Kolkenbrock S, Fetzner S FEBS Lett. 2014 Apr 2;588(7):1154-60. doi: 10.1016/j.febslet.2014.02.045. Epub, 2014 Mar 5. PMID:24613918[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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