Origin of the stereospecificity in binding hydroxamates of α- and β-phenylalanine methylamide to thermolysin revealed by the X-ray crystallographic study

Cited 5 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorSeung-Jun Kim-
dc.contributor.authorD H Kim-
dc.contributor.authorJ D Park-
dc.contributor.authorJoo Rang Woo-
dc.contributor.authorY H Jin-
dc.contributor.authorSeong Eon Ryu-
dc.date.accessioned2017-04-19T08:59:50Z-
dc.date.available2017-04-19T08:59:50Z-
dc.date.issued2003-
dc.identifier.issn09680896-
dc.identifier.uri10.1016/S0968-0896(03)00140-8ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6111-
dc.description.abstractOptically active N-formyl-N-hydroxy-α-phenylalanine methylamide (1) and N-formyl-N-hydroxy-β-phenylalanine methylamide (2) were evaluated as inhibitors for thermolysin (TLN) to find that while the D-form is more potent than its enantiomer in the case of the hydroxamate of α-Phe-NHMe, in the inhibition with hydroxamate of β-Phe-NHMe, the L-isomer (Ki=1.66±0.05 μM) is more effective than its enantiomer. In order to shed light on the stereochemical preference observed in the inhibitions, X-ray crystallographic analyses of the crystalline TLN·D-1 and TLN·L-2 complexes were performed to the resolution of 2.1 ?. While L-2 binds TLN like substrate does with its benzyl aromatic ring occupying the S1′ pocket, the electron density in the S1′ pocket in the complex of TLN·D-1 is weak and could best be accounted for by the methylcarbamoyl moiety. For both inhibitors, the hydroxamate moiety coordinates the active site zinc ion in a bidentate fashion.-
dc.publisherElsevier-
dc.titleOrigin of the stereospecificity in binding hydroxamates of α- and β-phenylalanine methylamide to thermolysin revealed by the X-ray crystallographic study-
dc.title.alternativeOrigin of the stereospecificity in binding hydroxamates of α- and β-phenylalanine methylamide to thermolysin revealed by the X-ray crystallographic study-
dc.typeArticle-
dc.citation.titleBioorganic & Medicinal Chemistry-
dc.citation.number11-
dc.citation.endPage2426-
dc.citation.startPage2421-
dc.citation.volume11-
dc.contributor.affiliatedAuthorSeung-Jun Kim-
dc.contributor.alternativeName김승준-
dc.contributor.alternativeName김동-
dc.contributor.alternativeName박정대-
dc.contributor.alternativeName우주랑-
dc.contributor.alternativeName진용호-
dc.contributor.alternativeName류성언-
dc.identifier.bibliographicCitationBioorganic & Medicinal Chemistry, vol. 11, no. 11, pp. 2421-2426-
dc.identifier.doi10.1016/S0968-0896(03)00140-8-
dc.description.journalClassY-
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.