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X-ray snapshot of the mechanism of inactivation of human neutrophil elastase by 1,2,5-thiadiazolidin-3-one 1,1-dioxide derivatives.

Abstract：

:The mechanism of action of a general class of mechanism-based inhibitors of serine proteases, including human neutrophil elastase (HNE), has been elucidated by determining the X-ray crystal structure of an enzyme-inhibitor complex. The captured intermediate indicates that processing of inhibitor by the enzyme generates an N-sulfonyl imine functionality that is tethered to Ser195, in accordance with the postulated mechanism of action of this class of inhibitors. The identity of the HNE-N-sulfonyl imine species was further corroborated using electrospray ionization mass spectrometry.

journal_name

J Med Chem

journal_title

Journal of medicinal chemistry

authors

Huang W,Yamamoto Y,Li Y,Dou D,Alliston KR,Hanzlik RP,Williams TD,Groutas WC

doi

10.1021/jm700966p

subject

Has Abstract

pub_date

2008-04-10 00:00:00

pages

2003-8

issue

7

eissn

0022-2623

issn

1520-4804

journal_volume

51

pub_type

杂志文章

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