当前位置： SCI文献检索 > ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS期刊下所有文献 > Residues in P-glycoprotein catalytic sites that react with the inhibitor 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole.

Residues in P-glycoprotein catalytic sites that react with the inhibitor 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole.

Abstract：

:7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl) is a specific covalent inhibitor of P-glycoprotein ATPase activity (M. K. Al-Shawi, and A. E. Senior, 1993, J. Biol. Chem. 268, 4197-4206). Complete inhibition occurs at a reaction stoichiometry of 1 mol NBD/mol P-glycoprotein, and the reagent has proved valuable in understanding catalytic mechanisms, particularly in relation to catalytic site cooperativity (A. E. Senior, and S. Bhagat, 1998, Biochemistry 37, 831-836). The actual location of reaction in the amino acid sequence has not yet been determined. Using a combined mutagenesis and biochemical approach we establish here that the initial reaction of NBD-Cl is with Cys within the Walker A consensus sequence of the N- or C-terminal nucleotide site (Cys-431 or Cys-1074 of human P-glycoprotein). Reaction with either Cys yields full inhibition. It was further found that inhibition consists of dithiothreitol (DTT)-reversible and DTT-irreversible components. The former predominates at low pH and the latter at higher pH. This demonstrates that, at higher pH, intramolecular transfer of NBD from Cys to Lys occurs, probably to the proximate Walker A Lys (Lys-433 or Lys-1076 of human P-glycoprotein). After transfer of NBD to Lys, P-glycoprotein ATPase remains fully inhibited.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Senior AE,Gros P,Urbatsch IL

doi

10.1006/abbi.1998.0778

subject

Has Abstract

pub_date

1998-09-01 00:00:00

pages

121-5

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(98)90778-0

journal_volume

357

pub_type

杂志文章

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