Site-directed mutagenesis of cation coordinating residues in the gastric H,K-ATPase.

Abstract:

:Site-mutations were introduced into putative cation binding site 1 of the H,K-ATPase at glu-797, thr-825, and glu-938. The side chain oxygen of each was not essential but the mutations produced different activation and inhibition kinetics. Site mutations thr-825 (ala, leu) and glu-938 (ala, gln) modestly decreased the apparent affinity to K+, while glu-797 (gln) was equivalent to wild type. As expected of competitive inhibition, mutations of thr-825 and glu-938 that decreased the apparent affinity for K+ also increased the apparent affinity for SCH28080. This is consistent with the participation of thr-825 and glu-938 in a cation binding domain. The sidechain geometry, but not the sidechain charge of glu-797, is essential to ATPase function as the site mutant glu-797 (gly) inactivated the H,K-ATPase, while glu-797 (gln) was active but the apparent affinity to SCH 28080 was decreased by four-fold. Lys-793, a unique residue of the H,K-ATPase, was essential for ATPase function. Since this residue is adjacent to site 1, the result suggests that charge pairing between lys-793 and residues at or near this site may be essential to ATPase function.

journal_name

Arch Biochem Biophys

authors

Rulli SJ,Louneva NM,Skripnikova EV,Rabon EC

doi

10.1006/abbi.2000.2243

subject

Has Abstract

pub_date

2001-03-01 00:00:00

pages

27-34

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(00)92243-4

journal_volume

387

pub_type

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