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Thimet oligopeptidase: site-directed mutagenesis disproves previous assumptions about the nature of the catalytic site.

Abstract：

:Zinc metallopeptidases that contain the His-Glu-Xaa-Xaa-His (HEXXH) motif generally have a third ligand of the metal ion that may be either a Glu residue (in clan MA) or a His residue (in clan MB) (Rawlings and Barrett (1995) Methods Enzymol. 248, 183-228). Thimet oligopeptidase has not yet been assigned to either clan, and both Glu and His residues have been proposed as the third ligand. We mutated candidate ligand residues in the recombinant enzyme and identified Glu, His and Asp residues that are important for catalytic activity and/or stability of the protein. However, neither of the Glu and His residues close to the HEXXH motif that have previously been suggested to be ligands is required for the binding of zinc. We conclude that thimet oligopeptidase is not a member of clan MA or clan MB and it is likely that the enzyme possesses a catalytic site and protein fold different from those identified in any metallopeptidase to date. The definitive identification of the third zinc ligand may well require the determination of the crystallographic structure of thimet oligopeptidase or one of its homologues.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Chen JM,Stevens RA,Wray PW,Rawlings ND,Barrett AJ

doi

10.1016/s0014-5793(98)01032-1

subject

Has Abstract

pub_date

1998-09-11 00:00:00

pages

16-20

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)01032-1

journal_volume

435

pub_type

杂志文章

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