His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate.

Abstract:

:Acylaminoacyl peptidase is a member of the prolyl oligopeptidase family. Amino acid sequence alignment suggests that the stabilization of the tetrahedral intermediate should be mediated by His507 rather than by a tyrosine residue found in the other family members of this serine peptidase group. The pH dependence of k(cat)/K(m) did not reveal any effect of His507. Substitution of an alanine for His507 gave the same bell-shaped pH rate profile with the same pK(a) values (7.0 and 8.7). However, the value of the rate constant was 85 times lower with the modified enzyme, which indicated that His507 is an important residue that is probably involved in the formation of the 3-dimensional structure.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kiss AL,Szeltner Z,Fülöp V,Polgár L

doi

10.1016/j.febslet.2004.06.054

keywords:

subject

Has Abstract

pub_date

2004-07-30 00:00:00

pages

17-20

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579304007987

journal_volume

571

pub_type

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