His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate
UNSPECIFIED. (2004) His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate. FEBS LETTERS, 571 (1-3). pp. 17-20. ISSN 0014-5793Full text not available from this repository.
Official URL: http://dx.doi.org/10.1016/j.febslet.2004.06.054
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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||FEBS LETTERS|
|Publisher:||ELSEVIER SCIENCE BV|
|Date:||30 July 2004|
|Number of Pages:||4|
|Page Range:||pp. 17-20|
Actions (login required)