Premium
Kinetics and mechanism of a reaction catalyzed by PST‐01 protease from Pseudomonas aeruginosa PST‐01
Author(s) -
Bobe Iulian M.,
Abdelmoez Wael,
Ogino Hiroyasu,
Yasuda Masahiro,
Ishimi Kosaku,
Ishikawa Haruo
Publication year - 2004
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.20052
Subject(s) - pseudomonas aeruginosa , kinetics , chemistry , protease , catalysis , mechanism (biology) , pseudomonadales , pseudomonadaceae , microbiology and biotechnology , bacteria , biochemistry , enzyme , biology , physics , genetics , quantum mechanics
The initial rates of carboxybenzoyl‐alanyl‐ l ‐leucyl‐amide ( Z ‐ l ‐Ala‐ l ‐Leu‐NH 2 ) synthesis from carboxybenzoy l ‐ l ‐alanine ( Z ‐ l ‐Ala) and l ‐leucineamide ( l ‐Leu‐NH 2 ) and Z ‐ l ‐Ala‐ l ‐Leu‐NH 2 hydrolysis in a homogeneous dimethyl sulfoxide‐aqueous buffer solution [1:1 (v/v)] system catalyzed by PST‐01 protease from Pseudomonas aeruginosa were measured under a wide range of Z ‐ l ‐Ala, l ‐Leu‐NH 2 and Z ‐ l ‐Ala‐ l ‐Leu‐NH 2 concentrations. The initial rates of the synthetic reaction, in which Z ‐ l ‐Ala‐ l ‐Leu‐NH 2 was produced from Z ‐ l ‐Ala and l ‐Leu‐NH 2 , were inhibited by the substrates. Furthermore, the initial rates of the synthetic reaction were not inhibited by the product Z ‐ l ‐Ala‐ l ‐Leu‐NH 2 , and those of the hydrolytic reaction were inhibited by Z ‐ l ‐Ala and l ‐Leu‐NH 2 . All the initial rate data of the synthetic and hydrolytic reactions were well correlated with the rate equation derived based on the proposed reaction scheme. © 2004 Wiley Periodicals, Inc.