Kinetic analysis of the inhibition of phenylalanine ammonia-lyase by 2-aminoindan-2-phosphonic acid and other phenylalanine analogues

被引：50

作者：

Appert, C

Zon, J

Amrhein, N ^{[1
]}

机构：

[1] Swiss Fed Inst Technol, Inst Plant Sci, CH-8092 Zurich, Switzerland

[2] Wroclaw Univ Technol, Inst Organ Chem Biochem & Biotechnol, PL-50370 Wroclaw, Poland

来源：

PHYTOCHEMISTRY | 2003年 / 62卷 / 03期

关键词：

Petroselinum crispum; 2-aminoindan-2-phosphonic acid (AIP); phenylalanine ammonia-lyase (PAL); slow-binding enzyme inhibitor;

D O I：

10.1016/S0031-9422(02)00561-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The conformationally restricted phenylalanine analogue 2-aminoindan-2-phosphonic acid (AIP) inhibits phenylalanine ammonialyase (PAL) competitively in a time-dependent manner. This phenomenon was investigated in more detail with the heterologously expressed, highly purified homotetrameric PAL-1 isozyme from parsley. The kinetic analysis revealed that the enzyme-inhibitor complex is formed in a single "slow" step with an association rate of k(2) = 2.6 +/- 0.04 10(4) M-1 s(-1). The inhibition is reversible with a dissociation rate of k(-2) = 1.8 +/- 0.04 10(-4) s(-1) I and an equilibrium constant of K-i = 7 +/- 2 nM. The previously described PAL inhibitor (S)-2-aminooxy-3-phenylpropanoic acid [(S)-AOPP] was also found to be a slow-binding inhibitor of PAL-1. The carboxyl analogue of AIP, 2-aminoindan-2-carboxylic acid, served as a substrate of PAL-1 and was converted to indene-2-carboxylic acid. (C) 2003 Elsevier Science Ltd. All rights reserved.

引用

页码：415 / 422

页数：8

共 30 条

[1]

AMRHEIN N, 1977, PLANT SCI LETT, V8, P313, DOI 10.1016/0304-4211(77)90148-1

[2]

AMRHEIN N, 1976, BER DEUT BOT GES, V89, P247

[3] INHIBITION OF ANTHOCYANIN FORMATION IN SEEDLINGS AND FLOWERS BY THE ENANTIOMERS OF "ALPHA-AMINOOXY-BETA-PHENYLPROPIONIC ACID AND THEIR N-BENZYLOXYCARBONYL DERIVATIVES [J].