ANION ACTIVATION OF MALEATE HYDRATASE

被引：7

作者：

BRITTEN, JS

MORELL, H

TAGGART, JV

机构：

[1] Department of Physiology, College of Physicians and Surgeons, Columbia University, New York

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 185卷 / 01期

关键词：

D O I：

10.1016/0005-2744(69)90296-4

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：

Maleate hydratase (d-malate hydro-lyase) has been found to have an absolute requirement for certain univalent anions. The relative effectiveness of the various anions in activating the hydratase can be ranked Br- - Cl-, NO3- < I- < SCN- < formate- < F- < accetate- =o. Activation appears to be independent of pH in the range 6.0-9.0 and, at least in the case of Cl-, is described by the expression V v=(I+ Ks [S]) (I + Ka [A]). where the v is the initial velocity; V, the maximal initial velocity; [S] substrate concentration; [A], anion concentration; Ks, a Michaelis constant; and Ka, the apparent dissaciation constant of enzyme with activating anion. © 1969.

引用

页码：220 / &

共 13 条

[1] SOME MECHANISMS FOR THE INTERPRETATION OF THE EFFECTS OF PH AND BUFFER SALTS ON A SIMPLE ENZYMATIC REACTION [J].