学术探索
学术期刊
新闻热点
数据分析
智能评审

EQUILIBRIUM CONSTANT FOR REVERSIBLE DEAMINATION OF ASPARTIC ACID

被引：26
作者：
BADA, JL
MILLER, SL
机构：
[1] University of California at San Diego, Department of Chemistry, La Jolla
来源：
BIOCHEMISTRY | 1968年 / 7卷 / 10期
关键词：
D O I：
10.1021/bi00850a014
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 equilibrium constant for the deamination of aspartic acid to fumaric acid and ammonia has been measured between 5 and 37° with the enzyme aspartase, and between 60 and 135° by the nonenzymatic reaction. The equilibrium constant is given by log KDL = 8.188 - 2315.5/T - 0.01025T. The equilibrium constant for the enzyme reaction, KL, is 2KDL. The pH and ionic strength dependence of this equilibrium were also investigated. © 1968, American Chemical Society. All rights reserved.
引用
收藏
页码：3403 / &
相关论文
共 32 条
1234