FUNCTIONS OF PHOSPHOENOLPYRUVATE CARBOXYKINASE AND MALIC ENZYME IN ANAEROBIC FORMATION OF SUCCINATE BY ASCARIS LUMBRICOIDES

被引：133

作者：

SAZ, HJ

LESCURE, OL

机构：

[1] The Johns Hopkins University, School of Hygiene and Public Health, Department of Pathobiology, Baltimore

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY | 1969年 / 30卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0010-406X(69)91296-1

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：

1. 1. Carbon dioxide stimulates two- to threefold the formation of pyruvate from phosphoenolpyruvate (PEP), and lactate from fructose-1,6-diphosphate by Ascaris muscle homogenates. 2. 2. The apparent Km value of Ascaris PEP carboxykinase for PEP is approximately one-seventh that for oxalacetate, which may account partially for the enzyme acting in a direction opposite to that reported for mammalian tissues. 3. 3. Distribution of enzymes and balance studies of malate utilization by Ascaris mitochondria suggest that cytoplasmic malate enters the mitochondrion, whereupon half is oxidized via the malic enzyme to pyruvate and acetate, while the remainder is reduced to succinate and propionate with the generation of ATP. © 1969.

引用

页码：49 / +

页数：1

共 37 条

[1]

BERGMEYER HU, 1963, METHODS ENZYMATIC ED, P332

[2]

BERGMEYER HU, 1963, METHODS ENZYMATIC ED, P229

[3] PYRUVATE KINASE AND PHOSPHOENOLPYRUVATE CARBOXYKINASE ACTIVITIES OF ASCARIS MUSCLE HYMENOLEPIS DIMINUTA AND SCHISTOSOMA MANSONI [J].