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叶绿体和细胞质酶:IV. 豌豆叶果糖1,6 -二磷酸醛缩酶

Chloroplast and Cytoplasmic Enzymes: IV. Pea Leaf Fructose 1,6-Diphosphate Aldolases.

作者信息

Anderson L E, Pacold I

机构信息

Department of Biological Sciences, University of Illinois at Chicago Circle, Chicago, Illinois 60680.

出版信息

Plant Physiol. 1972 Mar;49(3):393-7. doi: 10.1104/pp.49.3.393.

Abstract

Several peaks of aldolase activity are found in the isoelectric focusing pattern of pea (Pisum sativum) leaf chloroplast extracts. One peak, separated by 0.5 pH unit from the major chloroplast aldolase peak, is found when cytoplasmic extracts are focused. The chloroplast and cytoplasmic enzymes have a pH 7.4 optimum with fructose 1,6-diphosphate. The Michaelis constant for fructose-1,6-diphosphate is 19 muM for the chloroplast, 21 muM for the cytoplasmic enzyme, and for sedoheptulose 1,7-diphosphate, 8 muM for the chloroplast enzyme, 18 muM for the cytoplasmic enzyme. Both enzymes are inhibited by d-glyceraldehyde 3-phosphate and by ribulose 1,5-diphosphate. The similarity in the catalytic properties of the isoenzymes suggests that both enzymes have an amphibolic role in carbon metabolism in the green leaf.

摘要

在豌豆(Pisum sativum)叶片叶绿体提取物的等电聚焦图谱中发现了几个醛缩酶活性峰。当对细胞质提取物进行聚焦时,发现有一个峰与主要的叶绿体醛缩酶峰相隔0.5个pH单位。叶绿体和细胞质中的酶在以1,6-二磷酸果糖为底物时,最适pH为7.4。叶绿体醛缩酶对1,6-二磷酸果糖的米氏常数为19μM,细胞质醛缩酶为21μM;对于1,7-二磷酸景天庚酮糖,叶绿体醛缩酶的米氏常数为8μM,细胞质醛缩酶为18μM。两种酶都受到3-磷酸d-甘油醛和1,5-二磷酸核酮糖的抑制。同工酶催化特性的相似性表明,这两种酶在绿叶的碳代谢中都具有兼性作用。

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The preparation of sedoheptulose diphosphate.
J Biol Chem. 1956 Feb;218(2):745-52.
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Isolation and characterization of fructose diphosphate aldolase from Pisum sativum.
Biochim Biophys Acta. 1967 Jul 11;139(2):460-8. doi: 10.1016/0005-2744(67)90049-6.
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Isolation of crystalline pig kidney aldolase B.
Biochim Biophys Acta. 1971 Feb 10;227(2):460-3. doi: 10.1016/0005-2744(71)90077-5.
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Studies on the substrates of D-fructose 1,6-diphosphate aldolase in solution.
Biochemistry. 1970 Jun 9;9(12):2454-62. doi: 10.1021/bi00814a010.

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