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3-磷酸甘油醛铁氧还蛋白氧化还原酶,一种新型含钨酶,在嗜热古菌激烈火球菌中可能具有糖酵解作用。

Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus.

作者信息

Mukund S, Adams M W

机构信息

Department of Biochemistry and Molecular Biology, University of Georgia, Athens 30602, USA.

出版信息

J Biol Chem. 1995 Apr 14;270(15):8389-92. doi: 10.1074/jbc.270.15.8389.

DOI:10.1074/jbc.270.15.8389
PMID:7721730
Abstract

The archaeon Pyrococcus furiosus grows optimally at 100 degrees C by the fermentation of carbohydrates to yield acetate, CO2, and H2. Cell-free extracts contain very low activity of the glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase, but extremely high activity of glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR). GAPOR was purified under strictly anaerobic conditions. It is a monomeric, O2-sensitive protein of M(r) approximately 63,000 which contains pterin and approximately 1 tungsten and 6 iron atoms per molecule. The enzyme oxidized glyceraldehyde-3-phosphate (Km 28 microM) to 3-phosphoglycerate and reduced P. furiosus ferredoxin (Km 6 microM), but it did not oxidize formaldehyde, acetaldehyde, glyceraldehyde, benzaldehyde, glucose, glucose 6-phosphate, or glyoxylate, nor did it use NAD(P) as an electron acceptor. It is proposed that GAPOR has a glycolytic role and functions in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase.

摘要

嗜热栖热菌在100摄氏度时通过碳水化合物发酵产生乙酸盐、二氧化碳和氢气,生长最为适宜。无细胞提取物中糖酵解酶甘油醛-3-磷酸脱氢酶的活性非常低,但甘油醛-3-磷酸铁氧化还原酶(GAPOR)的活性极高。GAPOR是在严格厌氧条件下纯化得到的。它是一种单体蛋白,对氧气敏感,分子量约为63,000,每个分子含有蝶呤、约1个钨原子和6个铁原子。该酶将甘油醛-3-磷酸(Km为28微摩尔)氧化为3-磷酸甘油酸,并还原嗜热栖热菌铁氧化还原蛋白(Km为6微摩尔),但它不氧化甲醛、乙醛、甘油醛、苯甲醛、葡萄糖、6-磷酸葡萄糖或乙醛酸,也不以NAD(P)作为电子受体。有人提出,GAPOR具有糖酵解作用,可替代甘油醛-3-磷酸脱氢酶,可能还替代磷酸甘油酸激酶发挥功能。

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