瓜伊马氏热球菌的双功能丙酮酸脱羧酶/丙酮酸铁氧化还蛋白氧化还原酶。

IF 2.3 4区 生物学 Q3 MICROBIOLOGY
Archaea-An International Microbiological Journal Pub Date : 2014-05-29 eCollection Date: 2014-01-01 DOI:10.1155/2014/349379
Mohammad S Eram, Erica Oduaran, Kesen Ma
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引用次数: 18

摘要

超嗜热古菌瓜伊马热球菌(Thermococcus guaymasensis)产生乙醇作为代谢终产物,催化乙醛还原为乙醇的乙醇脱氢酶(ADH)已被纯化和表征。然而,催化乙醛形成的酶尚未被确定。本研究在严格厌氧条件下纯化了一种催化丙酮酸制乙醛的酶,并对其进行了表征。该酶具有丙酮酸脱羧酶(PDC)和丙酮酸铁氧化还蛋白氧化还原酶(POR)活性。它对氧敏感,PDC和POR活性的最佳温度分别为85°C和>95°C。纯化后的酶活性分别为3.8±0.22 U mg(-1)和20.2±1.8 U mg(-1),每种酶的最佳ph值分别为9.5和8.4。辅酶A对这两种活性都是必需的,尽管它不是前者的底物。酶的动力学参数分别测定。纯化后的酶为异四聚体。确定了双功能PDC/POR亚基的编码基因序列。预测所有嗜热β -酮酸铁氧化还蛋白氧化还原酶均具有双功能,可催化相应β -酮酸的非氧化和氧化脱羧活性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

The bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase from Thermococcus guaymasensis.

The bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase from Thermococcus guaymasensis.

The bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase from Thermococcus guaymasensis.

The bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase from Thermococcus guaymasensis.

The hyperthermophilic archaeon Thermococcus guaymasensis produces ethanol as a metabolic end product, and an alcohol dehydrogenase (ADH) catalyzing the reduction of acetaldehyde to ethanol has been purified and characterized. However, the enzyme catalyzing the formation of acetaldehyde has not been identified. In this study an enzyme catalyzing the production of acetaldehyde from pyruvate was purified and characterized from T. guaymasensis under strictly anaerobic conditions. The enzyme had both pyruvate decarboxylase (PDC) and pyruvate ferredoxin oxidoreductase (POR) activities. It was oxygen sensitive, and the optimal temperatures were 85°C and >95°C for the PDC and POR activities, respectively. The purified enzyme had activities of 3.8 ± 0.22 U mg(-1) and 20.2 ± 1.8 U mg(-1), with optimal pH-values of 9.5 and 8.4 for each activity, respectively. Coenzyme A was essential for both activities, although it did not serve as a substrate for the former. Enzyme kinetic parameters were determined separately for each activity. The purified enzyme was a heterotetramer. The sequences of the genes encoding the subunits of the bifunctional PDC/POR were determined. It is predicted that all hyperthermophilic β -keto acids ferredoxin oxidoreductases are bifunctional, catalyzing the activities of nonoxidative and oxidative decarboxylation of the corresponding β -keto acids.

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来源期刊
CiteScore
7.50
自引率
0.00%
发文量
1
审稿时长
>12 weeks
期刊介绍: Archaea is a peer-reviewed, Open Access journal that publishes original research articles as well as review articles dealing with all aspects of archaea, including environmental adaptation, enzymology, genetics and genomics, metabolism, molecular biology, molecular ecology, phylogeny, and ultrastructure. Bioinformatics studies and biotechnological implications of archaea will be considered. Published since 2002, Archaea provides a unique venue for exchanging information about these extraordinary prokaryotes.
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