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大肠杆菌中第二种吩嗪硫酸甲酯连接的甲酸脱氢酶同工酶。

A second phenazine methosulphate-linked formate dehydrogenase isoenzyme in Escherichia coli.

作者信息

Pommier J, Mandrand M A, Holt S E, Boxer D H, Giordano G

机构信息

Laboratoire de Chimie Bacterienne, CNRS, Marseille, France.

出版信息

Biochim Biophys Acta. 1992 Jun 30;1107(2):305-13. doi: 10.1016/0005-2736(92)90417-k.

Abstract

A biochemical and immunological study has revealed a new formate dehydrogenase isoenzyme in Escherichia coli. The enzyme is an isoenzyme of the respiratory formate dehydrogenase (FDH-N) which forms part of the formate to nitrate respiratory pathway found in the organisms when it is grown anaerobically in the presence of nitrate. The new enzyme, termed FDH-Z, cross reacts with antibodies raised to FDH-N and possesses a similar polypeptide composition to FDH-N. FDH-Z catalyses the phenazine methosulphate-linked formate dehydrogenase activity present in the aerobically-grown bacterium. FDH-Z and FDH-N exhibit distinct regulation. Like formate dehydrogenase N, formate dehydrogenase Z is a membrane-bound molybdoenzyme. With nitrate reductase it can catalyse electron transfer between formate and nitrate. Quinones are required for the physiological electron transfer to nitrate. It seems likely that like FDH-N, FDH-Z functions physiologically as a formate: quinone oxidoreductase.

摘要

一项生化与免疫学研究揭示了大肠杆菌中一种新的甲酸脱氢酶同工酶。该酶是呼吸型甲酸脱氢酶(FDH-N)的同工酶,当生物体在硝酸盐存在的情况下厌氧生长时,它是生物体中甲酸到硝酸盐呼吸途径的一部分。这种新酶被称为FDH-Z,它与针对FDH-N产生的抗体发生交叉反应,并且具有与FDH-N相似的多肽组成。FDH-Z催化需氧生长细菌中存在的吩嗪硫酸甲酯连接的甲酸脱氢酶活性。FDH-Z和FDH-N表现出不同的调节方式。与甲酸脱氢酶N一样,甲酸脱氢酶Z是一种膜结合钼酶。它可以与硝酸还原酶一起催化甲酸和硝酸盐之间的电子转移。醌是生理上向硝酸盐进行电子转移所必需的。似乎与FDH-N一样,FDH-Z在生理上作为甲酸:醌氧化还原酶发挥作用。

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