来自嗜热古菌激烈火球菌的一种活性过高的NAD(P)H：铁氧化还原蛋白氧化还原酶。
A hyperactive NAD(P)H:Rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus.
作者信息
Ma K, Adams M W
机构信息
Department of Biochemistry and Molecular Biology and Center for Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602, USA.
出版信息
J Bacteriol. 1999 Sep;181(17):5530-3. doi: 10.1128/JB.181.17.5530-5533.1999.
Abstract
NAD(P)H:rubredoxin oxidoreductase (NROR) has been purified from the hyperthermophilic archaeon Pyrococcus furiosus. The enzyme is exceedingly active in catalyzing the NADPH-dependent reduction of rubredoxin, a small (5.3-kDa) iron-containing redox protein that had previously been purified from this organism. The apparent Vmax at 80 degrees C is 20,000 micromol/min/mg, which corresponds to a kcat/Km value of 300,000 mM(-1) s(-1). The apparent Km values measured at 80 degrees C and pH 8.0 for rubredoxin, NADPH, and NADH were 50, 5, and 34 microM, respectively. The enzyme did not reduce P. furiosus ferredoxin. NROR is a monomer with a molecular mass of 45 kDa and contains one flavin adenine dinucleotide molecule per mole but lacks metals and inorganic sulfide. The possible physiological role of this hyperactive enzyme is discussed.
摘要
NAD(P)H：铁氧化还原蛋白氧化还原酶（NROR）已从嗜热古菌激烈火球菌中纯化出来。该酶在催化铁氧化还原蛋白的NADPH依赖性还原反应方面具有极高的活性，铁氧化还原蛋白是一种小的（5.3 kDa）含铁血氧化还原蛋白，此前已从该生物体中纯化出来。在80℃时的表观Vmax为20,000微摩尔/分钟/毫克，这对应于300,000 mM⁻¹ s⁻¹的kcat/Km值。在80℃和pH 8.0条件下测得的铁氧化还原蛋白、NADPH和NADH的表观Km值分别为50、5和34 microM。该酶不能还原激烈火球菌铁氧化还原蛋白。NROR是一种分子量为45 kDa的单体，每摩尔含有一个黄素腺嘌呤二核苷酸分子，但不含金属和无机硫化物。文中讨论了这种高活性酶可能的生理作用。
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