Crystallization and preliminary X-ray analysis of a NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
Crystallization and preliminary X-ray analysis of a NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
复制标题
NADPH 2-酮丙基辅酶 M 氧化还原酶/羧化酶的结晶和初步 X 射线分析。
DOI：
10.1107/s0907444901000695
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Peters,JW
中科院分区：
文献类型：
--
作者：
Jang,SB;Jeong,MS;Clark,DD;Ensign,SA;Peters,JW
NADPH 2-酮丙基辅酶M（2-巯基乙磺酸）氧化还原酶/羧化酶是丙烯转化为中心代谢物乙酰乙酸的代谢途径中的末端酶。该酶是一种含有fad的酶，是NADPH：二硫氧化还原酶家族的一员，催化2-酮丙基辅酶M的裂解和羧化，形成乙酰乙酸和辅酶M。结晶试验表明，当反应的底物或产物以化学计量量过量加入酶中时，可以获得最高的衍射质量晶体（优于2.0 Å分辨率）。
NADPH 2-ketopropyl-coenzyme M (2-mercaptoethanesulfonate) oxidoreductase/carboxylase is the terminal enzyme in a metabolic pathway that results in the conversion of propylene to the central metabolite acetoacetate. This enzyme is an FAD-containing enzyme that is a member of the NADPH:disulfide oxidoreductase family of enzymes and catalyzes the cleavage and carboxylation of 2-ketopropyl-coenzyme M to form acetoacetate and coenzyme M. Crystallization trials have revealed that the highest diffraction quality crystals (better that 2.0 Å resolution) could be achieved when the substrate or product of the reaction was added to the enzyme in a stoichiometric excess.