一种NADPH 2-酮丙基-辅酶M氧化还原酶/羧化酶的结晶及初步X射线分析
Crystallization and preliminary X-ray analysis of a NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
作者信息
Jang S B, Jeong M S, Clark D D, Ensign S A, Peters J W
机构信息
Department of Chemistry and Biochemistry, Utah State University, Logan, UT 84322-0300, USA.
出版信息
Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):445-7. doi: 10.1107/s0907444901000695.
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 A resolution) could be achieved when the substrate or product of the reaction was added to the enzyme in a stoichiometric excess.
NADPH 2-酮丙基辅酶M（2-巯基乙烷磺酸盐）氧化还原酶/羧化酶是代谢途径中的终端酶，该代谢途径可将丙烯转化为中心代谢物乙酰乙酸。这种酶是一种含黄素腺嘌呤二核苷酸（FAD）的酶，属于NADPH：二硫化物氧化还原酶家族，催化2-酮丙基辅酶M的裂解和羧化反应，生成乙酰乙酸和辅酶M。晶体学试验表明，当反应底物或产物以化学计量过量添加到酶中时，可获得衍射质量最高的晶体（分辨率优于2.0埃）。
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