鉴定大肠杆菌K12 YdcW蛋白为γ-氨基丁醛脱氢酶。
Identification of Escherichia coli K12 YdcW protein as a gamma-aminobutyraldehyde dehydrogenase.
作者信息
Samsonova Natalya N, Smirnov Sergey V, Novikova Anna E, Ptitsyn Leonid R
机构信息
Ajinomoto-Genetika Research Institute, 1st Dorozhny pr. 1, Moscow 117545, Russia.
出版信息
FEBS Lett. 2005 Aug 1;579(19):4107-12. doi: 10.1016/j.febslet.2005.06.038.
Gamma-aminobutyraldehyde dehydrogenase (ABALDH) from wild-type E. coli K12 was purified to apparent homogeneity and identified as YdcW by MS-analysis. YdcW exists as a tetramer of 202+/-29 kDa in the native state, a molecular mass of one subunit was determined as 51+/-3 kDa. Km parameters of YdcW for gamma-aminobutyraldehyde, NAD+ and NADP+ were 41+/-7, 54+/-10 and 484+/-72 microM, respectively. YdcW is the unique ABALDH in E. coli K12. A coupling action of E. coli YgjG putrescine transaminase and YdcW dehydrogenase in vitro resulted in conversion of putrescine into gamma-aminobutyric acid.
来自野生型大肠杆菌K12的γ-氨基丁醛脱氢酶（ABALDH）被纯化至表观均一，并通过质谱分析鉴定为YdcW。YdcW在天然状态下以202±29 kDa的四聚体形式存在，一个亚基的分子量测定为51±3 kDa。YdcW对γ-氨基丁醛、NAD⁺和NADP⁺的Km参数分别为41±7、54±10和484±72 μM。YdcW是大肠杆菌K12中唯一的ABALDH。大肠杆菌YgjG腐胺转氨酶和YdcW脱氢酶在体外的偶联作用导致腐胺转化为γ-氨基丁酸。
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