Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase

被引：37

作者：

Samsonova, NN ^{[1
]}

Smirnov, SV ^{[1
]}

Novikova, AE ^{[1
]}

Ptitsyn, LR ^{[1
]}

机构：

[1] Ajinomoto Genet Res Inst, Moscow 117545, Russia

来源：

FEBS LETTERS | 2005年 / 579卷 / 19期

关键词：

putrescine degradation; gamma-aminobutyraldehyde dehydrogenase; putrescine aminotransferase; Escherichia coli;

D O I：

10.1016/j.febslet.2005.06.038

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. K. parameters of YdcW for gamma-aminobutyraidehyde, NAD(+) and NADP(+) were 41 +/- 7, 54 +/- 10 and 484 +/- 72 mu M, 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. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：4107 / 4112

页数：6

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