期刊
FEMS MICROBIOLOGY LETTERS
卷 298, 期 1, 页码 93-98出版社
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2009.01699.x
关键词
Bordetella; 2-aminophenol derivative; 4-amino-3-hydroxybenzoate; 2-amino-5-carboxymuconic 6-semialdehyde; 2-amino-5-carboxymuconic 6-semialdehyde deaminase; 2-aminomuconate deaminase
类别
The 4-amino-3-hydroxybenzoate-assimilating Bordetella sp. strain 10d produces a deaminase that catalyzes the deamination of 2-amino-5-carboxymuconic 6-semialdehyde. A gene encoding the deaminase, ahdB, was cloned and expressed in Escherichia coli; ahdB is located downstream from the previously reported genes encoding 4-amino-3-hydroxybenzoate2,3-dioxygenase ( ahdA) and a LysR-type regulator. The deduced amino acid sequence of ahdB shows 30-33% identity to those of previously reported 2-aminomuconate deaminases. We identified a region (RAGDFLXVSG) conserved in AhdB and three other deaminases. The recombinant enzyme AhdB was purified to homogeneity. After a coupled enzyme assay with purified AhdA, AhdB, and the substrate 4-amino-3-hydroxybenzoate, the final product, formed by the action of AhdA, AhdB, and by nonenzymatic decarboxylation, was identified by HPLC, MS, and H-1-nuclear magnetic resonance analyses as 2-hydroxymuconic 6-semialdehyde.
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