Occurrence of a Novel Lyase Catalyzing β-Elimination Reaction toward threo-3-Chloro-L-aspartate in Pseudomonas putida TPU 7151
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概要
- 論文の詳細を見る
A bacterium, Pseudomonas putida TPU 7151,which degrades threo-3-chloro-L-aspartate, was isolated from soil and the enzyme responsible for the degradation of the amino acid was partially purified from the cell-free extract of the strain. The enzyme, which required PLP for its reaction, catalyzed a stoichiometric β-elimination reaction of threo-3-chloro-L-aspartate to form oxaloacetate, Cl^-, and NG_4^+. The enzyme was active toward only threo-3-chloro-L-aspartate and L-cysteine, but did not catalyze a β-replacement reaction. The enzyme can be classified in a new group of PLP-dependent amino acid-lyases [EC 4.2.1-].
- 社団法人日本農芸化学会の論文
- 2001-02-23
著者
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Asano Yasuhisa
Biotechnology Research Center Faculty Of Engineering Toyama Prefectural University
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Asano Yasuhisa
Biotechnology Res. Center And Dep. Of Biotechnology Toyama Prefectural Univ.
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Kato Yasuo
Biotechnology Research Center And Department Of Biotechnology Toyama Prefectural University
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