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- W2076641052 abstract "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 beta-elimination reaction of threo-3-chloro-L-aspartate to form oxaloacetate, Cl-, and NH4. The enzyme was active toward only threo-3-chloro-L-aspartate and L-cysteine, but did not catalyze a beta-replacement reaction. The enzyme can be classified in a new group of PLP-dependent amino acid-lyases [EC 4.2.1.-]." @default.
- W2076641052 created "2016-06-24" @default.
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- W2076641052 date "2001-01-01" @default.
- W2076641052 modified "2023-09-23" @default.
- W2076641052 title "Occurrence of a Novel Lyase Catalyzing β-Elimination Reaction toward threo-3-Chloro-L-aspartate in Pseudomonas putida TPU 7151" @default.
- W2076641052 cites W33105634 @default.
- W2076641052 doi "https://doi.org/10.1271/bbb.65.435" @default.
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