Occurrence of a novel lyase catalyzing beta-elimination reaction toward threo-3-chloro-L-aspartate in Pseudomonas putida TPU 7151.
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.-].
Kato
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Y
Biotechnology Research Center, Faculty of Engineering, Toyama Prefectural University, Kosugi, Japan.
Asano
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Y
D001224:Aspartic Acid / Q000031:analogs & derivatives / Q000378:metabolism*; D001673:Biodegradation, Environmental; D007700:Kinetics; D008190:Lyases / Q000302:isolation & purification / Q000378:metabolism*; D016958:Pseudomonas putida / Q000201:enzymology* / Q000302:isolation & purification; D012988:Soil Microbiology; D013379:Substrate Specificity
C432925:3-chloroaspartic acid; D001224:Aspartic Acid; D008190:Lyases