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US 4,590,161 AGranted
Microbiologically produced L-phenylalanine-dehydrogenase, process for its recovery and use
AssigneesDegussa AG, Gesellschaft fur biotechnologisch Forschung
InventorsMaria-Regina Kula, Werner Hummel, Horst Schutte, Wolfgang Leuchtenberger
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Abstract
The invention is directed to a microbiologically produced L-phenylalanine-dehydrogenase and a process for its recovery from Brevibacterium species DSM 2448. The new enzyme can be used for the enzymatic conversion of phenyl pyruvic acid, p-hydroxyphenyl pyruvic aid, indolyl pyruvic acid or 2-keto-4-(methylmercapto)-butyric acid into the corresponding L-.alpha.-aminocarboxylic acids.
Claims19
L-phenylalanine-dehydrogenase having the following properties:
- (a) it catalyzes the reductive amination of phenyl pyruvic acid to L-phenylalanine in the presence of ammonium ions and with NADH (nicotinamide-adenine-dinucleotide) as coenzyme.,
- (b) it catalyzes the reductive amination of .alpha.-ketocarboxylic acids to the corresponding .alpha.-aminocarboxylic acids, including p-hydroxyphenyl pyruvic acid to L-tyrosine, indolyl pyruvic acid to L-tryptophane and 2-keto-4-(methylmercapto)-butyric acid to L-methionine, in the presence of ammonium ions and with NADH as coenzyme,
- (c) it catalyzes the oxidative desamination of L-phenylalanine, 1-tyrosine, L-tryptophane and L-methionine with NAD.sup.+ as coenzyme,
- (d) it has an optimum pH region for the reductive amination of 8.5.+-.1, and
- (e) it has an optimum pH region for the oxidative desamination of 10.+-.1.
2 more elements
Dependencies are inferred from the claim text.