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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
1.3.1.7
349356
L- and mesotartaric acid dehydrogenase (crystalline)
Methods Enzymol.
9
236-240
1966
Bos taurus
-
1.3.1.7
349356
L- and mesotartaric acid dehydrogenase (crystalline)
Methods Enzymol.
9
236-240
1966
Pseudomonas sp.
-
1.3.1.7
349356
L- and mesotartaric acid dehydrogenase (crystalline)
Methods Enzymol.
9
236-240
1966
Pseudomonas putida
-
1.3.1.7
349356
L- and mesotartaric acid dehydrogenase (crystalline)
Methods Enzymol.
9
236-240
1966
Rattus norvegicus
-
1.3.1.7
349356
L- and mesotartaric acid dehydrogenase (crystalline)
Methods Enzymol.
9
236-240
1966
Pseudomonas sp. A
-
1.3.1.7
349359
Substrate determinants of the course of tartrate dehydrogenase-catalyzed reactions
Biochemistry
34
7517-7524
1995
Escherichia coli
7779796
1.3.1.7
349359
Substrate determinants of the course of tartrate dehydrogenase-catalyzed reactions
Biochemistry
34
7517-7524
1995
Pseudomonas putida
7779796
1.3.1.7
349358
Tartrate dehydrogenase-oxalate complexes: formation of a stable analog of a reaction intermediate complex
Arch. Biochem. Biophys.
315
255-261
1994
Escherichia coli
7986065
1.3.1.7
287509
The stereospecificity of sequential nicotinamide-adenine dinucleotide-dependent oxidoreductases in relation to the evolution of metabolic sequences
Biochem. J.
149
553-557
1975
Pseudomonas putida
1200995
1.3.1.7
287509
The stereospecificity of sequential nicotinamide-adenine dinucleotide-dependent oxidoreductases in relation to the evolution of metabolic sequences
Biochem. J.
149
553-557
1975
Pseudomonas putida ATCC 17642
1200995
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