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IUBMB Comments Catalyses hydrogen transfer from C3 4 S )-2-hydroxy acids to 2-oxo acids. It contains tightly bound nicotinamide nucleotide in its active centre. This prosthetic group cannot be removed without denaturation of the protein.
Synonyms
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malate-lactate transhydrogenase
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transhydrogenase, lactate-malate
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(S)-lactate + oxaloacetate = pyruvate + malate
(S)-lactate + oxaloacetate = pyruvate + malate
mechanism
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(S)-lactate + oxaloacetate = pyruvate + malate
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(S)-lactate:oxaloacetate oxidoreductase
Catalyses hydrogen transfer from C3 or C4 (S)-2-hydroxy acids to 2-oxo acids. It contains tightly bound nicotinamide nucleotide in its active centre. This prosthetic group cannot be removed without denaturation of the protein.
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(S)-lactate + oxaloacetate
malate + pyruvate
pyruvate + L-malate
(S)-lactate + oxaloacetate
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Substrates: -
r
(S)-lactate + oxaloacetate
malate + pyruvate
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Substrates: -
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(S)-lactate + oxaloacetate
malate + pyruvate
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Substrates: -
r
(S)-lactate + oxaloacetate
malate + pyruvate
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Substrates: catalyzes hydrogen transfer from C3 or C4(S)-2-hydroxy acids to 2-oxo-acids, hydrogen donors: L-malate, DL-lactate and DL-alpha-hydroxybutyrate, low activity with: DL-alpha-hydroxyglutarate, DL-alpha-hydroxyvalerate, DL-beta-hydroxybutyrate and DL-alpha-hydroxycaprylate, hydrogen acceptors: oxalacetate, low activity with: alpha-ketoglutarate, alpha-ketocaprylate
r
(S)-lactate + oxaloacetate
malate + pyruvate
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Substrates: keto-tautomer is the enzymatically active form of oxalacetate
r
(S)-lactate + oxaloacetate
malate + pyruvate
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Substrates: 50% higher specific activity with malate and pyruvate as substrates
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(S)-lactate + oxaloacetate
malate + pyruvate
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Substrates: first step in fermentation of lactate
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(S)-lactate + oxaloacetate
malate + pyruvate
(S)-lactate + oxaloacetate
malate + pyruvate
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Substrates: -
r
(S)-lactate + oxaloacetate
malate + pyruvate
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Substrates: first step in fermentation of lactate
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NAD+
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prosthetic group
NAD+
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tightly bound in the active centre
NAD+
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NAD+/NADH equivalent binding weight is 35000 Da
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additional information
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no metal ion required
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p-hydroxymercuribenzoate
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additional information
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non-specific inhibition by high ionic strength
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6.3 - 9.5
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about 50% of maximal activity at pH 6.3 and 9.5
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no activity in Escherichia coli
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no activity in Propionibacterium shermanii
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formerly named as Micrococcus lactilyticus
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30000
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3 (or 4) * 30000, sucrose gradient centrifugation of succinylated and urea solubilized enzyme
99000 - 100000
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sucrose density gradient studies
70000
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70000
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sedimentation-diffusion and high-speed equilibrium methods
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dimer
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2 * 30000-43000, SDS-PAGE
trimer or tetramer
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3 (or 4) * 30000, sucrose gradient centrifugation of succinylated and urea solubilized enzyme
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-15°C, as ammonium sulfate suspension, about 10-20 mg of protein per ml, 40% loss of activity after 1 year
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DEAE-cellulose, DEAE-Sephadex
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Allen, S.H.G.
The isolation and characterization of malate-lactate transhydrogenase from Micrococcus lactilyticus
J. Biol. Chem.
241
5266-5275
1966
no activity in Escherichia coli, no activity in Propionibacterium shermanii, Veillonella parvula
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Allen, S.H.G.
Malate-lactate transhydrogenase from Micrococcus lactilyticus
Methods Enzymol.
13
262-269
1969
Veillonella parvula
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brenda
Allen, S.H.G.; Patil, J.R.
Studies on the structure and mechanism of action of the malate-lactate transhydrogenase
J. Biol. Chem.
247
909-916
1972
Veillonella parvula
brenda
Allen, S.H.G.
Molecular weight and subunit structure of the malate-lactate transhydrogenase
Eur. J. Biochem.
35
338-345
1973
Veillonella parvula
brenda
Allen, S.H.G.
Lactate-oxaloacetate transhydrogenase from Veillonella alcalescens
Methods Enzymol.
89
367-376
1982
Veillonella parvula
brenda
Dolin, M.I.
Kinetics of malic-lactic transhydrogenase. Abortive complex formation with substrates and products
J. Biol. Chem.
244
5273-5285
1969
Veillonella parvula
brenda
Dolin, M.I.
Kinetics of malic-lactic transhydrogenase. Effect of the keto-enol tautomerism of oxalacetate on the kinetics of oxalacetate formation and utilization
J. Biol. Chem.
243
3916-3923
1968
Veillonella parvula
brenda
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