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IUBMB Comments This enzyme, isolated from the bacterium Chromohalobacter salexigens DSM 3043, acts only on the (S)-enantiomer of 3-sulfolactate. Combined with EC 1.1.1.338, (2R)-3-sulfolactate dehydrogenase (NADP+), it provides a racemase system that converts (2S)-3-sulfolactate to (2R)-3-sulfolactate, which is degraded further by EC 4.4.1.24, (2R)-sulfolactate sulfo-lyase.
The enzyme is specific for NAD+.
The enzyme appears in viruses and cellular organisms
Synonyms
(S)-sulfolactate oxidoreductase, SlcC,
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(S)-sulfolactate oxidoreductase
(S)-sulfolactate oxidoreductase
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(S)-sulfolactate oxidoreductase
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SlcC
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(2S)-3-sulfolactate + NAD+ = 3-sulfopyruvate + NADH + H+
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(2S)-sulfolactate:NAD+ oxidoreductase
This enzyme, isolated from the bacterium Chromohalobacter salexigens DSM 3043, acts only on the (S)-enantiomer of 3-sulfolactate. Combined with EC 1.1.1.338, (2R)-3-sulfolactate dehydrogenase (NADP+), it provides a racemase system that converts (2S)-3-sulfolactate to (2R)-3-sulfolactate, which is degraded further by EC 4.4.1.24, (2R)-sulfolactate sulfo-lyase.
The enzyme is specific for NAD+.
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(2S)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
3-sulfopyruvate + NADH + H+
(2S)-3-sulfolactate + NAD+
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(2S)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
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the specific activity is only about 5% of that in the reverse direction
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r
(2S)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
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the specific activity is only about 5% of that in the reverse direction
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3-sulfopyruvate + NADH + H+
(2S)-3-sulfolactate + NAD+
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r
3-sulfopyruvate + NADH + H+
(2S)-3-sulfolactate + NAD+
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r
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neither pyruvate, oxaloacetate, (S)-3-phosphoglycerate, (R)-malate, (R)-lactate, (S)-malate or (S)-lactate is a substrate
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neither pyruvate, oxaloacetate, (S)-3-phosphoglycerate, (R)-malate, (R)-lactate, (S)-malate or (S)-lactate is a substrate
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additional information
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SlcC is not inhibited by pyruvate or oxaloacetate (5 mM), (S)-3-phosphoglycerate, (R)-malate, (R)-lactate, (S)-malate or (S)-lactate
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7
(2S)-3-sulfolactate
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apparent value, in 25 mM Tris buffer, pH 9.0 and 25°C
0.14
3-sulfopyruvate
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apparent value, in 25 mM Tris buffer, pH 9.0 and 25°C
2
NAD+
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apparent value, in 25 mM Tris buffer, pH 9.0 and 25°C
0.05
NADH
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apparent value, in 25 mM Tris buffer, pH 9.0 and 25°C
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0.2
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crude extracts of acetate-grown cells, using 3-sulfopyruvate as substrate, at pH 9.0 and 25°C
675
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enzyme from sulfolactate-grown cells after 91fold purification, using 3-sulfopyruvate as substrate, at pH 9.0 and 25°C
7.4
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crude extracts of sulfolactate-grown cells, using 3-sulfopyruvate as substrate, at pH 9.0 and 25°C
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34000
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2 * 34000, SDS-PAGE
61000
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native enzyme, gel filtration
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homodimer
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2 * 34000, SDS-PAGE
homodimer
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2 * 34000, SDS-PAGE
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at 4°C, SlcC remains stable for several weeks and can be frozen and thawed without loss of activity
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at 4°C, SlcC remains stable for several weeks and can be frozen and thawed without loss of activity
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ammonium sulfate precipitation, Mono Q column chromatography, phenyl Superose gel filtration, Superose 12 gel filtration
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Denger, K.; Cook, A.M.
Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase
Microbiology
156
967-974
2010
Chromohalobacter salexigens, Chromohalobacter salexigens DSM 3043
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1.1.1.310 (S)-sulfolactate dehydrogenase
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