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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+ S )-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+
Synonyms
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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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MetaCyc
sulfolactate degradation I
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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+
additional information
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(2S)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
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Substrates: the specific activity is only about 5% of that in the reverse direction
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(2S)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
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Substrates: 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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Substrates: -
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3-sulfopyruvate + NADH + H+
(2S)-3-sulfolactate + NAD+
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Substrates: -
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Substrates: neither pyruvate, oxaloacetate, (S)-3-phosphoglycerate, (R)-malate, (R)-lactate, (S)-malate or (S)-lactate is a substrate
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Substrates: 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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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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MDH_METFV
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
339
0
36762
Swiss-Prot
other Location (Reliability: 5 )
SLCC_CHRSD
Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)
309
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33135
Swiss-Prot
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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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4
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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 israelensis, Chromohalobacter israelensis DSM 3043
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