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Information on EC 1.1.1.310 - (S)-sulfolactate dehydrogenase Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Chromohalobacter salexigens
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(S)-sulfolactate dehydrogenase
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(2S)-3-sulfolactate + NAD+ = 3-sulfopyruvate + NADH + H+
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sulfolactate degradation I
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Cysteine and methionine metabolism
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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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(S)-sulfolactate oxidoreductase
(S)-sulfolactate oxidoreductase
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(S)-sulfolactate oxidoreductase
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SlcC
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brenda
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brenda
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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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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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additional information
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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
7.4
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crude extracts of sulfolactate-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
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brenda
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brenda
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brenda
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brenda
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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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MDH_METFV
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
339
36762
Swiss-Prot
SLCC_CHRSD
Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768)
309
33135
Swiss-Prot
A0A087A1S5_9BIFI
326
36244
TrEMBL
D8GJD0_CLOLD
Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)
315
35972
TrEMBL
A0A143X466_9FIRM
300
34014
TrEMBL
A0A0P8AWQ7_9GAMM
336
35303
TrEMBL
A0A0P0LFX6_9BURK
359
38505
TrEMBL
A0A0P1GJS8_9RHOB
336
34719
TrEMBL
A0A0P0M8J5_9BURK
332
35862
TrEMBL
A0A165MK75_RHOFA
318
33891
TrEMBL
A0A0P1IIP7_9RHOB
326
35415
TrEMBL
A0A0F0KWH6_9MICO
360
37739
TrEMBL
A0A161KQA9_PEPDI
312
35757
TrEMBL
A0A0H4W207_9BORD
324
35563
TrEMBL
A0A166T1N4_9CLOT
315
35972
TrEMBL
A0A0M9EH10_9RHOB
326
35613
TrEMBL
A0A105TR28_9FLAO
314
35000
TrEMBL
A0A136LX65_9BACT
311
33474
TrEMBL
W7WTT2_9BURK
374
39849
TrEMBL
A0A151B505_9CLOT
315
36448
TrEMBL
A0A100J5S3_9ACTN
324
34139
TrEMBL
W7VU62_9BURK
374
39849
TrEMBL
A0A0N9Z2Y3_9ARCH
324
36299
TrEMBL
A0A0D1CPE2_9RHOB
301
31544
TrEMBL
A0A0P0MGL0_9BURK
321
34916
TrEMBL
A0A168LDM0_9CLOT
315
36009
TrEMBL
A0A0N0D883_9RHOB
305
31918
TrEMBL
A0A0H2M747_VARPD
313
32486
TrEMBL
A0A0N9YXL3_9ARCH
312
34522
TrEMBL
A0A0D6JF07_9RHIZ
314
33012
TrEMBL
A0A0M6Y588_9RHOB
336
35368
TrEMBL
A0A0H4VTB6_9BORD
328
35178
TrEMBL
A0A128EYE4_9GAMM
313
34772
TrEMBL
A0A162L4V8_9CLOT
388
42284
TrEMBL
A0A136N2U3_9BACT
300
33026
TrEMBL
A0A0D8HG50_9ACTN
331
35680
TrEMBL
A0A0P1EAR1_9RHOB
326
35720
TrEMBL
A0A0P1EQ73_9RHOB
305
31927
TrEMBL
A0A0F0KRH0_9MICO
324
34759
TrEMBL
A0A0M7APZ5_9RHOB
313
33140
TrEMBL
A0A0P7ZR88_9RHOB
321
33000
TrEMBL
A0A143QSN1_9NOCA
318
34007
TrEMBL
A0A0P1GCR1_9RHOB
320
35105
TrEMBL
A0A0M6YE22_9RHOB
300
31552
TrEMBL
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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
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