KEGG   ENZYME: 1.1.1.310
Entry
EC 1.1.1.310                Enzyme                                 
Name
(S)-sulfolactate dehydrogenase;
(2S)-3-sulfolactate dehydrogenase;
SlcC
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
(2S)-sulfolactate:NAD+ oxidoreductase
Reaction(IUBMB)
(2S)-3-sulfolactate + NAD+ = 3-sulfopyruvate + NADH + H+ [RN:R05693]
Reaction(KEGG)
R05693
Substrate
(2S)-3-sulfolactate [CPD:C11499];
NAD+ [CPD:C00003]
Product
3-sulfopyruvate [CPD:C05528];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
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+.
History
EC 1.1.1.310 created 2011, modified 2013
Pathway
ec00270  Cysteine and methionine metabolism
ec01100  Metabolic pathways
Orthology
K16843  (S)-sulfolactate dehydrogenase
Genes
SHAILMH63_10850
APRSBI364_08725
CSACsal_1770
HBEBEI_0838(slcC)
SVASVA_1860
RPJN234_02635
CUHBJN34_26760
REUReut_B3530
CTIRALTA_B0841(serA2)
CBWRR42_m0458
CGDCR3_0183(slcC)
COXE0W60_13290
CCAXKZ686_04915
CNANA2G96_27605
BXEBxe_B1896
BXBDR64_7205
PGISI6I06_21470
PACSFAZ98_25215
PANIDCO16_04965
PWUA8O14_02435
PTXABW99_10895
CABASBC2_17580(slcC)
TVLFAZ95_15405
BPTBpet0409(serA2)
BBROBAU06_18080
BFZBAU07_08200
BOHAKI39_17275
BGMCAL15_02265
BGVCAL12_19020
AXYAXYL_00471(serA1)
AXONH44784_017141
AXNAX27061_0477
AXXERS451415_00471(serA_1)
ADTAPT56_02490
AISBUW96_28015
ASWCVS48_11545
ACHRC2U31_07140
ADYHLG70_19610
ACHOH4P35_02080
AMUIPE062_26090
APESFOC84_10145
AAEGRA224_02315
AKATKWG_23305
AMIMMIM_c37610(serA2)
PARKLSG25_12710
VEIVeis_0891
VAPVapar_3820
VPDVAPA_1c39330
CKEB5M06_01520
ATERMW290_18645
HARHEAR3340
ACTBRHM62_14995
URUDSM104443_02184(slcC)
UPLDSM104440_02014(slcC)
ACOMCEW83_08350
BEBABWI17_15940
MESOBSQ44_12890
CHEAPVE73_02265
NIYFQ775_22315
KMNHW532_06430
EMXFKV68_25170
KAIK32_36520
OCAOCAR_7552
OCGOCA5_c05880(serA1)
OCOOCA4_c05870(serA1)
PCAXAFIC_002274
BOPAXW83_05585
BOSBSY19_2611
BVVBHK69_18040
BOIBLM15_06700
BOFFQV39_07605
BVESQO058_00755
MRDMrad2831_4214 Mrad2831_5977
METM446_6454
MORMOC_4868
MPHYMCBMB27_03728
METXA3862_10280
METIDK427_02130
MMESMMSR116_04765
MTADM6G65_25990
RVARvan_3575
RLACQMO75_13560
FILBN1229_v1_1881(slcC)
FIYBN1229_v1_1884(slcC)
CMETK6K41_04850
AUBLXB15_20875
LABPFJ695_09905
PSTGE8M01_21825
PAQTE8L99_13585
DSHDshi_1001(serA2)
TPROGa0080559_TMP3623
PSEWJHW44_18570
PAEXJHW48_16240
PFEOE3U26_14700
RSUNHU_04238
RHMB5V46_17730
RBGBG454_02465
POZI0K15_15000
CMAGCBW24_05860
ACIMGT370_19975
AZLAZL_004920(serA)
ALIAZOLI_0344
ATIAL072_01935
AHUA6A40_01385
AZMDM194_01050
AZSE6C72_06400
NCBC0V82_01490
SKTIGS68_14035
SMUCJL100_013875
SROEJL101_013570
VSUP3M64_05645
ELIOKO353_01270
TMURJBF11_07060
DMPFAK_06040
BACAFAY30_23715
BONA361_10255
HMNHM131_18630
LAOAOX59_17370
AQTFN924_15335
SCIAHUG15_20685
NMKCHR53_24465
PSABPSAB_19150
PBJVN24_05940
AFXJZ786_10480 JZ786_13645
ACURJZ785_23000
ADAUNZD86_03685
EFFskT53_05870
NTRB0W44_06085
DRUDesru_0084 Desru_1692
DKUDesku_0182
TMRTmar_1044
THEFE1B22_08885
THEPDYI95_005190
SAYTPY_1961(serA) TPY_2384(serA)
SAPSulac_2157 Sulac_3141
STHRBXT84_07540
STEDSPTER_32830(slcC)
RHARHA1_ro08844(serA3)
RKOJWS14_47745
MPHMLP_21630
AMAZLUW76_22385
ACTQOG417_30925
PLANA1s21148_06280
PVNA7sIIA15_00850
MRBMrub_2461
MREK649_10225
MTAIMtai_v1c20760
MSVMesil_1013
GMRGmarT_17400(serA_3)
GIMF1728_06080
GPNPan110_17230(serA_3)
 » show all
Reference
1  [PMID:20007648]
  Authors
Denger K, Cook AM
  Title
Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase.
  Journal
Microbiology 156:967-74 (2010)
DOI:10.1099/mic.0.034736-0
  Sequence
[csa:Csal_1770]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.310
IUBMB Enzyme Nomenclature: 1.1.1.310
ExPASy - ENZYME nomenclature database: 1.1.1.310
BRENDA, the Enzyme Database: 1.1.1.310

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