KEGG   ENZYME: 1.1.1.337
Entry
EC 1.1.1.337                Enzyme                                 

Name
L-2-hydroxycarboxylate dehydrogenase (NAD+);
(R)-sulfolactate:NAD+ oxidoreductase;
L-sulfolactate dehydrogenase;
(R)-sulfolactate dehydrogenase;
L-2-hydroxyacid dehydrogenase (NAD+);
ComC
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
(2S)-2-hydroxycarboxylate:NAD+ oxidoreductase
Reaction(IUBMB)
a (2S)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+ [RN:R10189]
Reaction(KEGG)
R10189 > R07136
Substrate
(2S)-2-hydroxycarboxylate [CPD:C15565];
NAD+ [CPD:C00003]
Product
2-oxocarboxylate [CPD:C00161];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate [3]. Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.
History
EC 1.1.1.337 created 2012
Pathway
ec00680  Methane metabolism
ec01100  Metabolic pathways
Orthology
K05884  L-2-hydroxycarboxylate dehydrogenase (NAD+)
Genes
VSH: BSZ05_08715
CNC: CNE_BB1p05710(comC)
CUH: BJN34_35490
BGP: BGL_2c13900
BPLA: bpln_2g14680
PNR: AT302_16585
BFZ: BAU07_07535 BAU07_19930
PUS: CKA81_13830
PIG: EGT29_10430
LIM: L103DPR2_01654(yjmC)
BPRC: D521_0584
SMER: DU99_24705
SFH: SFHH103_06683(mdh)
SHZ: shn_26825
MET: M446_3591
MMED: Mame_04860(yjmC_2)
OTM: OSB_08100(yjmC)
LRT: LRI_1196
THL: TEH_05010(mdh)
CRN: CAR_c14810(mdh)
CAE: SMB_G0579(mdh)
CAY: CEA_G0580
CLJ: CLJU_c05920(mdh)
CPAS: Clopa_1152
CPAT: CLPA_c31190(mdh)
CPAE: CPAST_c31190(mdh)
CTYK: CTK_C26970(mdh)
RUM: CK1_39560
CCT: CC1_29650
ROB: CK5_14170
BPRO: PMF13cell1_03197(yjmC_2)
EAC: EAL2_808p02730(mdh)
AWO: Awo_c16770(mdh)
CBAR: PATL70BA_1096(mdh)
TAE: TepiRe1_1949(mdh)
SLE: sle_01170(sle_01170)
SGE: DWG14_06080(dpkA)
OLS: Olsu_0270
HSW: Hsw_3558
CACI: CLOAM1159(mdh)
MINF: MESINF_0035(mdh) MESINF_1540(mdh)
BANA: BARAN1_1319(mdh)
MJA: MJ_1425
MMP: MMP1133(comC)
MMD: GYY_06515
MMAK: MMKA1_13120(comC)
MMAO: MMOS7_12420(comC)
MMAD: MMJJ_17120(yjmC)
MAE: Maeo_1015
MVO: Mvol_0905
MTH: MTH_1205
MMG: MTBMA_c15830(comC)
METC: MTCT_1098
MWO: MWSIV6_1598(comC)
METE: tca_01162(yjmC)
MST: Msp_0279(comC)
MRU: mru_1980(comC)
MSI: Msm_1040
MEB: Abm4_1552(comC)
MMIL: sm9_2052(comC)
MEYE: TL18_09445
MOL: YLM1_1417
METH: MBMB1_1726(comC)
MFC: BRM9_0342(comC)
MFI: DSM1535_0956(comC)
MCUB: MCBB_2038(comC)
MFV: Mfer_0389
MKA: MK0392(comC)
STO: STK_20900
STEP: IC006_0144
LOKI: Lokiarch_23620(mdh_3) Lokiarch_23630(mdh_4)
PSYT: DSAG12_01758(mdh)
 » show all
Reference
1  [PMID:10850983]
  Authors
Graupner M, Xu H, White RH.
  Title
Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea.
  Journal
J Bacteriol 182:3688-92 (2000)
DOI:10.1128/JB.182.13.3688-3692.2000
  Sequence
[mja:MJ_1425]
Reference
2  [PMID:11451450]
  Authors
Graupner M, White RH.
  Title
The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea.
  Journal
Biochim Biophys Acta 1548:169-73 (2001)
DOI:10.1016/S0167-4838(01)00220-5
  Sequence
[mja:MJ_1425]
Reference
3  [PMID:12013276]
  Authors
Graham DE, White RH.
  Title
Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics.
  Journal
Nat Prod Rep 19:133-47 (2002)
DOI:10.1039/b103714p
Reference
4  [PMID:15758220]
  Authors
Rein U, Gueta R, Denger K, Ruff J, Hollemeyer K, Cook AM.
  Title
Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA.
  Journal
Microbiology 151:737-47 (2005)
DOI:10.1099/mic.0.27548-0
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.337
IUBMB Enzyme Nomenclature: 1.1.1.337
ExPASy - ENZYME nomenclature database: 1.1.1.337
BRENDA, the Enzyme Database: 1.1.1.337
CAS: 81210-65-3

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