UniProt functional annotation for Q60176

UniProt code: Q60176.

Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
Taxonomy: Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus.
 
Function: Catalyzes the reversible oxidation of (S)-malate and (S)- sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruvate, nor alpha-ketoglutarate. {ECO:0000269|PubMed:10850983, ECO:0000269|PubMed:10998181, ECO:0000269|PubMed:19555779}.
 
Catalytic activity: Reaction=a (2S)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH; Xref=Rhea:RHEA:34555, ChEBI:CHEBI:15378, ChEBI:CHEBI:35179, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58123; EC=1.1.1.375; Evidence={ECO:0000269|PubMed:10850983, ECO:0000269|PubMed:10998181, ECO:0000269|PubMed:19555779};
Catalytic activity: Reaction=a (2S)-2-hydroxycarboxylate + NADP(+) = a 2-oxocarboxylate + H(+) + NADPH; Xref=Rhea:RHEA:42768, ChEBI:CHEBI:15378, ChEBI:CHEBI:35179, ChEBI:CHEBI:57783, ChEBI:CHEBI:58123, ChEBI:CHEBI:58349; EC=1.1.1.375; Evidence={ECO:0000269|PubMed:10850983, ECO:0000269|PubMed:10998181, ECO:0000269|PubMed:19555779};
Biophysicochemical properties: Kinetic parameters: KM=0.15 mM for (S)-malate (in the presence of NAD(+)) {ECO:0000269|PubMed:10850983}; KM=0.41 mM for (S)-malate (in the presence of NAD(+)) {ECO:0000269|PubMed:19555779}; KM=0.025 mM for (S)-malate (in the presence of NADP(+)) {ECO:0000269|PubMed:10850983}; KM=0.084 mM for (S)-malate (in the presence of NADP(+)) {ECO:0000269|PubMed:19555779}; KM=4.6 mM for (S)-sulfolactate (in the presence of NADP(+)) {ECO:0000269|PubMed:10850983}; KM=11 mM for (2S,3S)-tartrate (in the presence of NAD(+)) {ECO:0000269|PubMed:19555779}; KM=5.1 mM for (2S,3S)-tartrate (in the presence of NADP(+)) {ECO:0000269|PubMed:19555779}; KM=0.25 mM for oxaloacetate (in the presence of NADH) {ECO:0000269|PubMed:10850983}; KM=0.30 mM for oxaloacetate (in the presence of NADPH) {ECO:0000269|PubMed:10850983}; KM=1.3 mM for sulfopyruvate (in the presence of NADH) {ECO:0000269|PubMed:10850983}; KM=0.19 mM for sulfopyruvate (in the presence of NADPH) {ECO:0000269|PubMed:10850983}; KM=0.14 mM for NADH {ECO:0000269|PubMed:10998181}; KM=0.02 mM for NADPH {ECO:0000269|PubMed:10998181}; Vmax=0.6 umol/min/mg enzyme toward (S)-malate (in the presence of NAD(+)) {ECO:0000269|PubMed:10850983}; Vmax=3 umol/min/mg enzyme toward (S)-malate (in the presence of NADP(+)) {ECO:0000269|PubMed:10850983}; Vmax=3 umol/min/mg enzyme toward (S)-sulfolactate (in the presence of NADP(+)) {ECO:0000269|PubMed:10850983}; Vmax=29 umol/min/mg enzyme toward oxaloacetate (in the presence of NADH) {ECO:0000269|PubMed:10850983}; Vmax=49 umol/min/mg enzyme toward oxaloacetate (in the presence of NADPH) {ECO:0000269|PubMed:10850983}; Vmax=43 umol/min/mg enzyme toward sulfopyruvate (in the presence of NADH) {ECO:0000269|PubMed:10850983}; Vmax=69 umol/min/mg enzyme toward sulfopyruvate (in the presence of NADPH) {ECO:0000269|PubMed:10850983}; Note=kcat is 0.33 sec(-1) for NAD-dependent malate oxidation. kcat is 0.069 sec(-1) for NADP-dependent malate oxidation. {ECO:0000269|PubMed:19555779};
Subunit: Homotetramer. {ECO:0000269|PubMed:10998181, ECO:0000269|PubMed:11292347, ECO:0000269|PubMed:11513609}.
Subcellular location: Cytoplasm.
Similarity: Belongs to the LDH/MDH superfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.