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Literature summary extracted from

  • Zhang, Y.; Schofield, L.R.; Sang, C.; Dey, D.; Ronimus, R.S.
    Expression, purification, and characterization of (R)-sulfolactate dehydrogenase (ComC) from the rumen methanogen Methanobrevibacter millerae SM9 (2017), Archaea, 2017, 5793620 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.337 sulfopyruvate possible substrate inhibition at 0.60 mM Methanobrevibacter millerae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.337 additional information
-
 additional information typical Michaelis-Menten kinetics, comparison to ComC enzymes from other rumen methanogens from Methanobrevibacter Methanobrevibacter millerae
1.1.1.337 0.0551
-
 NADH pH 6.5, 37°C Methanobrevibacter millerae
1.1.1.337 0.196
-
 sulfopyruvate pH 6.5, 37°C Methanobrevibacter millerae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.337 KCl required Methanobrevibacter millerae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.337 sulfopyruvate + NADH + H+ Methanobrevibacter millerae
-
 sulfo-2-hydroxypropanoate + NAD+
-
 r
1.1.1.337 sulfopyruvate + NADH + H+ Methanobrevibacter millerae SM9
-
 sulfo-2-hydroxypropanoate + NAD+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.337 Methanobrevibacter millerae A0A0U3EA38
-
-
1.1.1.337 Methanobrevibacter millerae SM9 A0A0U3EA38
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.337 2-oxoglutarate + NADH + H+ 0.2% activity compared to sulfopyruvate Methanobrevibacter millerae 2-hydroxyglutarate + NAD+
-
 r
1.1.1.337 2-oxoglutarate + NADH + H+ 0.2% activity compared to sulfopyruvate Methanobrevibacter millerae SM9 2-hydroxyglutarate + NAD+
-
 r
1.1.1.337 oxaloacetate + NADH + H+ 31% activity compared to sulfopyruvate Methanobrevibacter millerae malate + NAD+
-
 r
1.1.1.337 oxaloacetate + NADH + H+ 31% activity compared to sulfopyruvate Methanobrevibacter millerae SM9 malate + NAD+
-
 r
1.1.1.337 sulfopyruvate + NADH + H+
-
 Methanobrevibacter millerae sulfo-2-hydroxypropanoate + NAD+
-
 r
1.1.1.337 sulfopyruvate + NADH + H+ preferred substrate Methanobrevibacter millerae sulfo-2-hydroxypropanoate + NAD+
-
 r
1.1.1.337 sulfopyruvate + NADH + H+
-
 Methanobrevibacter millerae SM9 sulfo-2-hydroxypropanoate + NAD+
-
 r
1.1.1.337 sulfopyruvate + NADH + H+ preferred substrate Methanobrevibacter millerae SM9 sulfo-2-hydroxypropanoate + NAD+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.337 (R)-sulfolactate dehydrogenase
-
 Methanobrevibacter millerae
1.1.1.337 ComC
-
 Methanobrevibacter millerae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.337 37
-
 assay at Methanobrevibacter millerae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.337 48.9
-
 NADH pH 6.5, 37°C Methanobrevibacter millerae
1.1.1.337 62.8
-
 sulfopyruvate pH 6.5, 37°C Methanobrevibacter millerae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.337 6.5
-
 assay at Methanobrevibacter millerae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.337 additional information ComC shows less than 1% specific activity in the reduction reaction with NADPH compared to NADH. ComC which shows a 5fold lower KM for sulfopyruvate in the presence of NADH compared to NADPH (0.055 mM and 0.21 mM, resp.) and a 60fold higher Vmax/KM Methanobrevibacter millerae
1.1.1.337 NAD+
-
 Methanobrevibacter millerae
1.1.1.337 NADH
-
 Methanobrevibacter millerae

General Information

EC Number General Information Comment Organism
1.1.1.337 evolution the enzyme ComC belongs to the LDH2/MDH2 oxidoreductase family Methanobrevibacter millerae
1.1.1.337 metabolism the enzyme is involved in the coenzyme M biosynthesis pathway. Coenzyme M is required for methanogenesis to occur Methanobrevibacter millerae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.337 320.4
-
 sulfopyruvate pH 6.5, 37°C Methanobrevibacter millerae
1.1.1.337 887.5
-
 NADH pH 6.5, 37°C Methanobrevibacter millerae