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Literature summary for 1.1.1.337 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 PubMed
Search for more literature for 1.1.1.337

Inhibitors

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
KCl required Methanobrevibacter millerae

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Methanobrevibacter millerae A0A0U3EA38
-
-
Methanobrevibacter millerae SM9 A0A0U3EA38
-
-

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
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
NAD+
-
 Methanobrevibacter millerae
NADH
-
 Methanobrevibacter millerae

General Information

General Information Comment Organism
evolution the enzyme ComC belongs to the LDH2/MDH2 oxidoreductase family Methanobrevibacter millerae
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]

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