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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 PubMedView publication on EuropePMC

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