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Literature summary for 1.3.1.6 extracted from

  • Bertsova, Y.; Oleynikov, I.; Bogachev, A.
    A new water-soluble bacterial NADH fumarate oxidoreductase (2020), FEMS Microbiol. Lett., 367, fnaa175 .
    View publication on PubMed
Search for more literature for 1.3.1.6

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae B5XRB0
-
-
Klebsiella pneumoniae 342 B5XRB0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fumarate + NADH + H+
-
 Klebsiella pneumoniae succinate + NAD+
-
 ?
fumarate + NADH + H+
-
 Klebsiella pneumoniae 342 succinate + NAD+
-
 ?

Synonyms

Synonyms Comment Organism
KPK_2907
-
 Klebsiella pneumoniae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 6.5 oxidation of NADH Klebsiella pneumoniae

Cofactor

Cofactor Comment Organism Structure
FMN
-
 Klebsiella pneumoniae
additional information no cofactor: NADPH Klebsiella pneumoniae
NADH NADH is an inherent electron donor for the enzyme Klebsiella pneumoniae

Expression

Organism Comment Expression
Klebsiella pneumoniae induction of FRD synthesis is observed only under anaerobic conditions in the presence of fumarate or malate up

General Information

General Information Comment Organism
physiological function aerobic incubation of FRD with NADH results in O2 consumption. Fumarate reductase activity of FRD significantly exceeds its NADH dehydrogenase activity. During the catalysis of NADH:fumarate oxidoreductase reaction, FRD turnover is limited by a very low rate (about 10/s) of electron transfer between the noncovalently and covalently bound FMN moieties Klebsiella pneumoniae