BRENDA - Enzyme Database

The Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) from Vibrio cholerae enhances insertion of FeS in overproduced NqrF subunit

Tao, M.; Fritz, G.; Steuber, J.; J. Inorg. Biochem. 102, 1366-1372 (2008)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
7.2.1.1
additional information
a soluble variant of NqrF lacking its hydrophobic, N-terminal helix (NqrF') is produced in Vibrio cholerae wild type and nqr deletion strain. Under identical conditions of growth and induction, the yield of NqrF' increased by 30% in the presence of the Na+-NQR. FAD-containing NqrF' species with or without the FeS cluster are observed, indicating that assembly of the FeS center, but not insertion of the flavin cofactor, is limited during overproduction in Vibrio cholerae. NqrF' lacking the [2Fe–2S] cluster is less stable, partially unfolded, and therefore prone to proteolytic degradation in Vibrio cholerae
Vibrio cholerae
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
7.2.1.1
membrane
bound to
Vibrio cholerae
16020
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
7.2.1.1
Fe
the NqrF subunit contains one FAD and a [2Fe–2S] cluster and catalyzes the initial oxidation of NADH. The Na+-NQR is proposed to increase the stability of NqrF' by stimulating the maturation of FeS centers
Vibrio cholerae
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
7.2.1.1
Vibrio cholerae
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7.2.1.1
NADH + H+ + ubiquinone-1
the NqrF subunit catalyzes the initial oxidation of NADH
699385
Vibrio cholerae
NAD+ + ubiquinol-1
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
7.2.1.1
FAD
the NqrF subunit contains one FAD and a [2Fe–2S] cluster and catalyzes the initial oxidation of NADH
Vibrio cholerae
7.2.1.1
NADH
-
Vibrio cholerae
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
7.2.1.1
FAD
the NqrF subunit contains one FAD and a [2Fe–2S] cluster and catalyzes the initial oxidation of NADH
Vibrio cholerae
7.2.1.1
NADH
-
Vibrio cholerae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
7.2.1.1
additional information
a soluble variant of NqrF lacking its hydrophobic, N-terminal helix (NqrF') is produced in Vibrio cholerae wild type and nqr deletion strain. Under identical conditions of growth and induction, the yield of NqrF' increased by 30% in the presence of the Na+-NQR. FAD-containing NqrF' species with or without the FeS cluster are observed, indicating that assembly of the FeS center, but not insertion of the flavin cofactor, is limited during overproduction in Vibrio cholerae. NqrF' lacking the [2Fe–2S] cluster is less stable, partially unfolded, and therefore prone to proteolytic degradation in Vibrio cholerae
Vibrio cholerae
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
7.2.1.1
membrane
bound to
Vibrio cholerae
16020
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
7.2.1.1
Fe
the NqrF subunit contains one FAD and a [2Fe–2S] cluster and catalyzes the initial oxidation of NADH. The Na+-NQR is proposed to increase the stability of NqrF' by stimulating the maturation of FeS centers
Vibrio cholerae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7.2.1.1
NADH + H+ + ubiquinone-1
the NqrF subunit catalyzes the initial oxidation of NADH
699385
Vibrio cholerae
NAD+ + ubiquinol-1
-
-
-
?