Enzyme

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     1. Oxidoreductases
        1.5 Acting on the CH-NH group of donors
            1.5.1 With NAD+ or NADP+ as acceptor
ID:1.5.1.41
Description:Riboflavin reductase (NAD(P)H).
Alternative Name: Riboflavine mononucleotide reductase.
Riboflavin mononucleotide reductase.
NAD(P)H-dependent FMN reductase.
NAD(P)H(2) dehydrogenase (FMN).
Flavine mononucleotide reductase.
Flavin mononucleotide reductase.
Cath: 3.40.50.80; 2.40.30.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.5.1.41
BRENDA Enzyme Link: BRENDA 1.5.1.41
KEGG Enzyme Link: KEGG1.5.1.41
BioCyc Enzyme Link: BioCyc 1.5.1.41
ExPASy Enzyme Link: ExPASy1.5.1.41
EC2PDB Enzyme Link: EC2PDB 1.5.1.41
ExplorEnz Enzyme Link: ExplorEnz 1.5.1.41
PRIAM enzyme-specific profiles Link: PRIAM 1.5.1.41
IntEnz Enzyme Link: IntEnz 1.5.1.41
MEDLINE Enzyme Link: MEDLINE 1.5.1.41
MSA:

1.5.1.41;

Phylogenetic Tree:

1.5.1.41;

Uniprot:
M-CSA:
RHEA:31455 NAD(+) + reduced riboflavin = 2 H(+) + NADH + riboflavin
RULE(radius=1) [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]:[nH;+0:10]:[c;H0;+0:11]1:[c;H0;+0:12](:[*:13])-[NH;+0:14]-[*:15]:[*:16]-[N;H0;+0:17]-1-[*:18]>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]:[n;H0;+0:10]:[c;H0;+0:11]1:[n;H0;+0:17](-[*:18]):[*:16]:[*:15]:[n;H0;+0:14]:[c;H0;+0:12]-1:[*:13]
Reaction
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References

TitleAuthorsDatePubMed ID
NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase.Fontecave M, Eliasson R, Reichard P1987 Sep 53305505
Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme.Spyrou G, Haggård-Ljungquist E, Krook M, Jörnvall H, Nilsson E, Reichard P1991 Jun2050627
Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli.Ingelman M, Ramaswamy S, Nivière V, Fontecave M, Eklund H1999 Jun 110353815

RHEA:19377 NADP(+) + reduced riboflavin = 2 H(+) + NADPH + riboflavin
RULE(radius=1) [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]:[nH;+0:10]:[c;H0;+0:11]1:[c;H0;+0:12](:[*:13])-[NH;+0:14]-[*:15]:[*:16]-[N;H0;+0:17]-1-[*:18]>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]:[n;H0;+0:10]:[c;H0;+0:11]1:[n;H0;+0:17](-[*:18]):[*:16]:[*:15]:[n;H0;+0:14]:[c;H0;+0:12]-1:[*:13]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Characterization of a second form of NADPH-flavin reductase purified from human erythrocytes.Yubisui T, Tamura M, Takeshita M1987 Jul3453680
NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase.Fontecave M, Eliasson R, Reichard P1987 Sep 53305505
Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme.Spyrou G, Haggård-Ljungquist E, Krook M, Jörnvall H, Nilsson E, Reichard P1991 Jun2050627
Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXbeta reductase (BVR-B).Cunningham O, Gore MG, Mantle TJ2000 Jan 1510620517
Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli.Ingelman M, Ramaswamy S, Nivière V, Fontecave M, Eklund H1999 Jun 110353815