Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.15.22
Description:Vitamin D 1,25-hydroxylase.
Alternative Name: CYP105A1.
Cath: 1.10.630.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.15.22
BRENDA Enzyme Link: BRENDA 1.14.15.22
KEGG Enzyme Link: KEGG1.14.15.22
BioCyc Enzyme Link: BioCyc 1.14.15.22
ExPASy Enzyme Link: ExPASy1.14.15.22
EC2PDB Enzyme Link: EC2PDB 1.14.15.22
ExplorEnz Enzyme Link: ExplorEnz 1.14.15.22
PRIAM enzyme-specific profiles Link: PRIAM 1.14.15.22
IntEnz Enzyme Link: IntEnz 1.14.15.22
MEDLINE Enzyme Link: MEDLINE 1.14.15.22
MSA:

1.14.15.22;

Phylogenetic Tree:

1.14.15.22;

Uniprot:
M-CSA:
RHEA:50700 calcidiol + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = calcitriol + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[Fe;H0;+0:8]-[*:9].[H+;H0:10].[H+;H0:11].[O;H0;+0:12]=[O;H0;+0:13]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:12].[*:4]-[Fe+;H0:5]-[*:6].[*:7]-[Fe+;H0:8]-[*:9].[OH2;+0:13]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Structure-based design of a highly active vitamin D hydroxylase from Streptomyces griseolus CYP105A1.Hayashi K, Sugimoto H, Shinkyo R, Yamada M, Ikeda S, Ikushiro S, Kamakura M, Shiro Y, Sakaki T2008 Nov 1818937506
Crystal structure of CYP105A1 (P450SU-1) in complex with 1alpha,25-dihydroxyvitamin D3.Sugimoto H, Shinkyo R, Hayashi K, Yoneda S, Yamada M, Kamakura M, Ikushiro S, Shiro Y, Sakaki T2008 Apr 118314962
Conversion of vitamin D3 to 1alpha,25-dihydroxyvitamin D3 by Streptomyces griseolus cytochrome P450SU-1.Sawada N, Sakaki T, Yoneda S, Kusudo T, Shinkyo R, Ohta M, Inouye K2004 Jul 1615207715

RHEA:50696 calciol + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = calcidiol + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[*:4].[*:5]-[Fe;H0;+0:6]-[*:7].[*:8]-[Fe;H0;+0:9]-[*:10].[H+;H0:11].[H+;H0:12].[O;H0;+0:13]=[O;H0;+0:14]>>[*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:13].[*:5]-[Fe+;H0:6]-[*:7].[*:8]-[Fe+;H0:9]-[*:10].[OH2;+0:14]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Structure-based design of a highly active vitamin D hydroxylase from Streptomyces griseolus CYP105A1.Hayashi K, Sugimoto H, Shinkyo R, Yamada M, Ikeda S, Ikushiro S, Kamakura M, Shiro Y, Sakaki T2008 Nov 1818937506
Crystal structure of CYP105A1 (P450SU-1) in complex with 1alpha,25-dihydroxyvitamin D3.Sugimoto H, Shinkyo R, Hayashi K, Yoneda S, Yamada M, Kamakura M, Ikushiro S, Shiro Y, Sakaki T2008 Apr 118314962
Conversion of vitamin D3 to 1alpha,25-dihydroxyvitamin D3 by Streptomyces griseolus cytochrome P450SU-1.Sawada N, Sakaki T, Yoneda S, Kusudo T, Shinkyo R, Ohta M, Inouye K2004 Jul 1615207715