EC number:1.14.15.16

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:1.14.15.16
Description:Vitamin D(3) 24-hydroxylase.
Alternative Name: CYP24A1.
Cath: 1.10.630.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.15.16
BRENDA Enzyme Link: BRENDA 1.14.15.16
KEGG Enzyme Link: KEGG1.14.15.16
BioCyc Enzyme Link: BioCyc 1.14.15.16
ExPASy Enzyme Link: ExPASy1.14.15.16
EC2PDB Enzyme Link: EC2PDB 1.14.15.16
ExplorEnz Enzyme Link: ExplorEnz 1.14.15.16
PRIAM enzyme-specific profiles Link: PRIAM 1.14.15.16
IntEnz Enzyme Link: IntEnz 1.14.15.16
MEDLINE Enzyme Link: MEDLINE 1.14.15.16

EC number:1.14.15.16

MSA:

1.14.15.16;
Phylogenetic Tree:

1.14.15.16;
Uniprot:
M-CSA:
RHEA:24964 calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitetrol + H2O + 2 oxidized [adrenodoxin]
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]
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References

TitleAuthorsDatePubMed ID
Human 25-hydroxyvitamin D3-24-hydroxylase, a multicatalytic enzyme.Beckman MJ, Tadikonda P, Werner E, Prahl J, Yamada S, DeLuca HF1996 Jun 258679605
Kinetic analysis of human CYP24A1 metabolism of vitamin D via the C24-oxidation pathway.Tieu EW, Tang EK, Tuckey RC2014 Jul24893882
Single A326G mutation converts human CYP24A1 from 25-OH-D3-24-hydroxylase into -23-hydroxylase, generating 1alpha,25-(OH)2D3-26,23-lactone.Prosser DE, Kaufmann M, O'Leary B, Byford V, Jones G2007 Jul 3117646648
Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-directed mutagenesis: amino acid residues responsible for species-based difference of CYP24A1 between humans and rats.Hamamoto H, Kusudo T, Urushino N, Masuno H, Yamamoto K, Yamada S, Kamakura M, Ohta M, Inouye K, Sakaki T2006 Jul16617161
Evidence for the activation of 1alpha-hydroxyvitamin D2 by 25-hydroxyvitamin D-24-hydroxylase: delineation of pathways involving 1alpha,24-dihydroxyvitamin D2 and 1alpha,25-dihydroxyvitamin D2.Masuda S, Strugnell SA, Knutson JC, St-Arnaud R, Jones G2006 Feb16516540
Metabolism of vitamin D3 by cytochromes P450.Sakaki T, Kagawa N, Yamamoto K, Inouye K2005 Jan 115574355
Enzymes involved in the activation and inactivation of vitamin D.Prosser DE, Jones G2004 Dec15544953
Metabolism of A-ring diastereomers of 1alpha,25-dihydroxyvitamin D3 by CYP24A1.Kusudo T, Sakaki T, Abe D, Fujishima T, Kittaka A, Takayama H, Hatakeyama S, Ohta M, Inouye K2004 Sep 315358094
Novel metabolism of 1 alpha,25-dihydroxyvitamin D3 with C24-C25 bond cleavage catalyzed by human CYP24A1.Sawada N, Kusudo T, Sakaki T, Hatakeyama S, Hanada M, Abe D, Kamao M, Okano T, Ohta M, Inouye K2004 Apr 2015078099
RHEA:24968 calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = H2O + 2 oxidized [adrenodoxin] + secalciferol
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]
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References

TitleAuthorsDatePubMed ID
Human 25-hydroxyvitamin D3-24-hydroxylase, a multicatalytic enzyme.Beckman MJ, Tadikonda P, Werner E, Prahl J, Yamada S, DeLuca HF1996 Jun 258679605
Kinetic analysis of human CYP24A1 metabolism of vitamin D via the C24-oxidation pathway.Tieu EW, Tang EK, Tuckey RC2014 Jul24893882
Single A326G mutation converts human CYP24A1 from 25-OH-D3-24-hydroxylase into -23-hydroxylase, generating 1alpha,25-(OH)2D3-26,23-lactone.Prosser DE, Kaufmann M, O'Leary B, Byford V, Jones G2007 Jul 3117646648
Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-directed mutagenesis: amino acid residues responsible for species-based difference of CYP24A1 between humans and rats.Hamamoto H, Kusudo T, Urushino N, Masuno H, Yamamoto K, Yamada S, Kamakura M, Ohta M, Inouye K, Sakaki T2006 Jul16617161
Evidence for the activation of 1alpha-hydroxyvitamin D2 by 25-hydroxyvitamin D-24-hydroxylase: delineation of pathways involving 1alpha,24-dihydroxyvitamin D2 and 1alpha,25-dihydroxyvitamin D2.Masuda S, Strugnell SA, Knutson JC, St-Arnaud R, Jones G2006 Feb16516540
Metabolism of vitamin D3 by cytochromes P450.Sakaki T, Kagawa N, Yamamoto K, Inouye K2005 Jan 115574355
Enzymes involved in the activation and inactivation of vitamin D.Prosser DE, Jones G2004 Dec15544953
Metabolism of A-ring diastereomers of 1alpha,25-dihydroxyvitamin D3 by CYP24A1.Kusudo T, Sakaki T, Abe D, Fujishima T, Kittaka A, Takayama H, Hatakeyama S, Ohta M, Inouye K2004 Sep 315358094
Novel metabolism of 1 alpha,25-dihydroxyvitamin D3 with C24-C25 bond cleavage catalyzed by human CYP24A1.Sawada N, Kusudo T, Sakaki T, Hatakeyama S, Hanada M, Abe D, Kamao M, Okano T, Ohta M, Inouye K2004 Apr 2015078099
Dual metabolic pathway of 25-hydroxyvitamin D3 catalyzed by human CYP24.Sakaki T, Sawada N, Komai K, Shiozawa S, Yamada S, Yamamoto K, Ohyama Y, Inouye K2000 Oct11012668
RHEA:24972 calcitetrol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1,25-dihydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin]
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[Fe;H0;+0:6]-[*:7].[*:8]-[Fe;H0;+0:9]-[*:10].[H+;H0:11].[O;H0;+0:12]=[O;H0;+0:13]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[Fe+;H0:6]-[*:7].[*:8]-[Fe+;H0:9]-[*:10].[OH2;+0:12].[OH2;+0:13]
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References

TitleAuthorsDatePubMed ID
Kinetic analysis of human CYP24A1 metabolism of vitamin D via the C24-oxidation pathway.Tieu EW, Tang EK, Tuckey RC2014 Jul24893882
Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-directed mutagenesis: amino acid residues responsible for species-based difference of CYP24A1 between humans and rats.Hamamoto H, Kusudo T, Urushino N, Masuno H, Yamamoto K, Yamada S, Kamakura M, Ohta M, Inouye K, Sakaki T2006 Jul16617161
Enzymes involved in the activation and inactivation of vitamin D.Prosser DE, Jones G2004 Dec15544953
Metabolism of A-ring diastereomers of 1alpha,25-dihydroxyvitamin D3 by CYP24A1.Kusudo T, Sakaki T, Abe D, Fujishima T, Kittaka A, Takayama H, Hatakeyama S, Ohta M, Inouye K2004 Sep 315358094
RHEA:24976 (1S)-1,25-dihydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1,23,25-trihydroxy-24-oxocalciol + H2O + 2 oxidized [adrenodoxin]
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]-[N;H0;+0:5]1-[CH;+0:6]=[C;H0;+0:7](-[*:8])-[CH2;+0:9]-[CH;+0:10]=[CH;+0:11]-1.[H+;H0:12].[O;H0;+0:13]=[O;H0;+0:14]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:13].[*:4]-[n+;H0:5]1:[cH;+0:6]:[c;H0;+0:7](-[*:8]):[cH;+0:9]:[cH;+0:10]:[cH;+0:11]:1.[OH2;+0:14]
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References

TitleAuthorsDatePubMed ID
Kinetic analysis of human CYP24A1 metabolism of vitamin D via the C24-oxidation pathway.Tieu EW, Tang EK, Tuckey RC2014 Jul24893882
Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-directed mutagenesis: amino acid residues responsible for species-based difference of CYP24A1 between humans and rats.Hamamoto H, Kusudo T, Urushino N, Masuno H, Yamamoto K, Yamada S, Kamakura M, Ohta M, Inouye K, Sakaki T2006 Jul16617161
Enzymes involved in the activation and inactivation of vitamin D.Prosser DE, Jones G2004 Dec15544953
Metabolism of A-ring diastereomers of 1alpha,25-dihydroxyvitamin D3 by CYP24A1.Kusudo T, Sakaki T, Abe D, Fujishima T, Kittaka A, Takayama H, Hatakeyama S, Ohta M, Inouye K2004 Sep 315358094
RHEA:24984 (1S)-1,23-dihydroxy-24,25,26,27-tetranorcalciol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1-hydroxy-23-oxo-24,25,26,27-tetranorcalciol + 2 H2O + 2 oxidized [adrenodoxin]
RULE(radius=1) [*:1]-[CH2;+0:2]-[OH;+0:3].[*: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]=[O;H0;+0:3].[*:4]-[Fe+;H0:5]-[*:6].[*:7]-[Fe+;H0:8]-[*:9].[OH2;+0:12].[OH2;+0:13]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Kinetic analysis of human CYP24A1 metabolism of vitamin D via the C24-oxidation pathway.Tieu EW, Tang EK, Tuckey RC2014 Jul24893882
Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-directed mutagenesis: amino acid residues responsible for species-based difference of CYP24A1 between humans and rats.Hamamoto H, Kusudo T, Urushino N, Masuno H, Yamamoto K, Yamada S, Kamakura M, Ohta M, Inouye K, Sakaki T2006 Jul16617161
Enzymes involved in the activation and inactivation of vitamin D.Prosser DE, Jones G2004 Dec15544953
Metabolism of A-ring diastereomers of 1alpha,25-dihydroxyvitamin D3 by CYP24A1.Kusudo T, Sakaki T, Abe D, Fujishima T, Kittaka A, Takayama H, Hatakeyama S, Ohta M, Inouye K2004 Sep 315358094
RHEA:24988 (1S)-1-hydroxy-23-oxo-24,25,26,27-tetranorcalciol + H(+) + O2 + 2 reduced [adrenodoxin] = calcitroate + H2O + 2 oxidized [adrenodoxin]
RULE(radius=1) [*:1]-[Fe;H0;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]=[CH;+0:8]-[*:9].[H+;H0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:1]-[Fe+;H0:2]-[*:3].[*:4]-[Fe+;H0:5]-[*:6].[*:7]=[C;H0;+0:8](-[*:9])-[OH;+0:11].[OH2;+0:12]
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References

TitleAuthorsDatePubMed ID
Kinetic analysis of human CYP24A1 metabolism of vitamin D via the C24-oxidation pathway.Tieu EW, Tang EK, Tuckey RC2014 Jul24893882
Enzymes involved in the activation and inactivation of vitamin D.Prosser DE, Jones G2004 Dec15544953
Metabolism of A-ring diastereomers of 1alpha,25-dihydroxyvitamin D3 by CYP24A1.Kusudo T, Sakaki T, Abe D, Fujishima T, Kittaka A, Takayama H, Hatakeyama S, Ohta M, Inouye K2004 Sep 315358094