KEGG ENZYME: 1.14.15.8

ENZYME: 1.14.15.8

Entry

EC 1.14.15.8                Enzyme

Name

steroid 15beta-monooxygenase;
cytochrome P-450meg;
cytochrome P450meg;
steroid 15beta-hydroxylase;
CYP106A2;
BmCYP106A2

Class

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor

Sysname

progesterone,reduced-ferredoxin:oxygen oxidoreductase (15beta-hydroxylating)

Reaction(IUBMB)

progesterone + 2 reduced [2Fe-2S] ferredoxin + O2 = 15beta-hydroxyprogesterone + 2 oxidized [2Fe-2S] ferredoxin + H2O [RN:R09587]

Reaction(KEGG)

R09587

Substrate

progesterone [CPD:C00410];
reduced [2Fe-2S] ferredoxin [CPD:C22150];
O2 [CPD:C00007]

Product

15beta-hydroxyprogesterone [CPD:C19726];
oxidized [2Fe-2S] ferredoxin [CPD:C22151];
H2O [CPD:C00001]

Comment

The enzyme from the bacterium Bacillus megaterium hydroxylates a variety of 3-oxo-Delta4-steroids in position 15beta. Ring A-reduced, aromatic, and 3beta-hydroxy-Delta4-steroids do not serve as substrates [2].

History

EC 1.14.15.8 created 2010

Orthology

K21114

steroid 15beta-monooxygenase

Genes

BSJ:	UP17_19080

BMUR:

ABE28_017965

PBUT:

DTO10_05970

PFRI:

L8956_19730

Reference

1 [PMID:109432]

Authors

Berg A, Ingelman-Sundberg M, Gustafsson JA

Title

Purification and characterization of cytochrome P-450meg.

Journal

J Biol Chem 254:5264-71 (1979)

Reference

2 [PMID:177422]

Authors

Berg A, Gustafsson JA, Ingelman-Sundberg M

Title

Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium.

Journal

J Biol Chem 251:2831-8 (1976)

Reference

3 [PMID:15178459]

Authors

Lisurek M, Kang MJ, Hartmann RW, Bernhardt R

Title

Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry.

Journal

Biochem Biophys Res Commun 319:677-82 (2004)
DOI:10.1016/j.bbrc.2004.05.037

Sequence

[ag:CAA79985]

Reference

4 [PMID:19635596]

Authors

Goni G, Zollner A, Lisurek M, Velazquez-Campoy A, Pinto S, Gomez-Moreno C, Hannemann F, Bernhardt R, Medina M

Title

Cyanobacterial electron carrier proteins as electron donors to CYP106A2 from Bacillus megaterium ATCC 13368.

Journal

Biochim Biophys Acta 1794:1635-42 (2009)
DOI:10.1016/j.bbapap.2009.07.012

Reference

5 [PMID:18481342]

Authors

Lisurek M, Simgen B, Antes I, Bernhardt R

Title

Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation.

Journal

Chembiochem 9:1439-49 (2008)
DOI:10.1002/cbic.200700670

Sequence

[ag:CAA79985]

Other DBs

ExplorEnz - The Enzyme Database:

1.14.15.8

IUBMB Enzyme Nomenclature:

1.14.15.8

ExPASy - ENZYME nomenclature database:

1.14.15.8

BRENDA, the Enzyme Database:

1.14.15.8

All links

Chemical substance (6)   
   KEGG COMPOUND (6)   
Chemical reaction (2)   
   KEGG REACTION (1)   
   KEGG RCLASS (1)   
Gene (6)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (5)   
Protein sequence (6)   
   UniProt (1)   
   SWISS-PROT (1)   
   PDBSTR (4)   
3D Structure (2)   
   PDB (2)   
Protein domain (4)   
   InterPro (4)   
All databases (26)   

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