KEGG   ENZYME: 1.14.14.57Help
Entry
EC 1.14.14.57               Enzyme                                 

Name
taurochenodeoxycholate 6alpha-hydroxylase;
CYP3A4;
CYP4A21;
taurochenodeoxycholate 6alpha-monooxygenase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
taurochenodeoxycholate,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (6alpha-hydroxylating)
Reaction(IUBMB)
(1) taurochenodeoxycholate + [reduced NADPH---hemoprotein reductase] + O2 = taurohyocholate + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R07205];
(2) lithocholate + [reduced NADPH---hemoprotein reductase] + O2 = hyodeoxycholate + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R07206]
Reaction(KEGG)
Substrate
taurochenodeoxycholate [CPD:C05465];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007];
lithocholate [CPD:C03990]
Product
taurohyocholate [CPD:C15516];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001];
hyodeoxycholate [CPD:C15517]
Comment
A cytochrome P-450 (heme-thiolate) protein. Requires cytochrome b5 for maximal activity. Acts on taurochenodeoxycholate, taurodeoxycholate and less readily on lithocholate and chenodeoxycholate. In adult pig (Sus scrofa), hyocholic acid replaces cholic acid as a primary bile acid [5].
History
EC 1.14.14.57 created 2005 asEC 1.14.13.97, transferred 2018 to EC 1.14.14.57
Orthology
K17689  cytochrome P450 family 3 subfamily A polypeptide 4
K18228  taurochenodeoxycholate 6alpha-hydroxylase
Genes
HSA: 1576(CYP3A4)
PTR: 463582(CYP3A4)
PPS: 100976899
GGO: 101149513
PON: 100436782
NLE: 100593175
MCC: 678670(CYP3A4)
MCF: 102144258(CYP3A8)
CSAB: 103246766
RRO: 104673585
RBB: 108538168
TUP: 102494214
CFA: 479740(CYP3A4)
SSC: 403327(CYP4A21)
 » show all
Taxonomy
Reference
1  [PMID:10216279]
  Authors
Araya Z, Wikvall K.
  Title
6alpha-hydroxylation of taurochenodeoxycholic acid and lithocholic acid by CYP3A4 in human liver microsomes.
  Journal
Biochim Biophys Acta 1438:47-54 (1999)
DOI:10.1016/S1388-1981(99)00031-1
  Sequence
[hsa:1576]
Reference
2  [PMID:7649186]
  Authors
Araya Z, Hellman U, Hansson R.
  Title
Characterisation of taurochenodeoxycholic acid 6 alpha-hydroxylase from pig liver microsomes.
  Journal
Eur J Biochem 231:855-61 (1995)
DOI:10.1111/j.1432-1033.1995.0855d.x
  Sequence
[ssc:403327]
Reference
3  [PMID:11069906]
  Authors
Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G, Corsiero D, Girbig F, Konig W, Weyland C.
  Title
Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
  Journal
J Biol Chem 276:7291-301 (2001)
DOI:10.1074/jbc.M006877200
Reference
4  [PMID:11113117]
  Authors
Lundell K, Hansson R, Wikvall K.
  Title
Cloning and expression of a pig liver taurochenodeoxycholic acid 6alpha-hydroxylase (CYP4A21): a novel member of the CYP4A subfamily.
  Journal
J Biol Chem 276:9606-12 (2001)
DOI:10.1074/jbc.M006584200
  Sequence
[ssc:403327]
Reference
5  [PMID:14643796]
  Authors
Lundell K, Wikvall K.
  Title
Gene structure of pig sterol 12alpha-hydroxylase (CYP8B1) and expression in fetal liver: comparison with expression of taurochenodeoxycholic acid 6alpha-hydroxylase (CYP4A21).
  Journal
Biochim Biophys Acta 1634:86-96 (2003)
DOI:10.1016/j.bbalip.2003.09.002
Reference
6  [PMID:12543708]
  Authors
Russell DW.
  Title
The enzymes, regulation, and genetics of bile acid synthesis.
  Journal
Annu Rev Biochem 72:137-74 (2003)
DOI:10.1146/annurev.biochem.72.121801.161712
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.57
IUBMB Enzyme Nomenclature: 1.14.14.57
ExPASy - ENZYME nomenclature database: 1.14.14.57
BRENDA, the Enzyme Database: 1.14.14.57
CAS: 105669-85-0
LinkDB All DBs

DBGET integrated database retrieval system