| Entry |
|
|---|
| Name |
cholestanetriol 26-monooxygenase;
5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase;
5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase;
cholestanetriol 26-hydroxylase;
sterol 27-hydroxylase;
sterol 26-hydroxylase;
cholesterol 27-hydroxylase;
CYP27A;
CYP27A1;
cytochrome P450 27A1' |
|---|
| Class |
Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
With NADH or NADPH as one donor, and incorporation of one atom of
oxygen into the other donor
 |
|---|
| Sysname |
5beta-cholestane-3alpha,7alpha,12alpha-triol,NADPH:oxygen
oxidoreductase (26-hydroxylating) |
|---|
| Reaction(IUBMB) |
5beta-cholestane-3alpha,7alpha,12alpha-triol + NADPH + H+ + O2 =
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NADP+ +
H2O [RN:R04807] |
|---|
| Reaction(KEGG) |
R04807;
(other) R04806 R08505 R08725 R08726 R08758 R08759 R08760 R08761
 |
|---|
| Substrate |
5beta-cholestane-3alpha,7alpha,12alpha-triol [CPD:C05454];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007] |
|---|
| Product |
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol;
NADP+ [CPD:C00006];
H2O [CPD:C00001] |
|---|
| Comment |
Requires ferrodoxin. Acts on cholesterol,
cholest-5-en-3beta,7alpha-diol, 7alpha-hydroxycholest-4-en-3-one,
5beta-cholestane-3alpha,7alpha-diol as well as
5beta-cholestane-3alpha,7alpha,12alpha-triol. With cholesterol as
well as 26-hydroxycholesterol, 24-hydroxy- and 25-hydroxycholesterol
are also formed. With prolonged treatment, 26-hydroxycholesterol is
converted into the corresponding 27-aldehyde and 27-oic acid. |
|---|
| Pathway |
PATH: ec00120 Primary bile acid biosynthesis
PATH: ec01066 Biosynthesis of alkaloids derived from terpenoid and
polyketide
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00488 cytochrome P450, family 27, subfamily A (cholestanetriol
26-monooxygenase) |
|---|
| Genes |
HSA: 1593(CYP27A1)
PTR: 459951
MCC: 700192
MMU: 104086(Cyp27a1)
RNO: 301517(Cyp27a1)
CFA: 610489
BTA: 511960(CYP27A1)
ECB: 100055936
MDO: 100011045(CYP27A1)
GGA: 431683(CYP27A1)
XLA: 446987(cyp27a1)
DRE: 565876(DKEY-91I10.3)
 |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:4388637]
Okuda K, Hoshita N.
Oxidation of 5-beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol by
rat-liver mitochondria.
Biochim. Biophys. Acta. 164 (1968) 381-8.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:6423637]
Wikvall K.
Hydroxylations in biosynthesis of bile acids. Isolation of a
cytochrome P-450 from rabbit liver mitochondria catalyzing
26-hydroxylation of C27-steroids.
J. Biol. Chem. 259 (1984) 3800-4.
Oryctolagus cuniculus |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:2722778]
Andersson S, Davis DL, Dahlback H, Jornvall H, Russell DW.
Cloning, structure, and expression of the mitochondrial cytochrome
P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme.
J. Biol. Chem. 264 (1989) 8222-9.
Oryctolagus cuniculus |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:2318307]
Usui E, Noshiro M, Okuda K.
Molecular cloning of cDNA for vitamin D3 25-hydroxylase from rat
liver mitochondria.
FEBS. Lett. 262 (1990) 135-8.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:10512735]
Furster C, Bergman T, Wikvall K.
Biochemical characterization of a truncated form of CYP27A purified
from rabbit liver mitochondria.
Biochem. Biophys. Res. Commun. 263 (1999) 663-6.
Oryctolagus cuniculus |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:8496170]
Holmberg-Betsholtz I, Lund E, Bjorkhem I, Wikvall K.
Sterol 27-hydroxylase in bile acid biosynthesis. Mechanism of
oxidation of 5 beta-cholestane-3 alpha,7 alpha,12 alpha,27-tetrol
into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid.
J. Biol. Chem. 268 (1993) 11079-85.
Oryctolagus cuniculus |
|---|
Reference
Authors
Title
Journal
Organism
|
7 [PMID:11412116]
Pikuleva IA, Puchkaev A, Bjorkhem I.
Putative helix F contributes to regioselectivity of hydroxylation in
mitochondrial cytochrome P450 27A1.
Biochemistry. 40 (2001) 7621-9.
Homo sapiens [GN:hsa] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.14.13.15
IUBMB Enzyme Nomenclature: 1.14.13.15
ExPASy - ENZYME nomenclature database: 1.14.13.15
BRENDA, the Enzyme Database: 1.14.13.15
CAS: 52227-77-7 |
|---|
