KEGG   ENZYME: 1.14.15.4Help
Entry
EC 1.14.15.4                Enzyme                                 

Name
steroid 11beta-monooxygenase;
steroid 11beta-hydroxylase;
steroid 11beta/18-hydroxylase
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
BRITE hierarchy
Sysname
steroid,reduced-adrenodoxin:oxygen oxidoreductase (11beta-hydroxylating)
Reaction(IUBMB)
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O [RN:R02726]
Reaction(KEGG)
Substrate
steroid [CPD:C00377];
reduced adrenodoxin [CPD:C00662];
O2 [CPD:C00007];
H+ [CPD:C00080]
Product
11beta-hydroxysteroid [CPD:C01058];
oxidized adrenodoxin [CPD:C00667];
H2O [CPD:C00001]
Comment
A heme-thiolate protein (P-450). Also hydroxylates steroids at the 18-position, and converts 18-hydroxycorticosterone into aldosterone.
History
EC 1.14.15.4 created 1961 as EC 1.99.1.7, transferred 1965 to EC 1.14.1.6, transferred 1972 to EC 1.14.15.4, modified 1989, modified 2014
Pathway
ec00140  Steroid hormone biosynthesis
ec01100  Metabolic pathways
Orthology
K00497  steroid 11beta-monooxygenase
K07433  steroid 11beta-monooxygenase / corticosterone 18-monooxygenase
Genes
HSA: 1584(CYP11B1) 1585(CYP11B2)
PTR: 464437(CYP11B1)
PPS: 100971238 100971586
GGO: 101142418
PON: 100459910
NLE: 100605657
MCC: 695793(CYP11B1) 695914(CYP11B2)
MCF: 102136659 102137301
CSAB: 103237546(CYP11B1)
RRO: 104679773 104679810
RBB: 108536535
CJC: 100415667(CYP11B1)
MMU: 110115(Cyp11b1) 13072(Cyp11b2)
RNO: 24294(Cyp11b2) 353498(Cyp11b3) 500892(Cyp11b1)
CFA: 482071(CYP11B2)
AML: 100478197
ORO: 101364874
FCA: 101097790
PTG: 102972244
AJU: 106989683
BTA: 282422(CYP11B1) 787628
PHD: 102327345
OAS: 101102377 767576(CYP11B1)
SSC: 110260194
CFR: 102517728
CDK: 105106427
LVE: 103089121
OOR: 101286768
EAI: 106827552
MYB: 102249727
MYD: 102752229
HAI: 109390820
RSS: 109434846
PALE: 102881458
LAV: 100654178
TMU: 101354125
MDO: 100032885
SHR: 100930767
OAA: 100082065
PHI: 102113159
FPG: 101918505
FCH: 102046275
ASN: 102375758
AMJ: 102575737(CYP11B1)
CPIC: 101950678
ACS: 100560890
PVT: 110084842
PBI: 103058342
GJA: 107116366
XLA: 108718624(CYP11B1)
XTR: 101731070
DRE: 791124(cyp11c1)
SRX: 107745157
SANH: 107698185
SGH: 107570796
CCAR: 109110857
IPU: 108263488
AMEX: 103026652
TRU: 101075863
LCO: 104920541
NCC: 104944920
MZE: 101463871
OLA: 100125822(cyp11b)
XMA: 102236274
PRET: 103478110
NFU: 107379700
CSEM: 103388284
LCF: 108885901
HCQ: 109522775
BPEC: 110163163
ELS: 105018961
SFM: 108925533
LCM: 102345423
 » show all
Taxonomy
Reference
1  [PMID:13276417]
  Authors
GRANT JK, BROWNIE AC.
  Title
The role of fumarate and TPN in steroid enzymic 11beta-hydroxylation.
  Journal
Biochim Biophys Acta 18:433-4 (1955)
Reference
2  [PMID:13211659]
  Authors
HAYANO M, DORFMAN RI.
  Title
On the mechanism of the C11 beta-hydroxylation of steroids.
  Journal
J Biol Chem 211:227-35 (1954)
Reference
3  [PMID:13426185]
  Authors
TOMKINS GM, MICHAEL PJ, CURRAN JF.
  Title
Studies on the nature of steroid 11-beta hydroxylation.
  Journal
Biochim Biophys Acta 23:655-6 (1957)
Reference
4  [PMID:3485096]
  Authors
Yanagibashi K, Haniu M, Shively JE, Shen WH, Hall P.
  Title
The synthesis of aldosterone by the adrenal cortex. Two zones (fasciculata and glomerulosa) possess one enzyme for 11 beta-, 18-hydroxylation, and aldehyde synthesis.
  Journal
J Biol Chem 261:3556-62 (1986)
Reference
5  [PMID:4967077]
  Authors
Zuidweg MH.
  Title
Hydroxylation of Reichstein's compound S with cell-free preparations from Curvularia lunata.
  Journal
Biochim Biophys Acta 152:144-58 (1968)
DOI:10.1016/0005-2760(68)90016-7
Other DBs
ExplorEnz - The Enzyme Database: 1.14.15.4
IUBMB Enzyme Nomenclature: 1.14.15.4
ExPASy - ENZYME nomenclature database: 1.14.15.4
BRENDA, the Enzyme Database: 1.14.15.4
CAS: 9029-66-7

DBGET integrated database retrieval system