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Information on EC 1.14.14.14 - aromatase and Organism(s) Sus scrofa and UniProt Accession P79304

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IUBMB Comments
A cytochrome P-450. The enzyme catalyses three sequential hydroxylations of the androgens androst-4-ene-3,17-dione and testosterone, resulting in their aromatization and forming the estrogens estrone and 17beta-estradiol, respectively. The direct electron donor to the enzyme is EC 1.6.2.4, NADPH---hemoprotein reductase.
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This record set is specific for:
Sus scrofa
UNIPROT: P79304
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The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
Synonyms
aromatase, cyp19a1, cyp19a1a, cyp19a, cyp19a1b, cyp19a3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CYP19A1
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
testosterone monooxygenase (17beta-estradiol-forming)
A cytochrome P-450. The enzyme catalyses three sequential hydroxylations of the androgens androst-4-ene-3,17-dione and testosterone, resulting in their aromatization and forming the estrogens estrone and 17beta-estradiol, respectively. The direct electron donor to the enzyme is EC 1.6.2.4, NADPH---hemoprotein reductase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
androst-4-ene-3,17-dione + 3 O2 + 3 reduced flavoproteins
estrone + formate + 4 H2O + 3 oxidized flavoproteins
show the reaction diagram
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-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
dimerization of the human P450arom, primarily via salt bridges at the I–H loop, leads to greater activity and reduced release of intermediates compared to porcine aromatase.The porcine gonadal P450arom has no ionic interaction at the I-H loop but forms a new intra-molecular salt bridge at the N termini of the I-helix that leads to locking of the substrate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CP193_PIG
501
2
57915
Swiss-Prot
Secretory Pathway (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
FRET and crystallization data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martin, L.L.; Holien, J.K.; Mizrachi, D.; Corbin, C.J.; Conley, A.J.; Parker, M.W.; Rodgers, R.J.
Evolutionary comparisons predict that dimerization of human cytochrome P450 aromatase increases its enzymatic activity and efficiency
J. Steroid Biochem. Mol. Biol.
154
294-301
2015
Homo sapiens (P11511), Sus scrofa (P79304)
Manually annotated by BRENDA team