Information on EC 1.14.15.19 - C-19 steroid 1alpha-hydroxylase

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The expected taxonomic range for this enzyme is: Sorangium cellulosum

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EC NUMBER
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1.14.15.19
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RECOMMENDED NAME
GeneOntology No.
C-19 steroid 1alpha-hydroxylase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
testosterone + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 1alpha-hydroxytestosterone + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
testosterone,reduced-ferredoxin:oxygen oxidoreductase (1alpha-hydroxylating)
The enzyme, characterized from the bacterium Sorangium cellulosum, is a class I cytochrome P-450, and uses ferredoxin as its electron donor [1]. It was shown to act on several C-19 steroid substrates, including testosterone, androstenedione, testosterone-acetate and 11-oxoandrostenedione [2].
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-nootkatone + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
?
show the reaction diagram
11-oxoandrostenedione + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
1alpha-hydroxy-11-oxoandrostenedione + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
Escherichia coli-based whole-cell biocatalyst system
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-
?
androstenedione + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
1alpha-hydroxyandrostenedione + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
Escherichia coli-based whole-cell biocatalyst system
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-
?
androstenedione + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
?
show the reaction diagram
testosterone + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
1alpha-hydroxytestosterone + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
testosterone + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1alpha-hydroxytestosterone + H2O + oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
testosterone-acetate + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
1alpha-hydroxytestosterone acetate + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
Escherichia coli-based whole-cell biocatalyst system
Escherichia coli-based whole-cell biocatalyst system produces a mixture (1:2.5:3) of an unknown compound and 1alpha- and 9alpha-hydroxytestosterone acetate
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?
zerumbone + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
?
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
testosterone + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1alpha-hydroxytestosterone + H2O + oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P-450
cytochrome P-450-dependent monooxygenase
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.031
androstenedione
pH and temperature not specified in the publication
0.04
testosterone
pH and temperature not specified in the publication
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50220
ESI-TOF mass spectrometry, holoenzyme
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in a soluble form in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
modification at the C-1 position of a steroid is of pharmaceutical interest. Biotransformation can overcome tedious multistep chemical synthesis
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.15.19)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)