Information on EC 1.14.15.9 - spheroidene monooxygenase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.14.15.9
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RECOMMENDED NAME
GeneOntology No.
spheroidene monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,2-dihydroxyspheroidene = spheroiden-2-one + H2O
show the reaction diagram
(1c), spontaneous
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2,2-dihydroxyspirilloxanthin = 2-oxospirilloxanthin + H2O
show the reaction diagram
(2c), spontaneous; (3c), spontaneous
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2-hydroxyspheroidene + reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2,2-dihydroxyspheroidene + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
(1b)
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2-hydroxyspirilloxanthin + reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2,2-dihydroxyspirilloxanthin + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
(2b)
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2-oxospirilloxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 O2 = 2,2'-dioxospirilloxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
show the reaction diagram
(3)
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2-oxospirilloxanthin + reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2'-hydroxy-2-oxospirilloxanthin + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
(3a); (3b)
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spheroidene + 2 reduced ferredoxin [iron-sulfur] cluster + 2 O2 = spheroiden-2-one + 2 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
show the reaction diagram
spheroidene + reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2-hydroxyspheroidene + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
(1a)
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spirilloxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 O2 = 2-oxospirilloxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
show the reaction diagram
(2)
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spirilloxanthin + reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2-hydroxyspirilloxanthin + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
(2a)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
spheroidene and spheroidenone biosynthesis
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spirilloxanthin and 2,2'-diketo-spirilloxanthin biosynthesis
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Carotenoid biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
spheroidene,reduced-ferredoxin:oxygen oxidoreductase (spheroiden-2-one-forming)
The enzyme is involved in spheroidenone biosynthesis and in 2,2'-dioxospirilloxanthin biosynthesis. The enzyme from Rhodobacter sphaeroides contains heme at its active site [1].
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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the enzyme is involved in spheroidene biosynthesis pathway and spirilloxanthin biosynthesis pathway. Methylated carotenoids, such as spheroidene and spirilloxanthin, function as accessory pigments in the light-harvesting and reaction-center complexes of purple bacteria
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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
1'-hydroxy-1-demethylspheroidene + reduced ferredoxin + O2
1'-hydroxy-1-demethylspheroiden-2-one + oxidized ferredoxin + H2O
show the reaction diagram
1'-hydroxyspheroidene + reduced ferredoxin + O2
1'-hydroxyspheroiden-2-one + oxidized ferredoxin + H2O
show the reaction diagram
1,1'-dihydroxy-3,4-didehydrolycopene + 2 reduced ferredoxin + 2 O2
2,2'-dioxo-1,1'-dihydroxy-3,4-didehydrolycopene + 2 oxidized ferredoxin + 2 H2O
show the reaction diagram
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?
1-hydroxy-3,4-didehydrolycopene + reduced ferredoxin + O2
2-oxo-1-hydroxy-3,4-didehydrolycopene + oxidized ferredoxin + H2O
show the reaction diagram
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?
2-hydroxyspheroidene + reduced ferredoxin + O2
spheroiden-2-one + oxidized ferredoxin + H2O
show the reaction diagram
3,4,3',4'-tetradehydrolycopene + reduced ferredoxin + O2
1,1'-dihydroxy-3,4,3',4'-tetradehydrolycopen-2-one + oxidized ferredoxin + H2O
show the reaction diagram
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?
3,4,3',4'-tetradehydrolycopene + reduced ferredoxin + O2
1-hydroxy-3,4,3',4'-tetradehydrolycopen-2-one + oxidized ferredoxin + H2O
show the reaction diagram
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?
3,4-didehydrolycopene + reduced ferredoxin + O2
1-hydroxy-3,4-didehydrolycopen-2-one + oxidized ferredoxin + H2O
show the reaction diagram
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?
spheroidene + reduced ferredoxin + O2
spheroiden-2-one + oxidized ferredoxin + H2O
show the reaction diagram
spheroidene + reduced ferredoxin + O2
spheroidenone + oxidized ferredoxin + H2O
show the reaction diagram
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?
spirilloxanthin + 2 reduced ferredoxin + 2 O2
2,2'-dioxosprilloxanthin + 2 oxidized ferredoxin + 2 H2O
show the reaction diagram
spirilloxanthin + reduced ferredoxin + O2
2-oxospirilloxanthin + oxidized ferredoxin + H2O
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
spheroidene + reduced ferredoxin + O2
spheroiden-2-one + oxidized ferredoxin + H2O
show the reaction diagram
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conversion rate: 36%
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
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CrtA has a 5-coordinated heme at its active site
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0101 - 0.0155
1'-hydroxyspheroidene
0.007 - 0.0191
spheroidene
0.009 - 0.0181
spirilloxanthin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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x * 32000, SDS-PAGE
65000
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x * 65000, calculated from sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli. Coexpression of CrtA with acyclic C40 carotenoid pathways can introduce a keto group at the C(2,2') position of unnatural substrates that do not exhibit a C(3,4) double bond. The complete conversion of tetradehydrolycopene to phillipsiaxanthin observed suggests it is a favorable substrate for CrtA activity when compared to the incomplete conversion of lycopene to lycopene-2-one in the presence of CrtA
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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construction of a simple and cost-effective sensor independent from specific reagents and instruments for monitoring qualities of marine aquacultural fields. A sensor strain consisting of a crtA deleted host strain of Rhodovulum sulfidophilum, in which the CrtA gene is reintroduced downstream of the promoter for the dimethyl sulfide dehydrogenase (Ddh) gene cluster, is constructed to detect dimethyl sulfide in the nursery of lavers based on the conversion of the carotenoid colors
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.15.9)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)