Information on EC 2.5.1.99 - all-trans-phytoene synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.99
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RECOMMENDED NAME
GeneOntology No.
all-trans-phytoene synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 geranylgeranyl diphosphate = all-trans-phytoene + 2 diphosphate
show the reaction diagram
overall reaction
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2 geranylgeranyl diphosphate = diphosphate + prephytoene diphosphate
show the reaction diagram
1a
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prephytoene diphosphate = all-trans-phytoene + diphosphate
show the reaction diagram
1b
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SYSTEMATIC NAME
IUBMB Comments
geranylgeranyl-diphosphate:geranylgeranyl-diphosphate geranylgeranyltransferase (all-trans-phytoene forming)
Requires Mn2+ for activity. The enzyme from the bacterium Pantoea agglomerans (previously known as Erwinia herbicola) produces the all-trans isomer of phytoene. cf. EC 2.5.1.32, 15-cis-phytoene synthase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
formerly Erwinia herbicola, gene crtB
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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Z-phytoene, synthesized by the all-trans-phytoene synthase is prevalent in higher plants, fungi, algae, and photosynthetic bacteria, while E-phytoene, synthesized by EC 2.5.1.32, often predominates in nonphotosynthetic bacteria. Z-phytoene is the sole product of PSase in a phylogenetically diverse group of organisms, while a smaller subset of organisms have an analogous enzyme that appears to be specific for synthesis of the E isomer
metabolism
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phytoene synthase catalyzes the first pathway specific reaction in the carotenoid biosynthetic pathway and controls flux into the pathway
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 geranylgeranyl diphosphate
all-trans-phytoene + 2 diphosphate
show the reaction diagram
2 geranylgeranyl diphosphate
diphosphate + prephytoene diphosphate
show the reaction diagram
prephytoene diphosphate
all-trans-phytoene + diphosphate
show the reaction diagram
additional information
?
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the all-trans-phytoene synthase, EC 2.5.1.99, catalyzes the formation of the trans-phytoene stereoisomer, while the cis-phytoene synthase, EC 2.5.1.32, catalyzes the formation of the cis-stereoisomer, mechanism for the synthesis of cis- and trans-phytoene directly from prephytoene diphosphate,overview
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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
2 geranylgeranyl diphosphate
all-trans-phytoene + 2 diphosphate
show the reaction diagram
2 geranylgeranyl diphosphate
diphosphate + prephytoene diphosphate
show the reaction diagram
prephytoene diphosphate
all-trans-phytoene + diphosphate
show the reaction diagram
additional information
?
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the all-trans-phytoene synthase, EC 2.5.1.99, catalyzes the formation of the trans-phytoene stereoisomer, while the cis-phytoene synthase, EC 2.5.1.32, catalyzes the formation of the cis-stereoisomer, mechanism for the synthesis of cis- and trans-phytoene directly from prephytoene diphosphate,overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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activates
Mn2+
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required for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
geranylgeranyl diphosphate
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substrate inhibition at concentrations above 0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the enzyme is strongly stimulated by detergent
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
geranylgeranyl diphosphate
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pH 7.2, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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purified recombinant EEF-modified enzyme, pH 7.2, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 34500, recombinant EEF-modified enzyme, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from photoinduced Mycobacterium sp. by ammoniumm sulfate fractionation, dialysis, ultracentrifugation, and anion exchange chromatography
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recombinant EEF-modified enzyme 13fold from Escherichia coli strain JM101/pCLPII49 by anion-exchange chromatography and immunoaffinity chromatography on an immobilized monoclonal anti-alpha-tubulin antibody YL1/2 column binding to the EEF tripeptide to over 90% homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene crtB, expression of the enzyme with a C-terminally inserted Glu-Glu-Phe (EEF) tripepetideEscherichia coli strain JM101/pCLPII49
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