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Literature summary extracted from

  • Schaub, P.; Yu, Q.; Gemmecker, S.; Poussin-Courmontagne, P.; Mailliot, J.; McEwen, A.G.; Ghisla, S.; Al-Babili, S.; Cavarelli, J.; Beyer, P.
    On the structure and function of the phytoene desaturase CRTI from Pantoea ananatis, a membrane-peripheral and FAD-dependent oxidase/isomerase (2012), PLoS ONE, 7, e39550.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.99.31 gene crtI, recombinant expression of His6-tagged enzyme in Escherichia coli Pantoea ananatis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.99.31 0.0176
-
 15-cis-phytoene recombinant His6-tagged enzyme, pH and temperature not specified in the publication Pantoea ananatis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.99.31 membrane membrane-peripheral enzyme, phosphatidyl-choline liposome membranes Pantoea ananatis 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.99.31 15-cis-phytoene + FAD Pantoea ananatis
-
 all-trans-phytofluene + FADH2
-
 ?
1.3.99.31 all-trans-neurosporene + FAD Pantoea ananatis
-
 all-trans-lycopene + FADH2
-
 ?
1.3.99.31 all-trans-phytofluene + FAD Pantoea ananatis
-
 all-trans-zeta-carotene + FADH2
-
 ?
1.3.99.31 all-trans-zeta-carotene + FAD Pantoea ananatis
-
 all-trans-neurosporene + FADH2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.99.31 Pantoea ananatis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.99.31 recombinant His6-tagged enzyme from Escherichia coli by nickel affinity cromatography and gel filtration Pantoea ananatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.99.31 15-cis-phytoene + FAD
-
 Pantoea ananatis all-trans-phytofluene + FADH2
-
 ?
1.3.99.31 all-trans-neurosporene + FAD
-
 Pantoea ananatis all-trans-lycopene + FADH2
-
 ?
1.3.99.31 all-trans-phytofluene + FAD
-
 Pantoea ananatis all-trans-zeta-carotene + FADH2
-
 ?
1.3.99.31 all-trans-zeta-carotene + FAD
-
 Pantoea ananatis all-trans-neurosporene + FADH2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.99.31 CrtI
-
 Pantoea ananatis
1.3.99.31 crtI-type phytoene desaturase
-
 Pantoea ananatis
1.3.99.31 phytoene desaturase
-
 Pantoea ananatis

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.99.31 FAD CRTI utilizes FAD as the sole redox-active cofactor, binding kinetics and structure analysis, molecular docking, overview. Oxygen, replaceable by quinones in its absence, is needed as the terminal electron acceptor. FAD, besides its catalytic role also displays a structural function by enabling the formation of enzymatically active CRTI membrane associates Pantoea ananatis
1.3.99.31 additional information no activity with FMN, NAD+, and NADP+ Pantoea ananatis

General Information

EC Number General Information Comment Organism
1.3.99.31 evolution CRTI-type phytoene desaturases prevailing in bacteria and fungi can form lycopene directly from phytoene while plants employ two distinct desaturases and two cis-tans isomerases for the same purpose Pantoea ananatis
1.3.99.31 physiological function CRTI is a membrane-peripheral oxidoreductase which utilizes FAD as the sole redox-active cofactor. Oxygen, replaceable by quinones in its absence, is needed as the terminal electron acceptor. FAD, besides its catalytic role also displays a structural function by enabling the formation of enzymatically active CRTI membrane associates. Under anaerobic conditions the enzyme can act as a carotene cis-trans isomerase. In silico-docking experiments yielded information on substrate binding sites, potential catalytic residues and is in favor of single half-site recognition of the symmetrical C40 hydrocarbon substrate Pantoea ananatis