Cloned (Comment) | Organism |
---|---|
gene crtI, recombinant expression of His6-tagged enzyme in Escherichia coli | Pantoea ananatis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0176 | - |
15-cis-phytoene | recombinant His6-tagged enzyme, pH and temperature not specified in the publication | Pantoea ananatis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | membrane-peripheral enzyme, phosphatidyl-choline liposome membranes | Pantoea ananatis | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
15-cis-phytoene + FAD | Pantoea ananatis | - |
all-trans-phytofluene + FADH2 | - |
? | |
all-trans-neurosporene + FAD | Pantoea ananatis | - |
all-trans-lycopene + FADH2 | - |
? | |
all-trans-phytofluene + FAD | Pantoea ananatis | - |
all-trans-zeta-carotene + FADH2 | - |
? | |
all-trans-zeta-carotene + FAD | Pantoea ananatis | - |
all-trans-neurosporene + FADH2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pantoea ananatis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity cromatography and gel filtration | Pantoea ananatis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
15-cis-phytoene + FAD | - |
Pantoea ananatis | all-trans-phytofluene + FADH2 | - |
? | |
all-trans-neurosporene + FAD | - |
Pantoea ananatis | all-trans-lycopene + FADH2 | - |
? | |
all-trans-phytofluene + FAD | - |
Pantoea ananatis | all-trans-zeta-carotene + FADH2 | - |
? | |
all-trans-zeta-carotene + FAD | - |
Pantoea ananatis | all-trans-neurosporene + FADH2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CrtI | - |
Pantoea ananatis |
crtI-type phytoene desaturase | - |
Pantoea ananatis |
phytoene desaturase | - |
Pantoea ananatis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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 | |
additional information | no activity with FMN, NAD+, and NADP+ | Pantoea ananatis |
General Information | Comment | Organism |
---|---|---|
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 |
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 |