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Information on EC 1.3.99.28 - phytoene desaturase (neurosporene-forming) and Organism(s) Rhodobacter capsulatus and UniProt Accession P17054

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EC Tree
IUBMB Comments
This enzyme is involved in carotenoid biosynthesis and catalyses up to three desaturation steps (cf. EC 1.3.99.29 [phytoene desaturase (zeta-carotene-forming)], EC 1.3.99.30 [phytoene desaturase (3,4-didehydrolycopene-forming)], EC 1.3.99.31 [phytoene desaturase (lycopene-forming)]). The enzyme is activated by FAD. NAD+, NADP+ or ATP show no activating effect .
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Rhodobacter capsulatus
UNIPROT: P17054
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The taxonomic range for the selected organisms is: Rhodobacter capsulatus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
3-step phytoene desaturase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phytoene desaturase
-
3-step phytoene desaturase
-
-
phytoene desaturase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
15-cis-phytoene + 3 acceptor = all-trans-neurosporene + 3 reduced acceptor
show the reaction diagram
overall reaction
-
SYSTEMATIC NAME
IUBMB Comments
15-cis-phytoene:acceptor oxidoreductase (neurosporene-forming)
This enzyme is involved in carotenoid biosynthesis and catalyses up to three desaturation steps (cf. EC 1.3.99.29 [phytoene desaturase (zeta-carotene-forming)], EC 1.3.99.30 [phytoene desaturase (3,4-didehydrolycopene-forming)], EC 1.3.99.31 [phytoene desaturase (lycopene-forming)]). The enzyme is activated by FAD. NAD+, NADP+ or ATP show no activating effect [1].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
show the reaction diagram
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
show the reaction diagram
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
show the reaction diagram
-
-
-
?
1,2-epoxyphytoene + acceptor
1,2-epoxyneurosporene + reduced acceptor
show the reaction diagram
-
-
-
-
?
15-cis-phytoene + 3 acceptor
all-trans-neurosporene + 3 reduced acceptor
show the reaction diagram
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
show the reaction diagram
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
show the reaction diagram
-
-
-
-
?
all-trans-phytofluene + 2 acceptor
all-trans-neurosporene + 2 reduced acceptor
show the reaction diagram
-
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
show the reaction diagram
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
C30-diapophytoene is not a substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
show the reaction diagram
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
show the reaction diagram
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
show the reaction diagram
-
-
-
?
15-cis-phytoene + 3 acceptor
all-trans-neurosporene + 3 reduced acceptor
show the reaction diagram
-
involved in carotenoid biosynthesis
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
show the reaction diagram
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
a low basal reaction is found in the absence of all coenzymes. Upon addition of FAD the activity is stimulated 5-fold. Km-value: 0.0049 mM
additional information
-
NAD+, NADP+ or ATP have no positive effect
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Diphenylamine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0333
15-cis-phytoene
-
pH 8.0, 30°C
0.0166
all-trans-zeta-carotene
-
pH 8.0, 30°C
additional information
additional information
classical Michaelis-Menten kinetic model
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
Diphenylamine
Rhodobacter capsulatus
-
pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00029
-
pH 8.0, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
metabolism
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. Rhodobacter capsulatus strain SB1003 also produces lycopene in vitro (cf. EC 1.3.99.31)
physiological function
involved in carotenoid biosynthesis
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
physiological function
-
involved in carotenoid biosynthesis
additional information
comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
x * 60000, SDS-PAGE
57000
-
x * 57000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 60000, SDS-PAGE
?
-
x * 57000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
expression in Escherichia coli
-
gene crtI, phylogenetic tree, co-expression with 5 other enzymes of the carotenoid pathway from Pantoea agglomerans, i.e. IPP isomerase, FPP synthase, GGPP synthase, phytoene synthase, lycopene cyclase, beta-carotene hydrolase, and zeaxanthin glucosyltransferase, in Escherichia coli, functional complementation by CrtI of Brevibacterium linens, CGI, CrtI of Corynebacterium glutamicum, RSI, CrtI of Rhodobacter sphaeroides RCI, CrtI of Rhodobacter capsulatus, and RBI, CrtI of Rhodopirellula baltica, and the homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG -CrtBPAG
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the phytoene desaturase gene, from Rhodobacter capsulatus is functionally complemented with a gene construct from Erwinia uredovora which encodes all enzymes responsible for formation of 15-cis phytoene in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Raisig, A.; Bartley, G.; Scolnik, P.; Sandmann, G.
Purification in an active state and properties of the 3-step phytoene desaturase from Rhodobacter capsulatus overexpressed in Escherichia coli
J. Biochem.
119
559-564
1996
Rhodobacter capsulatus
Manually annotated by BRENDA team
Bartley, G.E.; Scolnik, P.A.
Carotenoid biosynthesis in photosynthetic bacteria. Genetic characterization of the Rhodobacter capsulatus CrtI protein
J. Biol. Chem.
264
13109-13113
1989
Rhodobacter capsulatus (P17054)
Manually annotated by BRENDA team
Linden, H.; Misawa, N.; Chamovitz, D.; Pecker, I.; Hirschberg, J.; Sandmann, G.
Functional complementation in Escherichia coli of different phytoene desaturase genes and analysis of accumulated carotenes
Z. Naturforsch. C
46
1045-1051
1991
Rhodobacter capsulatus
Manually annotated by BRENDA team
Song, G.H.; Kim, S.H.; Choi, B.H.; Han, S.J.; Lee, P.C.
Heterologous carotenoid-biosynthetic enzymes: functional complementation and effects on carotenoid profiles in Escherichia coli
Appl. Environ. Microbiol.
79
610-618
2013
Brevibacterium linens, Brevibacterium linens DSM 20426, Cereibacter sphaeroides, Cereibacter sphaeroides KCTC 12085, Corynebacterium glutamicum, Corynebacterium glutamicum KCTC 1445, Pantoea agglomerans (K7WPN7), Pantoea agglomerans KCTC 2479 (K7WPN7), Rhodobacter capsulatus, Rhodobacter capsulatus KCTC 2583, Rhodopirellula baltica, Rhodopirellula baltica DSM 10527
Manually annotated by BRENDA team
Ding, B.Y.; Niu, J.; Shang, F.; Yang, L.; Chang, T.Y.; Wang, J.J.
Characterization of the geranylgeranyl diphosphate synthase gene in Acyrthosiphon pisum (Hemiptera Aphididae) and its association with carotenoid biosynthesis
Front. Physiol.
10
1398
2019
Cereibacter sphaeroides (P54980), Cereibacter sphaeroides ATCC 17023 (P54980), Cereibacter sphaeroides ATH 2.4.1. (P54980), Cereibacter sphaeroides CCUG 31486 (P54980), Cereibacter sphaeroides DSM 158 (P54980), Cereibacter sphaeroides JCM 6121 (P54980), Cereibacter sphaeroides LMG 2827 (P54980), Cereibacter sphaeroides NBRC 12203 (P54980), Cereibacter sphaeroides NCIMB 8253 (P54980), Rhodobacter capsulatus (P17054), Rhodobacter capsulatus ATCC BAA-309 (P17054), Rhodobacter capsulatus NBRC 16581 (P17054), Rhodobacter capsulatus SB1003 (P17054)
Manually annotated by BRENDA team