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Literature summary for 1.3.99.31 extracted from

  • 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 (2019), Front. Physiol., 10, 1398 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene carB, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli Blakeslea trispora
gene crtI, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli Pantoea ananatis
gene crtI, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli Mycolicibacterium aurum
gene crtI, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli Pantoea agglomerans
gene Rhu_A0493, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli Rhodospirillum rubrum

Protein Variants

Protein Variants Comment Organism
additional information competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway Pantoea ananatis
additional information competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway Blakeslea trispora
additional information competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway Mycolicibacterium aurum
additional information competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway Rhodospirillum rubrum
additional information competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway Pantoea agglomerans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information classical Michaelis-Menten kinetic model Pantoea ananatis
additional information
-
additional information classical Michaelis-Menten kinetic model Blakeslea trispora
additional information
-
additional information classical Michaelis-Menten kinetic model Mycolicibacterium aurum
additional information
-
additional information classical Michaelis-Menten kinetic model Rhodospirillum rubrum
additional information
-
additional information classical Michaelis-Menten kinetic model Pantoea agglomerans

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Blakeslea trispora 16020
-
membrane
-
Mycolicibacterium aurum 16020
-
membrane
-
Rhodospirillum rubrum 16020
-
membrane
-
Pantoea agglomerans 16020
-
membrane CrtI from Pantoea ananas associates spontaneously to liposomal membranes but no membrane-spanning region per se is evidenced, suggesting a monotopic binding to membranes Pantoea ananatis 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
15-cis-phytoene + acceptor Pantoea ananatis
-
all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor Blakeslea trispora
-
all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor Mycolicibacterium aurum
-
all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor Rhodospirillum rubrum
-
all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor Pantoea agglomerans
-
all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor Rhodospirillum rubrum S1
-
all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor Rhodospirillum rubrum NCIMB 8255
-
all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor Rhodospirillum rubrum ATH 1.1.1
-
all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor Rhodospirillum rubrum ATCC 11170
-
all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor Rhodospirillum rubrum LMG 4362
-
all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor Rhodospirillum rubrum DSM 467
-
all-trans-phytofluene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Pantoea ananatis
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Blakeslea trispora
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Mycolicibacterium aurum
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Rhodospirillum rubrum
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Pantoea agglomerans
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Rhodospirillum rubrum S1
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Rhodospirillum rubrum NCIMB 8255
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Rhodospirillum rubrum ATH 1.1.1
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Rhodospirillum rubrum ATCC 11170
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Rhodospirillum rubrum LMG 4362
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor Rhodospirillum rubrum DSM 467
-
all-trans-lycopene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Pantoea ananatis
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Blakeslea trispora
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Mycolicibacterium aurum
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Rhodospirillum rubrum
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Pantoea agglomerans
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Rhodospirillum rubrum S1
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Rhodospirillum rubrum NCIMB 8255
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Rhodospirillum rubrum ATH 1.1.1
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Rhodospirillum rubrum ATCC 11170
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Rhodospirillum rubrum LMG 4362
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor Rhodospirillum rubrum DSM 467
-
all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Pantoea ananatis
-
all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Blakeslea trispora
-
all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Mycolicibacterium aurum
-
all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Rhodospirillum rubrum
-
all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Pantoea agglomerans
-
all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Rhodospirillum rubrum S1
-
all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Rhodospirillum rubrum NCIMB 8255
-
all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Rhodospirillum rubrum ATH 1.1.1
-
all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Rhodospirillum rubrum ATCC 11170
-
all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Rhodospirillum rubrum LMG 4362
-
all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor Rhodospirillum rubrum DSM 467
-
all-trans-neurosporene + reduced acceptor
-
?

Organism

Organism UniProt Comment Textmining
Blakeslea trispora Q67GI0 Choanephora trispora
-
Mycolicibacterium aurum Q9K566 Mycobacterium aurum
-
Pantoea agglomerans E9LFG2 Erwinia herbicola or Pantoea agglomerans
-
Pantoea ananatis P21685 Erwinia uredovora
-
Rhodospirillum rubrum Q2RX47
-
-
Rhodospirillum rubrum ATCC 11170 Q2RX47
-
-
Rhodospirillum rubrum ATH 1.1.1 Q2RX47
-
-
Rhodospirillum rubrum DSM 467 Q2RX47
-
-
Rhodospirillum rubrum LMG 4362 Q2RX47
-
-
Rhodospirillum rubrum NCIMB 8255 Q2RX47
-
-
Rhodospirillum rubrum S1 Q2RX47
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
15-cis-phytoene + acceptor
-
Pantoea ananatis all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor
-
Blakeslea trispora all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor
-
Mycolicibacterium aurum all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor
-
Rhodospirillum rubrum all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor
-
Pantoea agglomerans all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor
-
Rhodospirillum rubrum S1 all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor
-
Rhodospirillum rubrum NCIMB 8255 all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor
-
Rhodospirillum rubrum ATH 1.1.1 all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor
-
Rhodospirillum rubrum ATCC 11170 all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor
-
Rhodospirillum rubrum LMG 4362 all-trans-phytofluene + reduced acceptor
-
?
15-cis-phytoene + acceptor
-
Rhodospirillum rubrum DSM 467 all-trans-phytofluene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Pantoea ananatis all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Blakeslea trispora all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Mycolicibacterium aurum all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Rhodospirillum rubrum all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Pantoea agglomerans all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Rhodospirillum rubrum S1 all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Rhodospirillum rubrum NCIMB 8255 all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Rhodospirillum rubrum ATH 1.1.1 all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Rhodospirillum rubrum ATCC 11170 all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Rhodospirillum rubrum LMG 4362 all-trans-lycopene + reduced acceptor
-
?
all-trans-neurosporene + acceptor
-
Rhodospirillum rubrum DSM 467 all-trans-lycopene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Pantoea ananatis all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Blakeslea trispora all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Mycolicibacterium aurum all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Rhodospirillum rubrum all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Pantoea agglomerans all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Rhodospirillum rubrum S1 all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Rhodospirillum rubrum NCIMB 8255 all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Rhodospirillum rubrum ATH 1.1.1 all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Rhodospirillum rubrum ATCC 11170 all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Rhodospirillum rubrum LMG 4362 all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-phytofluene + acceptor
-
Rhodospirillum rubrum DSM 467 all-trans-zeta-carotene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Pantoea ananatis all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Blakeslea trispora all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Mycolicibacterium aurum all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Rhodospirillum rubrum all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Pantoea agglomerans all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Rhodospirillum rubrum S1 all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Rhodospirillum rubrum NCIMB 8255 all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Rhodospirillum rubrum ATH 1.1.1 all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Rhodospirillum rubrum ATCC 11170 all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Rhodospirillum rubrum LMG 4362 all-trans-neurosporene + reduced acceptor
-
?
all-trans-zeta-carotene + acceptor
-
Rhodospirillum rubrum DSM 467 all-trans-neurosporene + reduced acceptor
-
?

Synonyms

Synonyms Comment Organism
CarB
-
Blakeslea trispora
CrtI
-
Pantoea ananatis
CrtI
-
Blakeslea trispora
CrtI
-
Mycolicibacterium aurum
CrtI
-
Rhodospirillum rubrum
CrtI
-
Pantoea agglomerans
PDS
-
Pantoea ananatis
PDS
-
Blakeslea trispora
PDS
-
Mycolicibacterium aurum
PDS
-
Rhodospirillum rubrum
PDS
-
Pantoea agglomerans
phytoene desaturase
-
Pantoea ananatis
phytoene desaturase
-
Blakeslea trispora
phytoene desaturase
-
Mycolicibacterium aurum
phytoene desaturase
-
Rhodospirillum rubrum
phytoene desaturase
-
Pantoea agglomerans
Rru_A0493
-
Rhodospirillum rubrum

General Information

General Information Comment Organism
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 Pantoea ananatis
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 Blakeslea trispora
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 Mycolicibacterium aurum
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 Rhodospirillum rubrum
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, formingtetradehydrolycopene. 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 Pantoea agglomerans
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. Pantoea ananatis CrtI produces lycopene in vivo, but also tetradehydrolycopene in vitro Pantoea ananatis
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. Mycolicibacterium aurum CrtI produces lycopene in vivo and in vitro Mycolicibacterium aurum
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. Rhodospirillum rubrum CrtI produces lycopene in vivo and in vitro Rhodospirillum rubrum
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. Blakeslea trispora CrtI produces lycopene in vivo and in vitro, but also didehydrolycopene in vivo (see also EC 1.3.99.30) Blakeslea trispora
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. Enterobacter agglomerans CrtI produces lycopene in vivo and in vitro, but also tetradehydrolycopene in vitro Pantoea agglomerans
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 Pantoea ananatis
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 Blakeslea trispora
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 Mycolicibacterium aurum
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 Rhodospirillum rubrum
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 Pantoea agglomerans