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Literature summary extracted from

  • Hiseni, A.; Otten, L.; Arends, I.
    Identification of catalytically important residues of the carotenoid 1,2-hydratases from Rubrivivax gelatinosus and Thiocapsa roseopersicina (2016), Appl. Microbiol. Biotechnol., 100, 1275-1284 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.131 gene crtC, sequence comparisons and rooted phylogenetic tree, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli TOP10 cells and strain BL21(DE3). While the removal of the N-terminus result in an increased expression level, all point mutations negatively influences the expression of the protein Rubrivivax gelatinosus
4.2.1.131 gene crtC, sequence comparisons and rooted phylogenetic tree, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli TOP10 cells and strain BL21(DE3). While the removal of the N-terminus result in an increased expression level, all point mutations negatively influences the expression of the protein Thiocapsa roseopersicina

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.131 D266A site-directed mutagenesis, inactive mutant Thiocapsa roseopersicina
4.2.1.131 D268A site-directed mutagenesis, inactive mutant Rubrivivax gelatinosus
4.2.1.131 H237A site-directed mutagenesis, inactive mutant Thiocapsa roseopersicina
4.2.1.131 H239A site-directed mutagenesis, inactive mutant Rubrivivax gelatinosus
4.2.1.131 H262A site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme Thiocapsa roseopersicina
4.2.1.131 H264A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Rubrivivax gelatinosus
4.2.1.131 additional information expression levels of wild-type and mutant enzymes from Escherichia coli strain BL21(DE3), overview. While the removal of the N-terminus result in an increased expression level, all point mutations negatively influences the expression of the protein. The N-terminally trubcated mutant also shows increased activity compared to the wild-type enzyme Thiocapsa roseopersicina
4.2.1.131 additional information expression levels of wild-type and mutant enzymes from Escherichia coli strain BL21(DE3), overview. While the removal of the N-terminus result in an increased expression level, all point mutations negatively influences the expression of the protein. The N-terminally truncated mutant also shows increased activity compared to the wild-type enzyme Rubrivivax gelatinosus
4.2.1.131 S58Q site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Thiocapsa roseopersicina
4.2.1.131 S58V site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Thiocapsa roseopersicina
4.2.1.131 W239A site-directed mutagenesis, inactive mutant Thiocapsa roseopersicina
4.2.1.131 W241A site-directed mutagenesis, inactive mutant Rubrivivax gelatinosus
4.2.1.131 Y266A site-directed mutagenesis, inactive mutant Rubrivivax gelatinosus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.131 2 lycopene + H2O Rubrivivax gelatinosus cofactor-independent catalysis 1-hydroxylycopene + 1,1'-dihydroxylycopene
-
 ?
4.2.1.131 2 lycopene + H2O Thiocapsa roseopersicina cofactor-independent catalysis 1-hydroxylycopene + 1,1'-dihydroxylycopene
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.131 Rubrivivax gelatinosus P95619
-
-
4.2.1.131 Thiocapsa roseopersicina Q7X3G5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.131 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Rubrivivax gelatinosus
4.2.1.131 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Thiocapsa roseopersicina

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.131 2 lycopene + H2O cofactor-independent catalysis Rubrivivax gelatinosus 1-hydroxylycopene + 1,1'-dihydroxylycopene
-
 ?
4.2.1.131 2 lycopene + H2O cofactor-independent catalysis Thiocapsa roseopersicina 1-hydroxylycopene + 1,1'-dihydroxylycopene
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.131 ? x * 44000, recombinant His-tagged enzyme, SDS-PAGE Rubrivivax gelatinosus
4.2.1.131 ? x * 44000, recombinant His-tagged enzyme, SDS-PAGE Thiocapsa roseopersicina

Synonyms

EC Number Synonyms Comment Organism
4.2.1.131 CrtC
-
 Rubrivivax gelatinosus
4.2.1.131 CrtC
-
 Thiocapsa roseopersicina
4.2.1.131 RgCrtC
-
 Rubrivivax gelatinosus
4.2.1.131 TrCrtC
-
 Thiocapsa roseopersicina

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.131 25
-
 assay at Rubrivivax gelatinosus
4.2.1.131 25
-
 assay at Thiocapsa roseopersicina

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.131 8
-
 assay at Rubrivivax gelatinosus
4.2.1.131 8
-
 assay at Thiocapsa roseopersicina

General Information

EC Number General Information Comment Organism
4.2.1.131 evolution the enzyme belongs to the PF07143 family Rubrivivax gelatinosus
4.2.1.131 evolution the enzyme belongs to the PF07143 family Thiocapsa roseopersicina