Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
phylogenetic tree of MaoC-like domains in PhaJ homologues encoded in Ralstonia eutropha H16 genome and domains in the known PhaJ proteins from Aeromonas caviae and Pseudomonas aeruginosa
evolution
phylogenetic tree of MaoC-like domains in PhaJ homologues encoded in Ralstonia eutropha H16 genome and domains in the known PhaJ proteins from Aeromonas caviae and Pseudomonas aeruginosa
evolution
all HFX-gene encoded proteins contain a MaoC-like domain (pfam01575), similar to PhaJAc, which is involved in PHA biosynthesis for supplying (R)-3HB-CoA from fatty acid beta-oxidation
evolution
enzyme PhaJYB4 shows a high homology to short chain-length (C4-C6)-specific PhaJs, e.g. Pseudomonas aeruginosa PhaJ1Pa and Aeromonas caviae PhaJAc, rather than medium chain-length (C8-C12)-specific PhaJs, e.g. Pseudomonas aeruginosa PhaJ4Pa4
evolution
-
enzyme PhaJYB4 shows a high homology to short chain-length (C4-C6)-specific PhaJs, e.g. Pseudomonas aeruginosa PhaJ1Pa and Aeromonas caviae PhaJAc, rather than medium chain-length (C8-C12)-specific PhaJs, e.g. Pseudomonas aeruginosa PhaJ4Pa4
-
evolution
-
all HFX-gene encoded proteins contain a MaoC-like domain (pfam01575), similar to PhaJAc, which is involved in PHA biosynthesis for supplying (R)-3HB-CoA from fatty acid beta-oxidation
-
evolution
-
phylogenetic tree of MaoC-like domains in PhaJ homologues encoded in Ralstonia eutropha H16 genome and domains in the known PhaJ proteins from Aeromonas caviae and Pseudomonas aeruginosa
-
malfunction
-
deletion of phaJ4aRe from the chromosome results in significant decrease of (R)-3-hydroxyhexanoate composition in the accumulated copolyester, whereas no change is observed with deletion of phaJ4bRe or phaJ4cRe
malfunction
-
inactivating mutations of multifunctional enzyme type 2 hydratase lead to D-bifunctional protein deficiency type II
malfunction
defects in either HC-PPase or ECH2 compromise cell proliferation due to defects in mobilizing seed storage lipids, phenotype, overview. Enoyl-CoA hydratase 2 (ECH2) gene mutation causes the A#3-1sm phenotypes, overview. Mutant A#3-1 has a cell size that is severely reduced, but the cell number remains similar to that of original fugu5-1. The cell number decreases in A#3-1 single mutant (A#3-1sm), similar to that of fugu5-1, but cell size is almost equal to that of the wild-type. A#3-1 mutation does not affect CCE in other compensation exhibiting mutant backgrounds, such as an3-4 and fugu2-1/fas1-6
malfunction
polyhydroxyalkanoate contents are slightly reduced in a phaJ deletion mutant DELTAphaJ1 compared to wild-type
malfunction
-
polyhydroxyalkanoate contents are slightly reduced in a phaJ deletion mutant DELTAphaJ1 compared to wild-type
-
malfunction
-
defects in either HC-PPase or ECH2 compromise cell proliferation due to defects in mobilizing seed storage lipids, phenotype, overview. Enoyl-CoA hydratase 2 (ECH2) gene mutation causes the A#3-1sm phenotypes, overview. Mutant A#3-1 has a cell size that is severely reduced, but the cell number remains similar to that of original fugu5-1. The cell number decreases in A#3-1 single mutant (A#3-1sm), similar to that of fugu5-1, but cell size is almost equal to that of the wild-type. A#3-1 mutation does not affect CCE in other compensation exhibiting mutant backgrounds, such as an3-4 and fugu2-1/fas1-6
-
malfunction
-
deletion of phaJ4aRe from the chromosome results in significant decrease of (R)-3-hydroxyhexanoate composition in the accumulated copolyester, whereas no change is observed with deletion of phaJ4bRe or phaJ4cRe
-
metabolism
-
the enzyme is involved in the peroxisomal beta-oxidation of fatty acids and their derivatives
metabolism
as the hydration reaction catalyzed by R-ECHs is a reversible process, R-ECHs may be involved in PHA degradation as well as in PHA biosynthesis
metabolism
-
as the hydration reaction catalyzed by R-ECHs is a reversible process, R-ECHs may be involved in PHA degradation as well as in PHA biosynthesis
-
metabolism
-
the enzyme is involved in the peroxisomal beta-oxidation of fatty acids and their derivatives
-
physiological function
-
MFE2 consists of a (3R)-hydroxyacyl-CoA dehydrogenase, HD, domain, a (2E)-enoyl-CoA hydratase 2, H2, domain, and a sterol carrier protein 2-like domain, and is known to catalyze the second and third steps of the peroxisomal beta-oxidation of fatty acids and their derivatives
physiological function
(R)-specific enoyl-CoA hydratase mediates polyhydroxyalkanoate mobilization in Haloferax mediterranei. Enoyl coenzyme A (enoyl-CoA) hydratases (ECHs) reversibly catalyze the syn and anti hydration of 2-enoyl-CoA to produce (S)- or (R)-3-hydroxyacyl-CoA (3HA-CoA). The (S)-specific ECHs (S-ECHs, EC 4.2.1.17) are involved in fatty acid beta-oxidation. Through catalyzing the hydration of intermediates in fatty acid beta-oxidation, the (R)-specific ECHs (R-ECHs) may play an important role in fatty acid metabolism in eukaryotes and in polyhydroxyalkanoate (PHA) biosynthesis in bacteria. Function of PhaJ1 on PHA mobilization
physiological function
(R)-specific enoyl-coenzyme A (enoyl-CoA) hydratases (PhaJs) are capable of supplying monomers from fatty acid beta-oxidation to polyhydroxyalkanoate (PHA) biosynthesis. PhaJ1Pp from Pseudomonas putida shows a broader substrate specificity
physiological function
(R)-specific enoyl-coenzyme A (enoyl-CoA) hydratases (PhaJs) are capable of supplying monomers from fatty acid beta-oxidation to polyhydroxyalkanoate (PHA) biosynthesis. PhaJ1Pp from Pseudomonas putida shows a broader substrate specificity
physiological function
Bacillus cereus accumulates polyhydroxyalkanoate (PHA). The MaoC-like protein has an R-specific enoyl-CoA hydratase activity and is referred to as PhaJ when involved in the PHA metabolism. In an in vivo assay using Escherichia coli as a host for PHA accumulation, the recombinant strain expressing PhaJYB4 and PHA synthase leads to increased PHA accumulation, suggesting that PhaJYB4 functioned as a monomer supplier
physiological function
comparison of the enzymes from Pseudomonas putida with residue 72Val resulting in increased preference for enoyl-coenzyme A substrates with shorter chain lengths and Pseudomonas aeruginosa with residue 72Ile resulting in an increased preference for enoyl-CoAs with longer chain lengths
physiological function
comparison of the enzymes from Pseudomonas putida with residue Val72 resulting in increased preference for enoyl-coenzyme A substrates with shorter chain lengths and Pseudomonas aeruginosa with residue Ile72 resulting in an increased preference for enoyl-CoAs with longer chain lengths
physiological function
role of the monofunctional peroxisomal enoyl-CoA hydratase 2 in compensated cell enlargement (CCE). Enzyme ECH2 alone likely promotes CCE during the post-mitotic cell expansion stage of cotyledon development, probably by converting indolebutyric acid to indole acetic acid
physiological function
-
Bacillus cereus accumulates polyhydroxyalkanoate (PHA). The MaoC-like protein has an R-specific enoyl-CoA hydratase activity and is referred to as PhaJ when involved in the PHA metabolism. In an in vivo assay using Escherichia coli as a host for PHA accumulation, the recombinant strain expressing PhaJYB4 and PHA synthase leads to increased PHA accumulation, suggesting that PhaJYB4 functioned as a monomer supplier
-
physiological function
-
(R)-specific enoyl-CoA hydratase mediates polyhydroxyalkanoate mobilization in Haloferax mediterranei. Enoyl coenzyme A (enoyl-CoA) hydratases (ECHs) reversibly catalyze the syn and anti hydration of 2-enoyl-CoA to produce (S)- or (R)-3-hydroxyacyl-CoA (3HA-CoA). The (S)-specific ECHs (S-ECHs, EC 4.2.1.17) are involved in fatty acid beta-oxidation. Through catalyzing the hydration of intermediates in fatty acid beta-oxidation, the (R)-specific ECHs (R-ECHs) may play an important role in fatty acid metabolism in eukaryotes and in polyhydroxyalkanoate (PHA) biosynthesis in bacteria. Function of PhaJ1 on PHA mobilization
-
physiological function
-
role of the monofunctional peroxisomal enoyl-CoA hydratase 2 in compensated cell enlargement (CCE). Enzyme ECH2 alone likely promotes CCE during the post-mitotic cell expansion stage of cotyledon development, probably by converting indolebutyric acid to indole acetic acid
-
physiological function
-
MFE2 consists of a (3R)-hydroxyacyl-CoA dehydrogenase, HD, domain, a (2E)-enoyl-CoA hydratase 2, H2, domain, and a sterol carrier protein 2-like domain, and is known to catalyze the second and third steps of the peroxisomal beta-oxidation of fatty acids and their derivatives
-
additional information
-
D-bifunctional enzyme is R-specific, while L-bifunctional enzyme is S-specific
additional information
-
MFE2 hydratase is R-specific, while MFE1 hydratase is S-specific
additional information
contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview
additional information
contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview
additional information
-
contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview
additional information
contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview. Active site and acyl-chain-binding pocket structure
additional information
-
contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview. Active site and acyl-chain-binding pocket structure