EC Number   |
General Information |
Reference |
|---|
   4.2.1.119 | 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 |
-, 749314 |
| 4.2.1.119 | 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 |
-, 747321 |
| 4.2.1.119 | 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 |
-, 729029 |
| 4.2.1.119 | 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 |
-, 747869 |
| 4.2.1.119 | 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 |
-, 729029 |
| 4.2.1.119 | malfunction |
inactivating mutations of multifunctional enzyme type 2 hydratase lead to D-bifunctional protein deficiency type II |
730244 |
| 4.2.1.119 | malfunction |
polyhydroxyalkanoate contents are slightly reduced in a phaJ deletion mutant DELTAphaJ1 compared to wild-type |
-, 749314 |
| 4.2.1.119 | 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 |
-, 749314 |
| 4.2.1.119 | metabolism |
the enzyme is involved in the peroxisomal beta-oxidation of fatty acids and their derivatives |
-, 715528 |
| 4.2.1.119 | more |
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 |
746834 |
