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Literature summary for 4.2.1.119 extracted from

  • Liu, G.; Cai, S.; Hou, J.; Zhao, D.; Han, J.; Zhou, J.; Xiang, H.
    Enoyl-CoA hydratase mediates polyhydroxyalkanoate mobilization in Haloferax mediterranei (2016), Sci. Rep., 6, 24015 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.119

Cloned(Commentary)

Cloned (Comment) Organism
gene phaJ or HFX_1483, DNA and amino acid sequence determination and analysis, genetic analysis of putative R-ECH homologous proteins encoded by genes HFX_2901, 5217, 6361, and 6433, Haloferax mediterranei

Protein Variants

Protein Variants Comment Organism
additional information polyhydroxyalkanoate contents are slightly reduced in a phaJ deletion mutant DELTAphaJ1 compared to wild-type. phaJ1 gene complementation is performed in Haloferax mediterranei EPSDELTAphaJ1. GC analysis demonstrates that the mutant strain Haloferax mediterranei EPSDELTAphaJ1 utilizes much less amount of accumulated PHA than that of the wild-type Haloferax mediterranei EPS. In contrast, compared to the strain Haloferax mediterranei EPSDELTAphaJ (pWL502) harboring empty plasmid, the phaJ1 complementation strain Haloferax mediterranei EPSDELTAphaJ1 (pWLJ1) harboring the PhaJ1-expression plasmid significantly increases PHA degradation Haloferax mediterranei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2E)-2-enoyl-CoA + H2O Haloferax mediterranei
-
 (3R)-3-hydroxyacyl-CoA
-
 r
(2E)-2-enoyl-CoA + H2O Haloferax mediterranei ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
-
 (3R)-3-hydroxyacyl-CoA
-
 r

Organism

Organism UniProt Comment Textmining
Haloferax mediterranei I3R4N1 i.e. Halobacterium mediterranei
-
Haloferax mediterranei ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4 I3R4N1 i.e. Halobacterium mediterranei
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E)-2-enoyl-CoA + H2O
-
 Haloferax mediterranei (3R)-3-hydroxyacyl-CoA
-
 r
(2E)-2-enoyl-CoA + H2O
-
 Haloferax mediterranei ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4 (3R)-3-hydroxyacyl-CoA
-
 r

Synonyms

Synonyms Comment Organism
(R)-specific ECH
-
 Haloferax mediterranei
(R)-specific enoyl-CoA hydratase
-
 Haloferax mediterranei
HFX_1483
-
 Haloferax mediterranei
phaJ
-
 Haloferax mediterranei
PhaJ1
-
 Haloferax mediterranei
R-ECH
-
 Haloferax mediterranei

General Information

General Information Comment Organism
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 Haloferax mediterranei
malfunction polyhydroxyalkanoate contents are slightly reduced in a phaJ deletion mutant DELTAphaJ1 compared to wild-type Haloferax mediterranei
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 Haloferax mediterranei
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 Haloferax mediterranei