EC Number   |
General Information |
Reference |
|---|
    4.2.1.116 | evolution |
Ms3HPCD shows an overall structure and the CoA-binding mode similar to other enoyl-CoA hydratase (ECH) family enzymes, but compared with the other ECHs, Ms3HPCD has a tightly formed alpha3 helix near the active site, and bulky aromatic residues are located at the enoyl-group binding site, resulting in the enzyme having an optimal substrate binding site for accepting short chain 3-hydroxyacyl-CoA as a substrate. Phylogenetic tree analysis. The 3HPCD homologues from the phylum Crenarchaeota have an enoyl-group binding pocket similar to that of bacterial short-chain ECHs |
-, 749360 |
| 4.2.1.116 | metabolism |
propionyl-CoA is a key precursor for 3-hydroxypropanoate formation |
746207 |
| 4.2.1.116 | more |
molecular docking simulations of 3-hydroxypropanoyl-CoA and (S)-3-hydroxybutyryl-CoA to Ms3HPCD structure, overview. When (R)-3-hydroxybutyryl-CoA is used as a substrate, the positions of the 3-hydroxyl-group and the C4-moiety are reversed each other, resulting in improper positioning of the (R)-3-hydroxybutyryl-moiety in the pocket. Structural comparison of Ms3HPCD with other enoyl-CoA hydratases, Structural basis for 3-hydroxypropanoyl-CoA substrate specificity of Ms3HPCD and active site structure, overview. Glutamate residues, Glu113 and Glu133, which act as catalytic acid and base, respectively, are positioned at the active site of Ms3HPCD |
-, 749360 |
| 4.2.1.116 | more |
yeast two-hybrid assay for protein interaction analysis of 3-hydroxypropionyl-CoA dehydratase and 3-hydroxypropionyl-CoA synthetase (HPCS-HPCD), method optimization, metabolic engineering, overview |
-, 745689 |
| 4.2.1.116 | physiological function |
3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle fixes CO2 in extremely thermoacidophilic archaea and holds promise for metabolic engineering because of its thermostability and potentially rapid pathway kinetics. Modelling of the reactions and kinetics of five of the cycle enzymes: malonyl-CoA/succinyl-CoA reductase, 3-hydroxypropionyl-CoA synthetase, 3-hydroxypropionyl-CoA dehydratase, acryloyl-CoA reductase, and succinic semialdehyde reductase, that are recombinantly expressed in Escherichia coli. Reaction kinetics model of the 3HP/4HB cycle, overview |
-, 745689 |
| 4.2.1.116 | physiological function |
Metallosphaera sedula is a thermoacidophilic autotrophic archaeon known to utilize the 3-hydroxypropionate/4-hydroxybutyrate cycle (3-HP/4-HB cycle) as carbon fixation pathway. 3-Hydroxypropionyl-CoA dehydratase (3HPCD) is an enzyme involved in the 3-HP/4-HB cycle by converting 3-hydroxypropionyl-CoA to acryloyl-CoA |
-, 749360 |
