EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    4.2.1.116 | (S)-3-hydroxybutyryl-CoA |
no substrate: (R)-3-hydroxybutyryl-CoA |
Metallosphaera sedula |
crotonyl-CoA + H2O |
- |
? |
| 4.2.1.116 | 3-hydroxypropanoyl-CoA |
- |
Chloroflexus aurantiacus |
acryloyl-CoA + H2O |
- |
r |
| 4.2.1.116 | 3-hydroxypropanoyl-CoA |
- |
Metallosphaera sedula |
acryloyl-CoA + H2O |
- |
? |
| 4.2.1.116 | 3-hydroxypropanoyl-CoA |
- |
Metallosphaera sedula |
acryloyl-CoA + H2O |
- |
r |
| 4.2.1.116 | 3-hydroxypropanoyl-CoA |
- |
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2 |
acryloyl-CoA + H2O |
- |
r |
| 4.2.1.116 | more |
coupled assay of enzyme HPCD with 3-hydroxypropionyl-CoA synthetase (HPCS) and acryloyl-CoA reductase (ACR) |
Metallosphaera sedula |
? |
- |
? |
| 4.2.1.116 | more |
substrate specificity of enzyme Ms3HPCD, modelling of 3-hydroxypropanoyl- and (S)-3-hydroxybutyryl-moiety binding mode of enzyme Ms3HPCD. The residues involved in the formation of the 3-hydroxypropanoate binding pocket are identified. Ms3HPCD cannot convert (R)-stereoisomer of 3-hydroxybutyryl-CoA. 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. 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 |
Metallosphaera sedula |
? |
- |
? |
| 4.2.1.116 | more |
coupled assay of enzyme HPCD with 3-hydroxypropionyl-CoA synthetase (HPCS) and acryloyl-CoA reductase (ACR) |
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2 |
? |
- |
? |
| 4.2.1.116 | more |
substrate specificity of enzyme Ms3HPCD, modelling of 3-hydroxypropanoyl- and (S)-3-hydroxybutyryl-moiety binding mode of enzyme Ms3HPCD. The residues involved in the formation of the 3-hydroxypropanoate binding pocket are identified. Ms3HPCD cannot convert (R)-stereoisomer of 3-hydroxybutyryl-CoA. 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. 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 |
Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2 |
? |
- |
? |
