TABLE 3.
Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula
| Organism and enzymea | Substrates | Products | Specific activity (U/mg)b | Apparent Km (μM) | Optimum pH | Turnover (s−1) | Native molecular mass (kDa [calculated])c | Composition | Specificity (%) |
|---|---|---|---|---|---|---|---|---|---|
| S. tokodaii acryloyl-CoA reductase | Acryloyl-CoA, NADPH, H+ | Propionyl-CoA, NADP+ | 18.7 | Acryloyl-CoA, <10; NADPH, 36 | 6 | 13 | 43 (36) | Monomer | Acryloyl-CoA 100; crotonyl-CoA, <1 |
| M. sedula 3-hydroxypropionyl-CoA dehydratase | 3-Hydroxypropionyl-CoA, (S)-3-hydroxybutyryl-CoA | Acryloyl-CoA, crotonyl-CoA, H2O | 151 | 3-Hydroxypropionyl-CoA, 60; (S)-3-hydroxybutyryl-CoA, 75 | 8.1 | 96 | 23 (31) | Monomer | 3-Hydroxypropionyl-CoA, 100; (S)-3-hydroxybutyryl-CoA, 100; (R)-3-hydroxybutyryl-CoA, <1 |
a
Accession numbers are ST0480 for the S. tokodaii reductase and Msed_2001 for the M. sedula dehydratase.
b
Activities were determined using the respective photometric assay at 65°C.
c
Determined by gel filtration.