EC Number   |
Protein Variants |
Reference |
|---|
   2.3.1.151 | A257G |
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme |
720639 |
| 2.3.1.151 | G339S |
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme |
720639 |
| 2.3.1.151 | G339V |
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme |
720639 |
| 2.3.1.151 | T133L |
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme |
720639 |
| 2.3.1.151 | T135A |
inactive enzyme |
704562 |
| 2.3.1.151 | T135F |
mutant functionally resemble the wild-type enzyme, albeit with reduced catalytic activities |
704562 |
| 2.3.1.151 | T135G |
inactive enzyme |
704562 |
| 2.3.1.151 | T135I |
inactive enzyme |
704562 |
| 2.3.1.151 | T135L |
a point mutation in the active site cavity transforms benzophenone synthase into a functional phenylpyrone synthase (PPS). The dramatic change in both substrate and product specificities of benzophenone synthase is rationalized by homology modeling. The mutation may open a new pocket that accommodates the phenyl moiety of the triketide intermediate but limits polyketide elongation to two reactions, resulting in phenylpyrone formation. kcat (substrate: benzoyl-CoA): 0.0086/sec, Km (benzoyl-CoA): 0.001 mM, Km (malonyl-CoA): 8.7 mM. In contrast to the wild-type enzyme, the T135L mutant forms phenylpyrone as a major product and only traces of 2,4,6-trihydroxybenzophenone when incubated with benzoyl-CoA and malonyl-CoA. T135L mutant is almost inactive with 3-hydroxybenzoyl-CoA |
704562 |
| 2.3.1.151 | T135N |
inactive enzyme |
704562 |
