EC Number   |
Protein Variants |
Reference |
|---|
   2.3.1.194 | C115A |
consumption of malonyl-CoA and an increase in acetyl-CoA. No formation of CoA or acetoacetyl-CoA. C115A mutant enzyme yields acetyl-CoA via its malonyl-CoA decarboxylation activity, presumably by the His256 and Asn286 residues, while it has lost its condensation activity |
706551 |
| 2.3.1.194 | C115A |
site-directed mutagenesis, the mutant cleaves malonyl-CoA into acetyl-CoA, but does not form CoA or acetoacetyl-CoA. C115A mutant enzyme yields acetyl-CoA via its malonyl-CoA decarboxylation activity, presumably by the His256 and Asn286 residues, while it has lost its condensation activity |
706551 |
| 2.3.1.194 | H256A |
can not ve obtained as a soluble protein |
706551 |
| 2.3.1.194 | H256A |
site-directed mutagenesis, the mutant enzyme exhibits acetoacetyl-CoA synthesizing activity, but its specific activity is approximately 40fold lower than that of wild-type NphT7 |
706551 |
| 2.3.1.194 | more |
engineering the production of polyhydroxyalkanoates (PHAs) into high biomass bioenergy crops has the potential to provide a sustainable supply of bioplastics and energy from a single plant feedstock. One of the major challenges in engineering C4 plants for the production of poly[(R)-3-hydroxybutyrate] (PHB) is the significantly lower level of polymer produced in the chloroplasts of mesophyll cells compared to bundle sheath cells, thereby limiting the full PHB yield potential of the plant. The access to substrate for PHB synthesis may limit polymer production in mesophyll cell chloroplasts. The use of an acetoacetyl-CoA synthase, that catalyses the conversion of acetyl-CoA and malonyl-CoA to acetoacetyl-CoA with the release of carbon dioxide, in place of a beta-ketothiolase, the first enzyme in the bacterial PHA pathway, enhances poly-3-hydroxybutyrate production in sugarcane mesophyll cells. The engineered cells shows increased production of PHB and increased polymer molecular weight. PhaA is the main contributor to low PHB yield in mesophyll cells. Phenotypes of transgenic sugarcane leafs, overview |
746014 |
| 2.3.1.194 | more |
heterologous expression of different nphT7 homologues for farnesene production. acetoacetyl-CoA synthase from might increase the flux through the mevalonate pathway, effect of acetoacetyl-CoA synthase on growth as well as the production of farnesene, overview. While plasmid-based expression of nphT7 does not improve final farnesene titers, the construction of an alternative pathway, which exclusively relies on the malonyl-CoA bypass, was detrimental for growth and farnesene production. The overall functionality of the bypass is limited by the efficiency of acetoacetyl-CoA synthase. Gene nphT7 from Streptomyces glaucescens shows clearly higher efficiency compared to Streptomyces sp. strain CL190, overview |
745496 |
| 2.3.1.194 | more |
heterologous expression of different nphT7 homologues for farnesene production. acetoacetyl-CoA synthase might increase the flux through the mevalonate pathway, effect of acetoacetyl-CoA synthase on growth as well as the production of farnesene, overview. While plasmid-based expression of nphT7 does not improve final farnesene titers, the construction of an alternative pathway, which exclusively relies on the malonyl-CoA bypass, was detrimental for growth and farnesene production. The overall functionality of the bypass is limited by the efficiency of acetoacetyl-CoA synthase. Gene nphT7 from Streptomyces glaucescens shows clearly higher efficiency compared to Streptomyces sp. strain CL190, overview |
745496 |
| 2.3.1.194 | N286A |
site-directed mutagenesis, the mutant cannot be produced recombionantly as a soluble protein |
706551 |
| 2.3.1.194 | N286A |
this mutant enzyme exhibits detectable acetoacetyl-CoA synthesizing activity, but its specific is approximately 40fold lower than that of wild-type NphT7 |
706551 |
