Crystallization (Comment) | Organism |
---|---|
using the crstal structure with PDB ID 1BQ6 for structure-function analysis, overview | Medicago sativa |
Protein Variants | Comment | Organism |
---|---|---|
F215S | the mutation does not significantly alter the Kd for CoA or acetyl-CoA binding, but dramatically alters the turnover rates for malonyl-CoA decarboxylation compared to the wild-type enzyme | Medicago sativa |
F215Y | the mutation does not significantly alter the Kd for CoA or acetyl-CoA binding, but dramatically alters the turnover rates for malonyl-CoA decarboxylation compared to the wild-type enzyme | Medicago sativa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3 malonyl-CoA + 4-coumaroyl-CoA | Medicago sativa | - |
4 CoA + naringenin chalcone + 3 CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Medicago sativa | P30074 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2 | reaction mechanism analysis by quantum mechanics calculations, overview. In loading step, only a tetrahedral intermediate is located without transition state. His303 acts as a H31 donor, but not a hydrogen bond donor, to stabilize the intermediate formation. In decarboxylation step, the reaction proceeds via a transition state and is sensitive to the environment. In elongation step, a tetrahedral transition state is located, structure-function analysis, overview | Medicago sativa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3 malonyl-CoA + 4-coumaroyl-CoA | - |
Medicago sativa | 4 CoA + naringenin chalcone + 3 CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
chalcone synthase | - |
Medicago sativa |
CHS | - |
Medicago sativa |