Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli strain BL21 | Oryctolagus cuniculus |
Protein Variants | Comment | Organism |
---|---|---|
W157A | site-directed mutagenesis, Trp157 is located in domain B and close to the active site | Oryctolagus cuniculus |
W481A/W514A | site-directed mutagenesis, Trp481 and Trp514 are located in domain C and close to the Y-interface | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | interactions with Mg2+ and K+ lead to more exposed tryptophan residues of PK while interactions with phosphoenolpyruvate and ADP decrease solvent accessibility of the tryptophan residues | Oryctolagus cuniculus | |
phenylalanine | allosteric inhibitor | Oryctolagus cuniculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | K+ is directly involved in the acquisition of the active conformation and movement of the B domain of the enzyme | Oryctolagus cuniculus | |
Mg2+ | required | Oryctolagus cuniculus | |
additional information | interaction of three Trp residues, Tr157, Trp481, and Trp514, with activating cations, overview. The majority of changes in tryptophan fluorescence signal from PK induced by the binding of activating cations come from Trp157. Interactions with Mg2+ and K+ lead to more exposed tryptophan residues of PK while interactions with phosphoenolpyruvate and ADP decrease solvent accessibility of the tryptophan residues | Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + pyruvate | Oryctolagus cuniculus | - |
ADP + phosphoenolpyruvate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes in Escherichia coli strain BL21 | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + pyruvate | - |
Oryctolagus cuniculus | ADP + phosphoenolpyruvate | - |
r |
Subunits | Comment | Organism |
---|---|---|
homotetramer | structure of muscle isozyme homotetramer and of the four monomers with Y-interface and Z-interface, each monomer consists of the N-terminal domain, domain A, domain B, and domain C, overview | Oryctolagus cuniculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
23 | - |
assay at | Oryctolagus cuniculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Oryctolagus cuniculus | |
ATP | - |
Oryctolagus cuniculus |
General Information | Comment | Organism |
---|---|---|
additional information | movement of the B domain is essential for the catalytic reaction. Rotation of the B domain in the opening of the cleft between domains B and A induced by the binding of activating cations allows substrates to bind, whereas substrate binding shifts the rotation of the B domain in the closure of the cleft. The enzyme exhibits a more dynamic structure after binding of activating metal ions and substrates, whereas binding of Phe decreases the dynamics | Oryctolagus cuniculus |
physiological function | catalytic allosteric mechanism, overview | Oryctolagus cuniculus |