Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-phenylalanine | acts as an allosteric inhibitor of muscle isozyme and induces the enzyme to exist in multiple conformations by locking it in an expanded or asymmetric conformation, which is contrary effect to that of phosphoenolpyruvate binding | Oryctolagus cuniculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | required | Oryctolagus cuniculus | |
Mg2+ | required | Oryctolagus cuniculus | |
additional information | enzyme spectra in the absence and presence of activating cations, overview | 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 | - |
- |
- |
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 | secondary and tertiary structure of muscle isozyme homotetramer and the four monomers with three tryptophans Trp157, Trp481, and Trp514, and bound Mg2+ and K+ per monomer, 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 | - |
aassay 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 | catalysis by muscle pyruvate kinase involves domain movements and conformational changes induced by activating cations and its substrates. Fluorescence acrylamide quenching analyses reveal that interactions with Mg2+ and K+ lead to a more exposed active site of the enzyme while interactions with phosphoenolpyruvate and ADP decrease solvent accessibility of the active site, overview | Oryctolagus cuniculus |