EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.5.4.6 | ADP | wild-type and trinitrobenzene sulfonic acid-desensitized enzyme | Oryctolagus cuniculus | |
3.5.4.6 | native muscle proteinase | limited cleavage increases enzyme activity in presence of low concentrations of K+, probably due to removal of a fragment from the enzyme, which holds the enzyme in an inactive state, cleavage occurs e.g. during storage of both the muscle and the purified enzyme | Oryctolagus cuniculus | |
3.5.4.6 | Trypsin | limited cleavage increases enzyme activity in presence of low concentrations of K+, probably due to removal of a fragment from the enzyme, which holds the enzyme in an inactive state | Oryctolagus cuniculus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.4.6 | 5,5-dithio-bis(2-nitrobenzoic acid) | reaction with thiol groups, leads to a decrease of 20-30% in Vmax | Oryctolagus cuniculus | |
3.5.4.6 | ATP | connection between the operation of the hypothesized anionic activating site, responsible for positive homotropic cooperativity, and the inhibition exerted by anionic compounds that compete for the same site, among them ATP is most efficient, no inhibition of the trinitrobenzene sulfonic acid-desensitized enzyme | Oryctolagus cuniculus | |
3.5.4.6 | GTP | wild-type and trinitrobenzene sulfonic acid-desensitized enzyme | Oryctolagus cuniculus | |
3.5.4.6 | trinitrobenzene sulfonic acid | regulatory function on activity and inhibition by other compounds, e.g. ATP, overview | Oryctolagus cuniculus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.4.6 | additional information | - |
additional information | kinetics | Oryctolagus cuniculus | |
3.5.4.6 | 0.9 | - |
AMP | pH 6.5, 20°C, wild-type enzyme | Oryctolagus cuniculus | |
3.5.4.6 | 1 | - |
AMP | pH 6.5, 20°C, trinitrobenzene sulfonic acid-treated enzyme | Oryctolagus cuniculus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.4.6 | KCl | stimulates, no stimulation of the trinitrobenzene sulfonic acid-desensitized enzyme due to blockage of the activation anionic site | Oryctolagus cuniculus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.5.4.6 | 310000 | - |
- |
Oryctolagus cuniculus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.4.6 | Oryctolagus cuniculus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.4.6 | - |
Oryctolagus cuniculus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.5.4.6 | skeletal muscle | from back and hind leg | Oryctolagus cuniculus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.5.4.6 | 1100 | - |
purified enzyme | Oryctolagus cuniculus |
EC Number | Storage Stability | Organism |
---|---|---|
3.5.4.6 | storage of the muscle material as well as the purified enzyme increases the enzyme activity due to limited proteolytic cleavage | Oryctolagus cuniculus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.4.6 | AMP + H2O | - |
Oryctolagus cuniculus | IMP + NH3 | - |
? | |
3.5.4.6 | additional information | 6 lysine residues are critical for the pH-dependent positive homotropic cooperativity behaviour of the enzyme, the lysines form a regulatory anionic site to which AMP must bind to stimulate the enzyme at alkaline pH | Oryctolagus cuniculus | ? | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.4.6 | 20 | - |
assay at | Oryctolagus cuniculus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.5.4.6 | additional information | - |
treatment of the enzyme with trinitrobenzene sulfonic acid at pH 7.2 results in a progressive increase in activity at pH 7.1, no effect on activity at pH 6.5 | Oryctolagus cuniculus |
3.5.4.6 | 6.5 | - |
- |
Oryctolagus cuniculus |