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Literature summary for 3.1.3.53 extracted from
- The myosin-bound form of protein phosphatase 1 (PP-1M) is the enzyme that dephosphorylates native myosin in skeletal and cardiac muscles (1988), Biochim. Biophys. Acta, 971, 163-169.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | dominant activity is PP-2A | Bos taurus | 5829 | - |
| myofibril | PP-1M activity is associated with the myofibrillar fraction | Bos taurus | 30016 | - |
| myofibril | PP-1M activity is associated with the myofibrillar fraction | Oryctolagus cuniculus | 30016 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 110000 | - |
isoenzyme PP-1M, gel filtration | Oryctolagus cuniculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
isoenzyme PP-1M and PP-2A, not isoenzyme PP-1G | - |
| Oryctolagus cuniculus | - |
myosin-bound form PP-1M, glycogen-bound form PP-1G and PP-2A | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cardiac muscle | isoenzyme PP-1M accounts for 90% of the myosin phosphatase activity, isoenzyme PP-1G is essentially absent | Bos taurus | - |
| skeletal muscle | - |
Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| myosin light-chain phosphate + H2O | isozyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A | Bos taurus | myosin light-chain + phosphate | - |
? |  |
| myosin light-chain phosphate + H2O | isozyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A | Oryctolagus cuniculus | myosin light-chain + phosphate | - |
? | |
| myosin light-chain phosphate + H2O | isozyme PP-1G dephosphorylates myosin, myosin P-light-chain and phosphorylase A at comparable rates | Oryctolagus cuniculus | myosin light-chain + phosphate | - |
? | |
| myosin light-chain phosphate + H2O | PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A | Bos taurus | myosin light-chain + phosphate | - |
? | |
| myosin light-chain phosphate + H2O | PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A | Oryctolagus cuniculus | myosin light-chain + phosphate | - |
? | |
| phosphorylated myosin + H2O | isoenzyme PP-1G dephosphorylates myosin, myosin P-light-chain and phosphorylase A at comparable rates | Oryctolagus cuniculus | myosin + phosphate | - |
? | |
| phosphorylated myosin + H2O | isoenzyme PP-1M is more active towards native myosin than PP-1G | Oryctolagus cuniculus | myosin + phosphate | - |
? | |
| phosphorylated myosin + H2O | isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A | Bos taurus | myosin + phosphate | - |
? | |
| phosphorylated myosin + H2O | isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A | Oryctolagus cuniculus | myosin + phosphate | - |
? | |
| phosphorylated myosin + H2O | isoenzyme PP-2A: low activity with native myosin | Bos taurus | myosin + phosphate | - |
? | |
| phosphorylated myosin + H2O | isoenzyme PP-2A: low activity with native myosin | Oryctolagus cuniculus | myosin + phosphate | - |
? | |
| phosphorylated phoshorylase A + H2O | PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A | Bos taurus | phosphorylase A + phosphate | - |
? | |
| phosphorylated phoshorylase A + H2O | PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A | Oryctolagus cuniculus | phosphorylase A + phosphate | - |
? | |
| phosphorylated phoshorylase A + H2O | isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A | Bos taurus | phosphorylase A + phosphate | - |
? | |
| phosphorylated phoshorylase A + H2O | isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A | Oryctolagus cuniculus | phosphorylase A + phosphate | - |
? | |
| phosphorylated phoshorylase A + H2O | isoenzyme PP-1G dephosphorylates myosin, myosin P-light-chains and phosphorylase A at comparable rates | Oryctolagus cuniculus | phosphorylase A + phosphate | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Bos taurus |
| 30 | - |
assay at | Oryctolagus cuniculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Bos taurus |
| 7 | - |
assay at | Oryctolagus cuniculus |
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Release 2023.1 (January 2023)
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