EC number:3.1.3.53
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.1 Acting on ester bonds |
| 3.1.3 Phosphoric-monoester hydrolases |
| ID: | 3.1.3.53 |
|---|---|
| Description: | [Myosin-light-chain] phosphatase. |
| Alternative Name: |
Myosin phosphatase. Myosin light-chain kinase phosphatase. |
| Cath: | 3.60.21.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.1.3.53 |
| BRENDA Enzyme Link: | BRENDA 3.1.3.53 |
| KEGG Enzyme Link: | KEGG3.1.3.53 |
| BioCyc Enzyme Link: | BioCyc 3.1.3.53 |
| ExPASy Enzyme Link: | ExPASy3.1.3.53 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.3.53 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.3.53 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.3.53 |
| IntEnz Enzyme Link: | IntEnz 3.1.3.53 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.3.53 |
| RHEA:53988 | [myosin light chain]-O-phospho-L-threonine + H2O = [myosin light chain]-L-threonine + phosphate |
| RULE(radius=1) | [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. The effect of calmodulin binding to myosin light chain kinase on dephosphorylation. | Pato MD, Adelstein RS | 1983 Jun 10 | 6304072 |
| A myofibrillar protein phosphatase from rabbit skeletal muscle contains the beta isoform of protein phosphatase-1 complexed to a regulatory subunit which greatly enhances the dephosphorylation of myosin. | Dent P, MacDougall LK, MacKintosh C, Campbell DG, Cohen P | 1992 Dec 15 | 1336456 |
| The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. | Alessi D, MacDougall LK, Sola MM, Ikebe M, Cohen P | 1992 Dec 15 | 1336455 |
| RHEA:12849 | [myosin light chain]-O-phospho-L-serine + H2O = [myosin light chain]-L-serine + phosphate |
| RULE(radius=1) | [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. The effect of calmodulin binding to myosin light chain kinase on dephosphorylation. | Pato MD, Adelstein RS | 1983 Jun 10 | 6304072 |
| A myofibrillar protein phosphatase from rabbit skeletal muscle contains the beta isoform of protein phosphatase-1 complexed to a regulatory subunit which greatly enhances the dephosphorylation of myosin. | Dent P, MacDougall LK, MacKintosh C, Campbell DG, Cohen P | 1992 Dec 15 | 1336456 |
| The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. | Alessi D, MacDougall LK, Sola MM, Ikebe M, Cohen P | 1992 Dec 15 | 1336455 |