EC number:2.1.1.77
| ID: | 2.1.1.77 |
|---|---|
| Description: | Protein-L-isoaspartate(D-aspartate) O-methyltransferase. |
| Alternative Name: |
Protein L-isoaspartyl methyltransferase. Protein D-aspartate methyltransferase. Protein beta-aspartate O-methyltransferase. L-isoaspartyl protein carboxyl methyltransferase. |
| Prosite: | PDOC00985; |
| PDB: |
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| Cath: | 1.10.10.10; 3.30.1330.20; 3.30.1330.200; 3.55.20.10; 3.40.50.150; 3.40.50.180; 3.40.50.2300; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.1.77 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.77 |
| KEGG Enzyme Link: | KEGG2.1.1.77 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.77 |
| ExPASy Enzyme Link: | ExPASy2.1.1.77 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.77 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.77 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.77 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.77 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.77 |
| RHEA:12705 | [protein]-L-beta-isoaspartate + S-adenosyl-L-methionine = [protein]-L-beta-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and properties of protein methylaase II. | Kim S, Paik WK | 1970 Apr 10 | 5438363 |
| Protein carboxyl methyltransferases: two distinct classes of enzymes. | Clarke S | 1985 | 3896126 |
| Methylation at specific altered aspartyl and asparaginyl residues in glucagon by the erythrocyte protein carboxyl methyltransferase. | Ota IM, Ding L, Clarke S | 1987 Jun 25 | 3597386 |