EC number:4.1.1.50
| ID: | 4.1.1.50 | ||||
|---|---|---|---|---|---|
| Description: | Adenosylmethionine decarboxylase. | ||||
| Alternative Name: |
S-adenosyl-L-methionine decarboxylase. S-adenosyl-L-methionine carboxy-lyase. | ||||
| Prosite: | PDOC01038; | ||||
| PDB: |
|
||||
| Cath: | 3.30.160.750; 3.30.360.110; 3.30.360.50; 3.60.90.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.1.50 |
| BRENDA Enzyme Link: | BRENDA 4.1.1.50 |
| KEGG Enzyme Link: | KEGG4.1.1.50 |
| BioCyc Enzyme Link: | BioCyc 4.1.1.50 |
| ExPASy Enzyme Link: | ExPASy4.1.1.50 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.1.50 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.1.50 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.1.50 |
| IntEnz Enzyme Link: | IntEnz 4.1.1.50 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.1.50 |
| RHEA:15981 | H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[*:6].[H+;H0:7]>>[*:5]-[CH2;+0:4]-[*:6].[*:1]=[C;H0;+0:2]=[O;H0;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Escherichia coli S-adenosylmethionine decarboxylase. Subunit structure, reductive amination, and NH2-terminal sequences. | Anton DL, Kutny R | 1987 Feb 25 | 3546296 |
| Structural and mechanistic properties of E. coli adenosylmethionine decarboxylase. | Anton DL, Kutny R | 1988 | 3076348 |