EC number:4.4.1.25
Enzyme
Download| EC Tree |
| 4. Lyases |
| 4.4 Carbon-sulfur lyases |
| 4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date) |
| ID: | 4.4.1.25 |
|---|---|
| Description: | L-cysteate sulfo-lyase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.4.1.25 |
| BRENDA Enzyme Link: | BRENDA 4.4.1.25 |
| KEGG Enzyme Link: | KEGG4.4.1.25 |
| BioCyc Enzyme Link: | BioCyc 4.4.1.25 |
| ExPASy Enzyme Link: | ExPASy4.4.1.25 |
| EC2PDB Enzyme Link: | EC2PDB 4.4.1.25 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.4.1.25 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.4.1.25 |
| IntEnz Enzyme Link: | IntEnz 4.4.1.25 |
| MEDLINE Enzyme Link: | MEDLINE 4.4.1.25 |
| RHEA:13441 | H2O + L-cysteate = H(+) + NH4(+) + pyruvate + sulfite |
| RULE(radius=1) | [*:1]-[S;H0;+0:2](=[*:3])(=[O;H0;+0:4])-[CH2;+0:5]-[CH;+0:6](-[*:7])-[NH2;+0:8].[OH2;+0:9]>>[*:7]-[C;H0;+0:6](-[CH3;+0:5])=[O;H0;+0:9].[*:1]-[S;H0;+0:2](=[*:3])-[OH;+0:4].[NH3;+0:8] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| L-cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T). | Denger K, Smits TH, Cook AM | 2006 Mar 15 | 16302849 |