| S-adenosylhomocysteine deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.4.28 | ||||||||
| CAS no. | 125149-24-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a S-adenosylhomocysteine deaminase ( EC 3.5.4.28) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-homocysteine + H2O S-inosyl-L-homocysteine + NH3
Thus, the two substrates of this enzyme are S-adenosyl-L-homocysteine and H2O, whereas its two products are S-inosyl-L-homocysteine and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is S-adenosyl-L-homocysteine aminohydrolase. This enzyme is also called adenosylhomocysteine deaminase.
References
- Zulty JJ, Speedie MK (1989). "Purification and characterization of S-adenosylhomocysteine deaminase from streptonigrin-producing Streptomyces flocculus". J. Bacteriol. 171 (12): 6840–4. PMC 210584. PMID 2592350.
| S-adenosylhomocysteine deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.4.28 | ||||||||
| CAS no. | 125149-24-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a S-adenosylhomocysteine deaminase ( EC 3.5.4.28) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-homocysteine + H2O S-inosyl-L-homocysteine + NH3
Thus, the two substrates of this enzyme are S-adenosyl-L-homocysteine and H2O, whereas its two products are S-inosyl-L-homocysteine and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is S-adenosyl-L-homocysteine aminohydrolase. This enzyme is also called adenosylhomocysteine deaminase.
References
- Zulty JJ, Speedie MK (1989). "Purification and characterization of S-adenosylhomocysteine deaminase from streptonigrin-producing Streptomyces flocculus". J. Bacteriol. 171 (12): 6840–4. PMC 210584. PMID 2592350.