Beta-lysine 5,6-aminomutase
| beta-lysine 5,6-aminomutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.3.3 | ||||||||
| CAS no. | 9075-69-8 | ||||||||
| 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 beta-lysine 5,6-aminomutase (EC 5.4.3.3) is an enzyme that catalyzes the chemical reaction
- (3S)-3,6-diaminohexanoate (3S,5S)-3,5-diaminohexanoate
Hence, this enzyme has one substrate, (3S)-3,6-diaminohexanoate, and one product, (3S,5S)-3,5-diaminohexanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is (3S)-3,6-diaminohexanoate 5,6-aminomutase. Other names in common use include beta-lysine mutase, and L-beta-lysine 5,6-aminomutase. This enzyme participates in lysine degradation. It employs one cofactor, cobamide.
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1XRS.
References
[edit]- Retey J, Kunz F, Arigoni D, Stadtman TC (1978). "Zur Kenntnis der beta-Lysin-Mutase-Reaktion: mechanismus und sterischer Verlauf". Helv. Chim. Acta. 61 (8): 2989–2998. doi:10.1002/hlca.19780610824.
- Stadtman TC, Renz P (1968). "Anaerobic degradation of lysine. V. Some properties of the cobamide coenzyme-dependent beta-lysine mutase of Clostridium sticklandii". Arch. Biochem. Biophys. 125 (1): 226–39. doi:10.1016/0003-9861(68)90657-7. PMID 5649516.
