| 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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1XRS.
References
- 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.
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