D-lysine 5,6-aminomutase
| D-lysine 5,6-aminomutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 5.4.3.4 | ||||||||
| CAS number | 9075-70-1 | ||||||||
| 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 / EGO | ||||||||
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| D-Lysine 5,6-aminomutase alpha subunit | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of lysine 5,6-aminomutase in complex with plp, cobalamin, and 5'-deoxyadenosine | |||||||||
| Identifiers | |||||||||
| Symbol | Lys-AminoMut_A | ||||||||
| Pfam | PF09043 | ||||||||
| InterPro | IPR015130 | ||||||||
| |||||||||
In enzymology, a D-lysine 5,6-aminomutase (EC 5.4.3.4) is an enzyme that catalyzes the chemical reaction
- D-lysine 2,5-diaminohexanoate
Hence, this enzyme has one substrate, D-lysine, and one product, 2,5-diaminohexanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is D-2,6-diaminohexanoate 5,6-aminomutase. Other names in common use include D-alpha-lysine mutase, and adenosylcobalamin-dependent D-lysine 5,6-aminomutase. This enzyme participates in lysine degradation. It employs one cofactor, cobamide.
Structure
The structure of the alpha subunit is predominantly a PLP-binding TIM barrel domain, with several additional alpha-helices and beta-strands at the N and C termini. These helices and strands form an intertwined accessory clamp structure that wraps around the sides of the TIM barrel and extends up toward the Ado ligand of the Cbl cofactor, providing most of the interactions observed between the protein and the Ado ligand of the Cbl, suggesting that its role is mainly in stabilising AdoCbl in the precatalytic resting state.[1]
References
- ↑ Berkovitch F, Behshad E, Tang KH, Enns EA, Frey PA, Drennan CL (2004). "A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase.". Proc Natl Acad Sci U S A. 101 (45): 15870–5. doi:10.1073/pnas.0407074101. PMC 528771
. PMID 15514022.
Further reading
- Morley CG, Stadtman TC (1970). "Studies on the fermentation of D-alpha-lysine. Purification and properties of an adenosine triphosphate regulated B 12-coenzyme-dependent D-alpha-lysine mutase complex from Clostridium sticklandii". Biochemistry. 9 (25): 4890–900. doi:10.1021/bi00827a010. PMID 5480154.
- Stadtman TC, Tsai L (1967). "A cobamide coenzyme dependent migration of the epsilon-amino group of D-lysine". Biochem. Biophys. Res. Commun. 28 (6): 920–6. doi:10.1016/0006-291X(67)90067-8. PMID 4229021.
This article incorporates text from the public domain Pfam and InterPro IPR015130