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
Search PMC articles PubMed articles NCBI proteins

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
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In enzymology, a D-lysine 5,6-aminomutase (EC 5.4.3.4) is an enzyme that catalyzes the chemical reaction

D-lysine $\rightleftharpoons$ 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

1. 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