EC 5.4.3.3 - Lysine 5,6-aminomutase

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IntEnz Enzyme Nomenclature
EC 5.4.3.3

Names

Accepted name:
lysine 5,6-aminomutase
Other names:
β-lysine mutase
L-β-lysine 5,6-aminomutase
β-lysine 5,6-aminomutase
D-lysine 5,6-aminomutase
D-α-lysine mutase
adenosylcobalamin-dependent D-lysine 5,6-aminomutase
Systematic name:
(3S)-3,6-diaminohexanoate 5,6-aminomutase

Reactions

Cofactors

Comments:

This enzyme is a member of the 'AdoMet radical' (radical SAM) family. It requires pyridoxal 5'-phosphate and adenosylcobalamin for activity. A 5'-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of adenosylcobalamin, which is regenerated at the end of the reaction.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047702
CAS Registry Number: 9075-69-8
UniProtKB/Swiss-Prot:

References

  1. Retey, J., Kunz, F., Arigoni, D. and Stadtman, T.C.
    Zur Kenntnis der β-Lysin-Mutase-Reaktion: mechanismus und sterischer Verlauf.
    Helv. Chim. Acta 61: 2989-2998 (1978).
  2. Stadtman, T.C. and Renz, P.
    Anaerobic degradation of lysine. V. Some properties of the cobamide coenzyme-dependent β-lysine mutase of Clostridium sticklandii.
    Arch. Biochem. Biophys. 125: 226-239 (1968). [PMID: 5649516]
  3. Morley, C. G., Stadtman, T. C.
    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: 4890-4900 (1970). [PMID: 5480154]
  4. Chang, C. H., Frey, P. A.
    Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-lysine 5, 6-aminomutase from Clostridium sticklandii.
    J. Biol. Chem. 275: 106-114 (2000). [PMID: 10617592]
  5. Tang, K. H., Harms, A., Frey, P. A.
    Identification of a novel pyridoxal 5'-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis.
    Biochemistry 41: 8767-8776 (2002). [PMID: 12093296]
  6. Tang, K. H., Mansoorabadi, S. O., Reed, G. H., Frey, P. A.
    Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase.
    Biochemistry 48: 8151-8160 (2009). [PMID: 19634897]
  7. Berkovitch, F., Behshad, E., Tang, K. H., Enns, E. A., Frey, P. A., Drennan, C. L.
    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: 15870-15875 (2004). [PMID: 15514022]

[EC 5.4.3.3 created 1972 (EC 5.4.3.4 created 1972, incorporated 2017), modified 2017]