EC 5.4.3.11 - Phenylalanine aminomutase (D-β-phenylalanine forming)

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 5.4.3.11

Names

Accepted name:
phenylalanine aminomutase (D-β-phenylalanine forming)
Other names:
admH (gene name)
L-phenylalanine 2,3-aminomutase [(S)-3-amino-3-phenylpropanoate]
Systematic name:
L-phenylalanine 2,3-aminomutase [(S)-3-amino-3-phenylpropanoate-forming]

Reaction

Cofactor

Comments:

The enzyme from the bacterium Pantoea agglomerans produces D-β-phenylalanine, an intermediate in the biosynthesis of the polyketide non-ribosomal antibiotic andrimid. The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.10, phenylalanine aminomutase (L-β-phenylalanine forming).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB

References

  1. Ratnayake, N. D., Wanninayake, U., Geiger, J. H., Walker, K. D.
    Stereochemistry and mechanism of a microbial phenylalanine aminomutase.
    J. Am. Chem. Soc. 133 : 8531-8533 (2011). [PMID: 21561099]

[EC 5.4.3.11 created 2013]