EC |
5.4.3.10 |
Accepted name: |
phenylalanine aminomutase (L-β-phenylalanine forming) |
Reaction: |
L-phenylalanine = L-β-phenylalanine |
Glossary: |
L-β-phenylalanine = (R)-3-amino-3-phenylpropanoate |
Systematic name: |
L-phenylalanine 2,3-aminomutase [(R)-3-amino-3-phenylpropanoate-forming] |
Comments: |
The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO). This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.11, phenylalanine aminomutase (D-β-phenylalanine forming). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Feng, L., Wanninayake, U., Strom, S., Geiger, J. and Walker, K.D. Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase. Biochemistry 50 (2011) 2919–2930. [DOI] [PMID: 21361343] |
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[EC 5.4.3.10 created 2013] |
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EC |
5.4.3.11 |
Accepted name: |
phenylalanine aminomutase (D-β-phenylalanine forming) |
Reaction: |
L-phenylalanine = D-β-phenylalanine |
Glossary: |
D-β-phenylalanine = (S)-3-amino-3-phenylpropanoate |
Other name(s): |
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] |
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: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ratnayake, N.D., Wanninayake, U., Geiger, J.H. and Walker, K.D. Stereochemistry and mechanism of a microbial phenylalanine aminomutase. J. Am. Chem. Soc. 133 (2011) 8531–8533. [DOI] [PMID: 21561099] |
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[EC 5.4.3.11 created 2013] |
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