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5.4.3.10: phenylalanine aminomutase (L-beta-phenylalanine forming)

This is an abbreviated version!
For detailed information about phenylalanine aminomutase (L-beta-phenylalanine forming), go to the full flat file.

Word Map on EC 5.4.3.10

Reaction

L-phenylalanine
=
L-beta-phenylalanine

Synonyms

(R)-PAM, (R)-selective PAM, admH, CctP, More, PAM, phenylalanine AM, phenylalanine aminomutase, phenylalanine-2,3-aminomutase, TcPAM

ECTree

     5 Isomerases
         5.4 Intramolecular transferases
             5.4.3 Transferring amino groups
                5.4.3.10 phenylalanine aminomutase (L-beta-phenylalanine forming)

Crystallization

Crystallization on EC 5.4.3.10 - phenylalanine aminomutase (L-beta-phenylalanine forming)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of TcdPAM, PDB ID 3NZ4
to 2.38 A resolution, space group C2. A (E)-cinnamate molecule is bound in the active site, lying above the 4-methylidene-1H-imidazol-5(4H)-one cofactor and under a loop region that includes residues 80-97, which define the top of the active site. The (E)-cinnamate molecule lies about 3.4 A above the methylidene carbon of the 4-methylidene-1H-imidazol-5(4H)-one moiety. The carboxylate of the cinnamate makes a salt bridge interaction with a strongly conserved residue R325, which serves to position the product in the active site. The plane of the aromatic ring of the cinnamate is displaced about 20° from the perpendicular relative to the pi-bond plane of the propenoate carboncarbon double bond. The aromatic ring is bound relatively loosely in the active site, making only one direct hydrophobic interaction with residue L104
crystal structure analysis of TcPAM mutants, PDB IDs 4V2R and 4V2Q
purified recombinant wild-type PAM in complex with (R)-beta-phenylalanine or with L-beta-Phe analogue (S)-3-amino-2,2-difluoro-phenylpropanoic acid, enzyme mutant Y80A complexed with (S)-3-amino-2,2-difluoro-phenylpropanoic acid, and MIO-less enzyme mutants N231A and Y322A, crystallization from 0.2-0.5 mM TCEP, pH 7.0, with or without 2.0-20 mM ligand, X-ray diffraction structure determination and analysis at 1.85-2.20 A resolution