EC Number   |
|---|
    5.4.3.10 | crystal structure analysis of TcdPAM, PDB ID 3NZ4 |
| 5.4.3.10 | crystal structure analysis of TcPAM mutants, PDB IDs 4V2R and 4V2Q |
| 5.4.3.10 | 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 |
| 5.4.3.10 | 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 |
