1309470-49-2Relevant academic research and scientific papers
Stereochemistry and mechanism of a microbial phenylalanine aminomutase
Ratnayake, Nishanka Dilini,Wanninayake, Udayanga,Geiger, James H.,Walker, Kevin D.
supporting information; experimental part, p. 8531 - 8533 (2011/07/29)
The stereochemistry of a phenylalanine aminomutase (PAM) on the andrimid biosynthetic pathway in Pantoea agglomerans (Pa) is reported. PaPAM is a member of the 4-methylidene-1H-imidazol-5(4H)-one (MIO)-dependent family of catalysts and isomerizes (2S)-α-phenylalanine to (3S)-β-phenylalanine, which is the enantiomer of the product made by the mechanistically similar aminomutase TcPAM from Taxus plants. The NH2 and pro-(3S) hydrogen groups at Cα and Cβ, respectively, of the substrate are removed and interchanged completely intramolecularly with inversion of configuration at the migration centers to form β-phenylalanine. This is a contrast to the retention of configuration mechanism followed by TcPAM.
