Fig. 6: Molecular basis explaining the amination of the β-MeCA substrate by the mutants. | Nature Communications

Fig. 6: Molecular basis explaining the amination of the β-MeCA substrate by the mutants.

From: Direct asymmetric synthesis of β-branched aromatic α-amino acids using engineered phenylalanine ammonia lyases

Fig. 6

a Gibbs energy diagram of the cMD simulations projected onto the distance from the amino N of MIO to the αC of the substrates and the angle between MIO and the double bond of the substrates within the (β-MeCA)/(PcPAL-L256V-I460V) mutant. b the pocket volume detected during the US simulations of the (β-MeCA)/(PcPAL-L256V-I460V) complex. c Optimized pre-reaction states of β-MeCA in the PcPAL-L256V-I460V mutant using the Quantum Mechanics/Molecular Mechanics (QM/MM) methodology. d, e, f Gibbs energy diagram of the cMD simulations projected at the distance from βC of β-MeCA to amino acid 256 and the benzene ring center and amino acid 460 within the (β-MeCA)/(PcPAL-L256V-I460V) complex, (CA)/(PcPAL-WT) complex, and (β-MeCA)/(PcPAL-WT) complex respectively. Source data are provided in Source Data 3 to Source Data 5. CA cinnamic acid, β-MeCA β-methyl cinnamic acid, MIO 3,5-dihydro-5-methylidene-4H-imidazol-4-one.

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