An aminomutase, naturally catalyzing the interconversion of (S)--phenylalanine and (R)--phenylalanine, was converted into an ammonia lyase catalyzing the nonoxidative deamination of phenylalanine to cinnamic acid by a rational single-point mutation. It could be shown by crystal structures and kinetic data that the flexibility of the lid that covers the active site decides whether the enzyme acts as a lyase or a mutase. An Arg92Ser mutation destabilized the closed conformation of the lid structure and converted the mutase into a lyase that exhibited up to 44-fold increased reaction rates in the enantioselective deamination of (R)--phenylalanine. In addition, the amination rates of cinnamic acid yielding optically pure (S)-- and (R)--phenylal...
We describe a simple and efficient enzymatic tandem reaction for the preparation of enantiomerically...
Engineered variants of phenylalanine ammonia lyase from Planctomyces brasiliensis were developed thr...
Ammonia lyases (AL) and aminomutases (AM) are emerging in green synthetic routes to chiral amines an...
An aminomutase, naturally catalyzing the interconversion of (S)--phenylalanine and (R)--phenylalanin...
Turn to switch: A mutant of phenylalanine aminomutase was engineered that can catalyze the regiosele...
Phenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyzes the c...
AbstractPhenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyz...
Enantiopure non-natural amino acids are valuable building blocks for the production of chemicals and...
The effect of extended reaction times on the regio- and enantioselectivity of the phenylalanine ammo...
Phenylalanine-2,3-aminomutase (PAM) from Taxus chinensis, a 4-methylidene-imidazole-5-one (MIO)-depe...
Enzymes of the class I lyase-like family catalyze the asymmetric addition of ammonia to arylacrylate...
Deciphering the structural features that functionally separate ammonia lyases from aminomutases is o...
We describe a simple and efficient enzymatic tandem reaction for the preparation of enantiomerically...
Engineered variants of phenylalanine ammonia lyase from Planctomyces brasiliensis were developed thr...
Ammonia lyases (AL) and aminomutases (AM) are emerging in green synthetic routes to chiral amines an...
An aminomutase, naturally catalyzing the interconversion of (S)--phenylalanine and (R)--phenylalanin...
Turn to switch: A mutant of phenylalanine aminomutase was engineered that can catalyze the regiosele...
Phenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyzes the c...
AbstractPhenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyz...
Enantiopure non-natural amino acids are valuable building blocks for the production of chemicals and...
The effect of extended reaction times on the regio- and enantioselectivity of the phenylalanine ammo...
Phenylalanine-2,3-aminomutase (PAM) from Taxus chinensis, a 4-methylidene-imidazole-5-one (MIO)-depe...
Enzymes of the class I lyase-like family catalyze the asymmetric addition of ammonia to arylacrylate...
Deciphering the structural features that functionally separate ammonia lyases from aminomutases is o...
We describe a simple and efficient enzymatic tandem reaction for the preparation of enantiomerically...
Engineered variants of phenylalanine ammonia lyase from Planctomyces brasiliensis were developed thr...
Ammonia lyases (AL) and aminomutases (AM) are emerging in green synthetic routes to chiral amines an...