Mutational analysis of phenylalanine ammonia lyase to improve reactions rates for various substrates.
Bartsch
Sebastian
S
Department of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, D-17487 Greifswald, Germany.
Bornscheuer
Uwe T
UT
D000588:Amines / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites / Q000235:genetics; D055162:Biocatalysis; D002264:Carboxylic Acids / Q000737:chemistry / Q000378:metabolism; D002934:Cinnamates / Q000737:chemistry / Q000378:metabolism*; D004252:DNA Mutational Analysis; D019020:Directed Molecular Evolution; D007700:Kinetics; D008958:Models, Molecular; D009154:Mutation / Q000235:genetics / Q000502:physiology; D028528:Petroselinum / Q000201:enzymology / Q000235:genetics; D010650:Phenylalanine Ammonia-Lyase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D013379:Substrate Specificity / Q000235:genetics
D000588:Amines; D002264:Carboxylic Acids; D002934:Cinnamates; D010650:Phenylalanine Ammonia-Lyase