Chiral preference of cutinase in the reaction with phosphonate inhibitors.
Mannesse
M L
ML
Department of Enzymology and Protein Engineering, Utrecht University, The Netherlands.
de Haas
G H
GH
van der Hijden
H T
HT
Egmond
M R
MR
Verheij
H M
HM
D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors*; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D007536:Isomerism; D007700:Kinetics; D063065:Organophosphonates / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D017354:Point Mutation; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D063065:Organophosphonates; D011994:Recombinant Proteins; D002265:Carboxylic Ester Hydrolases; C019952:cutinase