Enzymic hydrolysis of ethyl 3-hydroxy-3-phenylpropanoate: observations on an enzyme active-site model

1992 ◽  
Vol 57 (15) ◽  
pp. 4289-4292 ◽  
Author(s):  
Neil W. Boaz

ChemInform ◽  
2010 ◽  
Vol 29 (4) ◽  
pp. no-no
Author(s):  
J. MORAVCOVA ◽  
Z. VANCLOVA ◽  
J. CAPKOVA ◽  
K. KEFURT ◽  
J. STANEK


1997 ◽  
Vol 16 (7) ◽  
pp. 1011-1028 ◽  
Author(s):  
Jitka Moravcová ◽  
Zita Vanclová ◽  
Jindra Čapková ◽  
Karel Kefurt ◽  
Jan Staněk


2000 ◽  
Vol 65 (10) ◽  
pp. 1619-1629 ◽  
Author(s):  
Jitka Moravcová ◽  
Karel Kefurt ◽  
Romana Hladůvková ◽  
Jan Staněk

Methyl 2,3,4-tri-O-acetyl-β-D-arabinopyranoside (1), methyl 2,3,4-tri-O-acetyl-β-D-ribopyranoside (2), and methyl 2,3,5-tri-O-acetyl-β-D-ribofuranoside (3) were deacetylated in porcine liver esterase-catalyzed reactions. Triacetate 1 gave methyl 3,4-di-O-acetyl-β-D-arabinopyranoside in 70% preparative yield while the regioselectivities found for the substrates 2 and 3 were substantially lower. Both the Michaelis constant and maximum rate were calculated for deacetylation of 1, 2, and 3. The results were interpreted using an active site model for the esterase proposed by Jones.



2002 ◽  
Vol 41 (21) ◽  
pp. 5513-5520 ◽  
Author(s):  
Seiji Ogo ◽  
Ryo Yamahara ◽  
Mark Roach ◽  
Tomoyoshi Suenobu ◽  
Michihiko Aki ◽  
...  


1991 ◽  
Vol 1 (5) ◽  
pp. 277-280 ◽  
Author(s):  
P. Chan ◽  
P. Cotelle ◽  
N. Cotelle ◽  
J.L. Bernier ◽  
J.P. Hénichart


Sign in / Sign up

Export Citation Format

Share Document