ChemInform Abstract: Highly Efficient Asymmetric Reduction of Arylpropionic Aldehydes by Horse Liver Alcohol Dehydrogenase Through Dynamic Kinetic Resolution.

Highly Efficient ◽

Highly efficient asymmetric reduction of arylpropionic aldehydes by Horse Liver Alcohol Dehydrogenase through dynamic kinetic resolution

Chemical Communications ◽

10.1039/b712290j ◽

2007 ◽

pp. 4038 ◽

Cited By ~ 46

Author(s):

Daria Giacomini ◽

Paola Galletti ◽

Arianna Quintavalla ◽

Gabriele Gucciardo ◽

Francesca Paradisi

Keyword(s):

Alcohol Dehydrogenase ◽

Kinetic Resolution ◽

Asymmetric Reduction ◽

Dynamic Kinetic Resolution ◽

Highly Efficient ◽

Highly efficient coenzyme regeneration system for reduction of cyclohexanone by horse liver alcohol dehydrogenase in organic solvent

Biotechnology Letters ◽

10.1007/bf00180152 ◽

1993 ◽

Vol 15 (8) ◽

Cited By ~ 6

Author(s):

Toshiaki Itozawa ◽

Hideo Kise

Keyword(s):

Alcohol Dehydrogenase ◽

Organic Solvent ◽

Regeneration System ◽

Coenzyme Regeneration ◽

Highly Efficient ◽

Kinetic resolution of organosilicon compounds by stereoselective dehydrogenation with horse liver alcohol dehydrogenase

Applied Microbiology and Biotechnology ◽

10.1007/bf00174470 ◽

1992 ◽

Vol 38 (2) ◽

Cited By ~ 14

Author(s):

Toshiaki Fukui ◽

Min-Hua Zong ◽

Takuo Kawamoto ◽

Atsuo Tanaka

Keyword(s):

Alcohol Dehydrogenase ◽

Kinetic Resolution ◽

Organosilicon Compounds ◽

Chloroprothixene binding into the active site pocket of horse liver alcohol dehydrogenase

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19760928 ◽

1976 ◽

Vol 41 (3) ◽

pp. 928-940 ◽

Cited By ~ 1

Author(s):

J. Kovář ◽

L. Skurský ◽

K. Bláha

Keyword(s):

Alcohol Dehydrogenase ◽

Active Site ◽

Active Site Pocket ◽

Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)45387-8 ◽

1982 ◽

Vol 257 (23) ◽

pp. 14349-14358 ◽

Cited By ~ 1

Author(s):

H Eklund ◽

B V Plapp ◽

J P Samama ◽

C I Brändén

Keyword(s):

Alcohol Dehydrogenase ◽

Ternary Complex ◽

Activation and inactivation of horse liver alcohol dehydrogenase with pyridoxal compounds.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)42001-2 ◽

1975 ◽

Vol 250 (1) ◽

pp. 205-210

Author(s):

D C Sogin ◽

B V Plapp

Keyword(s):

Alcohol Dehydrogenase ◽

The Behavior of Horse Liver Alcohol Dehydrogenase in Guanidine Hydrochloride Solutions

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)94306-1 ◽

1969 ◽

Vol 244 (18) ◽

pp. 5034-5043

Author(s):

R W Green ◽

R H McKay

Keyword(s):

Alcohol Dehydrogenase ◽

Guanidine Hydrochloride ◽

Rate constants for a mechanism including intermediates in the interconversion of ternary complexes by horse liver alcohol dehydrogenase

Biochemistry ◽

10.1021/bi00470a005 ◽

1990 ◽

Vol 29 (18) ◽

pp. 4289-4295 ◽

Cited By ~ 70

Author(s):

V. Chandra Sekhar ◽

Bryce V. Plapp

Keyword(s):

Alcohol Dehydrogenase ◽

Rate Constants ◽

Ternary Complexes ◽

Synthetic model peptides of the noncatalytic zinc site of EE and SS isozymes of horse liver alcohol dehydrogenase: Interaction with cobalt (II) and nickel (II) ions

Journal of Inorganic Biochemistry ◽

10.1016/0162-0134(95)97417-o ◽

1995 ◽

Vol 59 (2-3) ◽

pp. 316

Author(s):

Grazyna Formicka ◽

Ralf Hoffmann ◽

Stephan Rawer ◽

Michael Zeppezauer

Keyword(s):

Alcohol Dehydrogenase ◽

Synthetic Model ◽

Horse Liver ◽

Zinc Site ◽

Model Peptides

Coordination geometry for cadmium in the catalytic zinc site of horse liver alcohol dehydrogenase: studies by PAC spectroscopy

European Biophysics Journal ◽

10.1007/bf00183458 ◽

1991 ◽

Vol 20 (4) ◽

Cited By ~ 16

Author(s):

R. Bauer ◽

H.W. Adolph ◽

I. Andersson ◽

E. Danielsen ◽

G. Formicka ◽

...

Keyword(s):

Alcohol Dehydrogenase ◽

Coordination Geometry ◽

Pac Spectroscopy ◽

Horse Liver ◽

Catalytic Zinc ◽

Zinc Site