Substitutions in a Flexible Loop of Horse Liver Alcohol Dehydrogenase Hinder the Conformational Change and Unmask Hydrogen Transfer†,‡

S. Ramaswamy; Doo-Hong Park; Bryce V. Plapp

doi:10.1021/bi991731i

Substitutions in a Flexible Loop of Horse Liver Alcohol Dehydrogenase Hinder the Conformational Change and Unmask Hydrogen Transfer†,‡

Biochemistry ◽

10.1021/bi991731i ◽

1999 ◽

Vol 38 (42) ◽

pp. 13951-13959 ◽

Cited By ~ 56

Author(s):

S. Ramaswamy ◽

Doo-Hong Park ◽

Bryce V. Plapp

Keyword(s):

Alcohol Dehydrogenase ◽

Conformational Change ◽

Hydrogen Transfer ◽

Horse Liver Alcohol Dehydrogenase ◽

Flexible Loop ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Substitutions of a buried glutamate residue hinder the conformational change in horse liver alcohol dehydrogenase and yield a surprising complex with endogenous 3′-Dephosphocoenzyme A

Archives of Biochemistry and Biophysics ◽

10.1016/j.abb.2018.07.003 ◽

2018 ◽

Vol 653 ◽

pp. 97-106 ◽

Cited By ~ 1

Author(s):

Yun Ho Kim ◽

David S. Gogerty ◽

Bryce V. Plapp

Keyword(s):

Alcohol Dehydrogenase ◽

Conformational Change ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Influence of anions and pH on the conformational change of horse liver alcohol dehydrogenase induced by binding of oxidized nicotinamide adenine dinucleotide: binding of chloride to the catalytic metal ion

Biochemistry ◽

10.1021/bi00355a020 ◽

1986 ◽

Vol 25 (7) ◽

pp. 1584-1588 ◽

Cited By ~ 21

Author(s):

Wolfgang Maret ◽

Michael Zeppezauer

Keyword(s):

Alcohol Dehydrogenase ◽

Conformational Change ◽

Nicotinamide Adenine Dinucleotide ◽

Metal Ion ◽

Nicotinamide Adenine ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Catalytic Metal

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Substitutions of Amino Acid Residues in the Substrate Binding Site of Horse Liver Alcohol Dehydrogenase Have Small Effects on the Structures but Significantly Affect Catalysis of Hydrogen Transfer

Biochemistry ◽

10.1021/acs.biochem.9b01074 ◽

2020 ◽

Vol 59 (7) ◽

pp. 862-879

Author(s):

Keehyuk Kim ◽

Bryce V. Plapp

Keyword(s):

Amino Acid ◽

Alcohol Dehydrogenase ◽

Binding Site ◽

Hydrogen Transfer ◽

Substrate Binding ◽

Amino Acid Residues ◽

Horse Liver Alcohol Dehydrogenase ◽

Substrate Binding Site ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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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 ◽

Horse Liver Alcohol Dehydrogenase ◽

Active Site Pocket ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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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 ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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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 ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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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 ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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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 ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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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 ◽

Horse Liver Alcohol Dehydrogenase ◽

Synthetic Model ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Zinc Site ◽

Model Peptides

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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 Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Catalytic Zinc ◽

Zinc Site

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