Basis for Half-of-the-Site Reactivity and the Dominance of the K487 Oriental Subunit over the E487 Subunit in Heterotetrameric Human Liver Mitochondrial Aldehyde Dehydrogenase†

Jianzhong Zhou; Henry Weiner

doi:10.1021/bi001221k

Basis for Half-of-the-Site Reactivity and the Dominance of the K487 Oriental Subunit over the E487 Subunit in Heterotetrameric Human Liver Mitochondrial Aldehyde Dehydrogenase†

Biochemistry ◽

10.1021/bi001221k ◽

2000 ◽

Vol 39 (39) ◽

pp. 12019-12024 ◽

Cited By ~ 27

Author(s):

Jianzhong Zhou ◽

Henry Weiner

Keyword(s):

Aldehyde Dehydrogenase ◽

Human Liver

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Human Liver High Km Aldehyde Dehydrogenase (ALDH4): Properties and Structural Relationship to the Glutamic γ-Semialdehyde Dehydrogenase

Advances in Experimental Medicine and Biology - Enzymology and Molecular Biology of Carbonyl Metabolism 4 ◽

10.1007/978-1-4615-2904-0_21 ◽

1993 ◽

pp. 191-197 ◽

Cited By ~ 1

Author(s):

Dharam P. Agarwal ◽

Rolf Eckey ◽

John Hempel ◽

H. Werner Goedde

Keyword(s):

Aldehyde Dehydrogenase ◽

Human Liver ◽

Structural Relationship ◽

Semialdehyde Dehydrogenase

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Chemical modifications to study mutations that affect the ability of the general base (E268) to function in human liver mitochondrial aldehyde dehydrogenase

Chemico-Biological Interactions ◽

10.1016/s0009-2797(02)00177-1 ◽

2003 ◽

Vol 143-144 ◽

pp. 85-91 ◽

Cited By ~ 4

Author(s):

Baoxian Wei ◽

Dennis C Mays ◽

James J Lipsky ◽

Henry Weiner

Keyword(s):

Aldehyde Dehydrogenase ◽

Human Liver ◽

Chemical Modifications ◽

General Base

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Human liver mitochondrial aldehyde dehydrogenase: a C-terminal segment positions and defines the structure corresponding to the one reported to differ in the Oriental enzyme variant

FEBS Letters ◽

10.1016/0014-5793(84)80807-8 ◽

1984 ◽

Vol 173 (2) ◽

pp. 367-373 ◽

Cited By ~ 45

Author(s):

John Hempel ◽

Rudolf Kaiser ◽

Hans Jörnvall

Keyword(s):

Aldehyde Dehydrogenase ◽

Human Liver ◽

Terminal Segment ◽

The One ◽

Enzyme Variant

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Effect of cholesta-3,5-dien-7-one on human liver aldehyde dehydrogenase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(91)90126-k ◽

1991 ◽

Vol 1079 (2) ◽

pp. 203-208 ◽

Cited By ~ 9

Author(s):

Maria T. Ryzlak ◽

Wojciech Ambroziak ◽

Carl P. Schaffner

Keyword(s):

Aldehyde Dehydrogenase ◽

Human Liver ◽

Liver Aldehyde Dehydrogenase

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The activation of aldehyde dehydrogenase by diethylstilboestrol and 2,2′-dithiodipyridine

Biochemical Journal ◽

10.1042/bj2070081 ◽

1982 ◽

Vol 207 (1) ◽

pp. 81-89 ◽

Cited By ~ 13

Author(s):

T M Kitson

Keyword(s):

Enzyme Activity ◽

Aldehyde Dehydrogenase ◽

Human Liver ◽

Common Property ◽

Rabbit Liver ◽

Aldehyde Dehydrogenases ◽

Cytoplasmic Enzyme ◽

Sheep Liver ◽

Low Concentrations ◽

Liver Aldehyde Dehydrogenase

1. The activation of sheep liver cytoplasmic aldehyde dehydrogenase by diethylstilboestrol and by 2,2′-dithiodipyridine is described. The effects of the two modifiers are very similar with respect to variation with acetaldehyde concentration, pH and temperature. Thus the degree of activation is maximal when the enzyme is assayed at approx. 1 mM-acetaldehyde, is greater at 25 degrees C than at 37 degrees C, and is greater at pH 7.4 than at pH 9.75. With low concentrations of acetaldehyde both modifiers decrease the enzyme activity. 2. Diethylstilboestrol affects the sheep liver cytoplasmic enzyme in a very similar way to that previously described for a rabbit liver cytoplasmic enzyme. Preliminary experiments show that the same is true for a preparation of human liver aldehyde dehydrogenase. It is proposed that sensitivity to diethylstilboestrol (and steroids) is a common property of all mammalian cytoplasmic aldehyde dehydrogenases.

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Aldehyde dehydrogenase content and composition of human liver

Alcohol ◽

10.1016/0741-8329(85)90098-9 ◽

1985 ◽

Vol 2 (3) ◽

pp. 375-381 ◽

Cited By ~ 17

Author(s):

Claire M. Forte-McRobbie ◽

Regina Pietruszko

Keyword(s):

Aldehyde Dehydrogenase ◽

Human Liver

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Purification of Human Liver Aldehyde Dehydrogenase by High-Performance Liquid Chromatography and Identification of Isoenzymes by Immunoblotting

Alcoholism Clinical and Experimental Research ◽

10.1111/j.1530-0277.1987.tb01264.x ◽

1987 ◽

Vol 11 (1) ◽

pp. 60-65 ◽

Cited By ~ 9

Author(s):

Charles T Johnson ◽

William F Bosron ◽

Colleen A Harden ◽

Ting-Kai Li

Keyword(s):

High Performance Liquid Chromatography ◽

Liquid Chromatography ◽

Aldehyde Dehydrogenase ◽

Human Liver ◽

High Performance ◽

Liver Aldehyde Dehydrogenase

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Subcellular distribution of aldehyde dehydrogenase activities in human liver

Alcohol ◽

10.1016/0741-8329(85)90025-4 ◽

1985 ◽

Vol 2 (1) ◽

pp. 107-110 ◽

Cited By ~ 22

Author(s):

Gary T.M. Henehan ◽

Kevin Ward ◽

Nicholas P. Kennedy ◽

Donald G. Weir ◽

Keith F. Tipton

Keyword(s):

Aldehyde Dehydrogenase ◽

Subcellular Distribution ◽

Human Liver

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Spatial distribution of human liver aldehyde dehydrogenase isoenzymes

Histochemistry and Cell Biology ◽

10.1007/s004180050382 ◽

1999 ◽

Vol 111 (6) ◽

pp. 461-466 ◽

Cited By ~ 2

Author(s):

I. Piotr Maly ◽

Valérie Crotet ◽

D. Sasse

Keyword(s):

Spatial Distribution ◽

Aldehyde Dehydrogenase ◽

Human Liver ◽

Liver Aldehyde Dehydrogenase

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HUMAN LIVER ALDEHYDE DEHYDROGENASE

Alcohol and Aldehyde Metabolizing Systems ◽

10.1016/b978-0-12-691402-3.50025-1 ◽

1977 ◽

pp. 195-202 ◽

Cited By ~ 2

Author(s):

R. Pietruszko ◽

N.J. Greenfield ◽

C.R. Edson

Keyword(s):

Aldehyde Dehydrogenase ◽

Human Liver ◽

Liver Aldehyde Dehydrogenase

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