Differences in the binding of coenzyme to L-3-hydroxyacyl-coenzyme A dehydrogenase in the crystalline state and in solution (original) (raw)

L-3-hydroxyacyl coenzyme A dehydrogenase. The location of NAD binding sites and the bilobal subunit structure

Leonard Banaszak

Journal of Biological Chemistry, 1983

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l-3-Hydroxyacyl coenzyme A dehydrogenase: Crystallographic properties of the pig heart enzyme

Leonard Banaszak

Journal of Molecular Biology, 1974

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Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution

Jens Birktoft

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Pig heart short chain L-3-hydroxyacyl-CoA dehydrogenase revisited: Sequence analysis and crystal structure determination

Leonard Banaszak

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European journal of biochemistry / FEBS, 1972

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Binding of Coenzyme and Substrate and Coenzyme Analogues to 6-Phosphogluconate Dehydrogenase from Sheep Liver. An X-Ray Study at 0.6-nm Resolution

margaret adams

European Journal of Biochemistry, 1979

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Mitochondrial malate dehydrogenase. Crystallographic properties of the pig heart enzyme

Leonard Banaszak

Journal of Molecular Biology, 1978

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Sequestration of the active site by interdomain shifting: crystallographic and spectroscopic evidence for distinct conformations of L-3-Hydroxyacyl-CoA dehydrogenase

Leonard Banaszak

Journal of Biological Chemistry, 2000

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The Crystal Structure of Complexes between Horse Liver Alcohol Dehydrogenase and the Coenzyme Analogues 3-Iodopyridine-adenine Dinucleotide and Pyridine-adenine Dinucleotide

Jean Francois Biellmann

European Journal of Biochemistry, 1977

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Evidence for Ligand-Induced Conformational Changes in Rabbit-Muscle Glyceraldehyde-3-Phosphate Dehydrogenase

Yoav Henis

European journal of biochemistry, 1979

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A structural study of pig liver glyceraldehyde-3-phosphate dehydrogenase

Lorenzo Minchiotti

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1976

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Microenvironment of the enzyme-bound NADH is different in lobster and pig muscle glyceraldehyde-3-phosphate dehydrogenase microcrystals

Mária Vas

Archives of Biochemistry and Biophysics, 1986

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Protein isomerization in the NAD+-dependent activation of beta-(2-furyl)acryloyl-glyceraldehyde-3-phosphate dehydrogenase in the crystal

Mária Vas

Journal of Biological Chemistry, 1982

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Evidence for binding of NAD dimers to NAD-dependent dehydrogenases

Antonio Casini

Biochimica et Biophysica Acta (BBA) - Enzymology, 1981

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Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 A resolution

Tuomo Glumoff

Structure (London, England : 1993), 2003

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Structure-function correlation of fatty acyl-CoA dehydrogenase and fatty acyl-CoA oxidase

Camilo Rojas

Biochemistry, 1985

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The presence of a histidine-aspartic acid pair in the active site of 2-hydroxyacid dehydrogenases. X-ray refinement of cytoplasmic malate dehydrogenase

Leonard Banaszak

Journal of Biological Chemistry, 1983

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The nature of enzyme-substrate complexes in acyl-coenzyme a dehydrogenases

Colin Thorpe

Archives of Biochemistry and Biophysics, 1988

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Effect of the side chain structure of coenzyme Q on the steady state kinetics of bovine heart NADH: coenzyme Q oxidoreductase

Yoshikawa Shinya

Journal of bioenergetics and biomembranes, 2003

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Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-.ANG. resolution

Leonard Banaszak

Biochemistry, 1989

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Structure/activity relationship of adenine-modified NAD derivatives with respect to porcine heart lactate dehydrogenase isozyme H4 simulated with molecular mechanics

Dietmar Schomburg

European Journal of Biochemistry, 1993

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Dye-affinity labelling of bovine heart mitochondrial malate dehydrogenase and study of the NADH-binding site

Nikolaos Labrou

The Biochemical journal, 1996

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The nature of enzyme-substrate complexes in acyl-coenzyme a dehydrogenases*1

Colin Thorpe

Archives of Biochemistry and Biophysics, 1988

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Structure of Human Isovaleryl-CoA Dehydrogenase at 2.6 Å Resolution: Structural Basis for Substrate Specificity,

Al-Walid Mohsen

Biochemistry, 1997

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Functional non-identity of subunits and isolation of active dimers of D-glyceraldehyde-3-phosphate dehydrogenase

Judit Ovádi

European journal of biochemistry / FEBS, 1971

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Energy-linked transhydrogenase. Characterization of a nucleotide-binding sequence in nicotinamide nucleotide transhydrogenase from beef heart

Jan A. Berden

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1992

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Kinetic studies of crystalline enzymes by single crystal microspectrophotometry. Analysis of a single catalytic turnover in a D-glyceraldehyde-3-phosphate dehydrogenase crystal

Mária Vas

Journal of Biological Chemistry, 1979

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Catalytic mechanism and interactions of NAD+ with glyceraldehyde-3-phosphate dehydrogenase: correlation of EPR data and enzymatic studies

Jens Birktoft

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989

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Raman spectroscopic studies of NAD coenzymes bound to malate dehydrogenases by difference techniques

John Burgner

Biochemistry, 1991

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Study of Coenzyme Binding Site of Octopine Dehydrogenase Using Analogues of NAD+

Jean Francois Biellmann

European Journal of Biochemistry, 1975

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An Investigation of the Active Site of Lactate Dehydrogenase with NAD+ Analogues

Jean Francois Biellmann

European Journal of Biochemistry, 1981

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The Crystal and Solution Structures of Glyceraldehyde-3-phosphate Dehydrogenase Reveal Different Quaternary Structures

Ana Damas

Journal of Biological Chemistry, 2006

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