The investigation of substrate-induced changes in subunit interactions in glyceraldehyde 3-phosphate dehydrogenases by measurement of the kinetics and thermodynamics of subunit exchange

scientific article published on October 1, 1975

The investigation of substrate-induced changes in subunit interactions in glyceraldehyde 3-phosphate dehydrogenases by measurement of the kinetics and thermodynamics of subunit exchange is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1042/BJ1510037
P953full work available at URLhttps://europepmc.org/articles/PMC1172322
https://europepmc.org/articles/PMC1172322?pdf=render
https://portlandpress.com/biochemj/article-pdf/151/1/37/564985/bj1510037.pdf
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/174555/?tool=EBI
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/174555/pdf/?tool=EBI
P932PMC publication ID1172322
P698PubMed publication ID174555
P5875ResearchGate publication ID22960354

P2093author name stringH. H. Osborne
M. R. Hollaway
P2860cites workCo-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. I. Equilibrium and temperature-jump studies at pH 8-5 and 40 degrees CQ28239759
Activation of a covalent enzyme-substrate bond by noncovalent interaction with an effectorQ35108446
Rate-determining processes and the number of simultaneously active sties of D-glyceraldehyde 3-phosphate dehydrogenaseQ41761059
The hybridization of glyceraldehyde 3-phosphate dehydrogenases from rabbit muscle and yeast. Kinetics and thermodynamics of the reaction and isolation of the hybridQ41873191
Aspects of the chemistry of D-glyceraldehyde 3-phosphate dehydrogenaseQ42152246
Functional non-identity of subunits and isolation of active dimers of D-glyceraldehyde-3-phosphate dehydrogenaseQ44119202
Effect of D2O and nicotinamide adenine dinucleotide on the sedimentation properties and structure of glyceraldehyde phosphate dehydrogenaseQ44831169
Hybridization of glyceraldehyde-3-phosphate dehydrogenaseQ47841162
Binding of NAD + and NADH to rabbit-muscle glyceraldehydephosphate dehydrogenase.Q53771251
Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase.Q53913851
The binding of oxidized and reduced nicotinamide adenine-dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase.Q54123955
Half-of-the-sites and all-of-the-sites reactivity in rabbit muscle glyceraldehyde 3-phosphate dehydrogenase.Q54335404
Glyceraldehyde 3-Phosphate Dehydrogenase from Pig MuscleQ59056349
Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster MuscleQ59076368
Coenzyme-induced changes in the optical rotatory dispersion properties of glyceraldehyde 3-phosphate dehydrogenaseQ68553044
Reversible inactivation of dehydrogenasesQ68560672
Negative cooperativity in enzyme action. The binding of diphosphopyridine nucleotide to glyceraldehyde 3-phosphate dehydrogenaseQ68586060
Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. II. Stopped-flow studies at pH 8-5 and 40 degrees CQ68626180
The binding of NAD+ to rabbit muscle glyceraldehyde-3-phosphate dehydrogenase studied by protein fluorescence quenchingQ68626327
Structure-function studies on glyceraldehyde 3-phosphate dehydrogenase. IV. Subunit interactions of the rabbit muscle and yeast enzymesQ68638480
Study of the position of NAD and its effect on the conformation of D-glyceraldehyde-3-phosphate dehydrogenase by small-angle x-ray scatteringQ68650322
Adenine nucleotide-mediated subunit exchange between isoenzymes of glyceraldehyde-3-phosphate dehydrogenaseQ68672490
Structure-function relationship in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Trinitrophenylation of the lysine residuesQ68695919
Three-dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenaseQ68708412
Half-of-the-sites reactivity and negative co-operativity: The case of yeast glyceraldehyde 3-phosphate dehydrogenaseQ69333311
Hybrid Molecules of Yeast and Rabbit GPD containing Native and Modified SubunitsQ71502868
Thermodynamics of nicotinamide-adenine dinucleotide addition to the glyceraldehyde 3-phosphate dehydrogenases of yeast and of rabbit skeletal muscle. An equilibrium and calorimetric analysis over a range of temperaturesQ71759956
On the mechanism of the dissociation of haemoglobinQ72241605
The coenzyme content of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenaseQ74214919
AMINO ACID SEQUENCES AROUND THE REACTIVE CYSTEINE RESIDUES IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASESQ76568884
Glyceraldehyde 3-phosphate dehydrogenase: Amino acid sequence of enzyme from baker's yeastQ77919701
Inactivation of muscle triosephosphate dehydrogenase by reduced diphosphopyridine nucleotide at physiological concentrationsQ79431818
P433issue1
P407language of work or nameEnglishQ1860
P921main subjectbiochemistryQ7094
cell biologyQ7141
P1104number of pages9
P304page(s)37-45
P577publication date1975-10-01
P1433published inBiochemical JournalQ864221
P1476titleThe investigation of substrate-induced changes in subunit interactions in glyceraldehyde 3-phosphate dehydrogenases by measurement of the kinetics and thermodynamics of subunit exchange
P478volume151

Reverse relations

cites work (P2860)
Q40013505An investigation of the nicotinamide-adenine dinucleotide-induced ‘tightening’ of the structure of glyceraldehyde 3-phosphate dehydrogenase
Q41665016Effect of association-dissociation on the catalytic properties of glyceraldehyde 3-phosphate dehydrogenase
Q47409048Interaction of enzymes involved in triosephosphate metabolism. Comparison of yeast and rabbit muscle cytoplasmic systems
Q42268023Kinetic behaviour and oligomeric state of 3-phosphoglyceroyl-D-glyceraldehyde-3-phosphate dehydrogenase
Q40123136Mechanism of Reactivation and Refolding of Glyceraldehyde-3-Phosphate Dehydrogenase from Yeast after Denaturation and Dissociation
Q39657569Recombinant human sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDHS) is expressed at high yield as an active homotetramer in baculovirus-infected insect cells
Q40857509Role of Lysine-183 in d-Glyceraldehyde-3-Phosphate Dehydrogenases. Properties of the N-Acetylated Yeast, Sturgeon Muscle and Rabbit Muscle Enzymes
Q48633570Sevoflurane modulates the activity of glyceraldehyde 3-phosphate dehydrogenase
Q27656083Structure of Insoluble Rat Sperm Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) via Heterotetramer Formation with Escherichia coli GAPDH Reveals Target for Contraceptive Design
Q28330810Synthesis and use of bifunctional chloromethylalkanedione derivatives of variable chain length for cross-linking thiol groups in oligomeric proteins. Specific cross-linking in glyceraldehyde 3-phosphate dehydrogenase
Q40264682The development of SS′-polymethylenebis(methanethiosulphonates) as reversible cross-linking reagents for thiol groups and their use to form stable catalytically active cross-linked dimers within glyceraldehyde 3-phosphate dehydrogenase
Q39984485The effect of substrates on the association equilibrium of mammalian D-glyceraldehyde 3-phosphate dehydrogenase
Q28326455The reaction of rabbit muscle creatine kinase with some derivatives of iodoacetamide
Q70473244[Comparative study on the chemical modification of sulfhydryl groups of glyceraldehyde-3-phosphate dehydrogenases from yeast and rabbit muscle. The relationship between structure and chemical reactivity]

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