Subunit interaction in catalysis. Some experimental and theoretical approaches with glyceraldehyde-3-phosphate dehydrogenase.

Cardon, J W; Boyer, Paul D.

doi:10.1016/s0021-9258(18)34424-7

Cited by 20 publications

(2 citation statements)

References 53 publications

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“…On this basis, the nicotinamide ring itself would provide the site for proteinprotein recognition provided that the complex is between an A and a B dehydrogenase. A qualitatively similar mechanism was suggested by Cardón & Boyer (1982) to explain more rapid NADH production in the GPDH-catalyzed reaction of glyceraldehyde 3-phosphate with NAD"1" in the presence of LDH.…”

Section: Discussionsupporting

confidence: 64%

Direct transfer of reduced nicotinamide adenine dinucleotide from glyceraldehyde 3-phosphate dehydrogenase to liver alcohol dehydrogenase

Srivastava¹,

Bernhard²

1984

Biochemistry

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The reduction of benzaldehyde and p-nitrobenzaldehyde by NADH, catalyzed by horse liver alcohol dehydrogenase (LADH), has been found to be faster when NADH is bound to glyceraldehyde-3-phosphate dehydrogenase (GPDH) than with free NADH. The rate of reduction of aldehyde substrate with GPDH-NADH follows a Michaelian concentration dependence on GPDH-NADH. The reaction velocity is independent of GPDH concentration when [GPDH] greater than [NADH]total. The Km for GPDH-NADH is higher than that for free NADH. The reaction velocities in the presence of excess GPDH over NADH cannot be accounted for on the basis of the free NADH concentration arising from dissociation of the GPDH-NADH complex. These observations suggest that transfer of NADH from GPDH to LADH proceeds through the initial formation of a GPDH-NADH-LADH complex. Arguments for a direct enzyme-coenzyme-enzyme transfer mechanism are substantiated and quantitated both by steady-state kinetic studies and by determinations of all of the appropriate enzyme-coenzyme equilibrium dissociation constants. In contrast, over a similar concentration range, the complex lactate dehydrogenase (LDH)-NADH is not a substrate for the LADH-catalyzed reductions. Likewise, the LADH-NADH complex is not a substrate for the LDH-catalyzed reduction of pyruvate.

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Section: Discussionsupporting

confidence: 64%

Direct transfer of reduced nicotinamide adenine dinucleotide from glyceraldehyde 3-phosphate dehydrogenase to liver alcohol dehydrogenase

Srivastava¹,

Bernhard²

1984

Biochemistry

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“…The addition of substrate D-glyceraldehyde-3-phosphate inhibited the capture whereas a more bulky phosphate, L-tyrosine-O-phosphate, was ineffective. Since D-glyceraldehyde-3-phosphate binds near to the active site sulfhydryl group (27), it is interesting that the enough space for the substrate binding is still remains after the introduction of phenyl diazirine moiety. Although bulky ligands may have a conflict with the photoreactive group, the result also suggests that a small phosphate may be a candidate for a lead structure of the GAPDH inhibitor.…”

mentioning

confidence: 99%

A Novel Approach for Affinity-Based Screening of Target Specific Ligands: Application of Photoreactive d-Glyceraldehyde-3-phosphate Dehydrogenase

2003

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A novel application of the photoaffinity technique has been developed for the efficient discovery of small ligand and macromolecule interaction. The approach, photoaffinity capture, uses a photoreactive protein together with immobilized ligand for the rapid screening of competitive inhibitors. The set of photoreactive glyceraldehyde-3-phosphate dehydrogenase (photo-GAPDH) and immobilized dye ligand was prepared and examined as a model system. The photo-GAPDH was shown to efficiently capture the immobilized ligand. When nonimmobilized competitive ligands were included in the system, the capture was prevented in accordance with the affinity of the ligands. The present approach would provide an efficient tool for affinity-based screening of ligand libraries.

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pH-dependent conformational transformation in mung bean glyceraldehyde-3-phosphate dehydrogenase

Malhotra¹,

Srinivasan²

1985

Archives of Biochemistry and Biophysics

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Subunit interaction in catalysis. Some experimental and theoretical approaches with glyceraldehyde-3-phosphate dehydrogenase.

Cited by 20 publications

References 53 publications

Direct transfer of reduced nicotinamide adenine dinucleotide from glyceraldehyde 3-phosphate dehydrogenase to liver alcohol dehydrogenase

Direct transfer of reduced nicotinamide adenine dinucleotide from glyceraldehyde 3-phosphate dehydrogenase to liver alcohol dehydrogenase

A Novel Approach for Affinity-Based Screening of Target Specific Ligands: Application of Photoreactive d-Glyceraldehyde-3-phosphate Dehydrogenase

pH-dependent conformational transformation in mung bean glyceraldehyde-3-phosphate dehydrogenase

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