Proton-translocating nicotinamide nucleotide transhydrogenase of Escherichia coli. Involvement of aspartate 213 in the membrane-intercalating domain of the beta subunit in energy transduction (Q46968831)

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scientific article published in July 1995

Language	Label	Description	Also known as
English	Proton-translocating nicotinamide nucleotide transhydrogenase of Escherichia coli. Involvement of aspartate 213 in the membrane-intercalating domain of the beta subunit in energy transduction	scientific article published in July 1995

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scholarly article

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

Proton-translocating nicotinamide nucleotide transhydrogenase of Escherichia coli. Involvement of aspartate 213 in the membrane-intercalating domain of the beta subunit in energy transduction (English)

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

1 reference

based on heuristic

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Escherichia coli

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based on heuristic

inferred from title

author name string

Yamaguchi M

1

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

Hatefi Y

2

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Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

language of work or name

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publication date

1 July 1995

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Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

Journal of Biological Chemistry

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Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

270

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Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

16653-16659

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Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

28

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change.

1 reference

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Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli.

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New method for generating deletions and gene replacements in Escherichia coli

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Prediction and site-specific mutagenesis of residues in transmembrane alpha-helices of proton-pumping nicotinamide nucleotide transhydrogenases from Escherichia coli and bovine heart mitochondria.

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Protein-ligand binding studies with a table-top, air-driven high-speed centrifuge

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21 January 2018

Kinetic resolution of the reaction catalysed by proton-translocating transhydrogenase from Escherichia coli as revealed by experiments with analogues of the nucleotide substrates.

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Utilization of binding energy and coupling rules for active transport and other coupled vectorial processes.

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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A simplification of the protein assay method of Lowry et al. which is more generally applicable

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Cloning and sequencing of the genes for the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and the implications for the domain structure of the enzyme

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Mitochondrial nicotinamide nucleotide transhydrogenase: NADPH binding increases and NADP binding decreases the acidity and susceptibility to modification of cysteine-893.

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Energy-transducing nicotinamide nucleotide transhydrogenase: nucleotide sequences of the genes and predicted amino acid sequences of the subunits of the enzyme from Rhodospirillum rubrum

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Mitochondrial energy-linked nicotinamide nucleotide transhydrogenase: effect of substrates on the sensitivity of the enzyme to trypsin and identification of tryptic cleavage sites

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Primary structure of an Entamoeba histolytica nicotinamide nucleotide transhydrogenase

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Crosslinking and radiation inactivation analysis of the subunit structure of the pyridine nucleotide transhydrogenase of Escherichia coli

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Energy-linked nicotinamide nucleotide transhydrogenase 1963-1988: a commentary on 'Equilibrium Studies of the Energy-Dependent and Non-Energy-Dependent Pyridine Nucleotide Transhydrogenase Reactions'.

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Effects of N,N'-dicyclohexylcarbodiimide and N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline on hydride ion transfer and proton translocation activities of mitochondrial nicotinamidenucleotide transhydrogenase

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Mitochondrial nicotinamide nucleotide transhydrogenase: active site modification by 5'-[p-(fluorosulfonyl)benzoyl]adenosine

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Eimeria refractile body proteins contain two potentially functional characteristics: transhydrogenase and carbohydrate transport

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Identifiers

10.1074/JBC.270.28.16653

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

1 reference

Europe PubMed Central

27 December 2017

http://europepmc.org/abstract/MED/7622474

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