Single-molecule kinetics reveals signatures of half-sites reactivity in dihydroorotate dehydrogenase A catalysis - Test2 - elhamkhani - TriplyDB

Single-molecule kinetics reveals signatures of half-sites reactivity in dihydroorotate dehydrogenase A catalysis

Single-molecule kinetics reveals signatures of half-sites reactivity in dihydroorotate dehydrogenase A catalysis

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Shedding light on protein folding, structural and functional dynamics by single molecule studies Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase Single-molecule analysis reveals three phases of DNA degradation by an exonuclease.Probing biomolecular structures and dynamics of single molecules using in-gel alternating-laser excitation.The enzyme mechanism of nitrite reductase studied at single-molecule level Rate theories for biologists 1,4-naphthoquinones and other NADPH-dependent glutathione reductase-catalyzed redox cyclers as antimalarial agents Determination of the oligomer size of amyloidogenic protein beta-amyloid(1-40) by single-molecule spectroscopy Single-enzyme kinetics with fluorogenic substrates: lessons learnt and future directions.Single-Molecule Fluorescence Using Nucleotide Analogs: A Proof-of-Principle.Metallic-Nanostructure-Enhanced Fluorescence of Single Flavin Cofactor and Single Flavoenzyme Molecules.

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Single-molecule kinetics reveals signatures of half-sites reactivity in dihydroorotate dehydrogenase A catalysis

http://www.wikidata.org/entity/Q34595992

description

2006 nî lūn-bûn

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2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2006年の論文

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2006年論文

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Single-molecule kinetics revea ...... tate dehydrogenase A catalysis

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Proceedings of the National Academy of Sciences of the United States of America

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Single-molecule kinetics revea ...... tate dehydrogenase A catalysis

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Ari Gafni

http://www.w3.org/2001/XMLSchema#string

Duncan Steel

http://www.w3.org/2001/XMLSchema#string

Joe Dertouzos

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Jue Shi

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P2860

The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function

Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function

The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis

In vitro and in vivo dimerization of human endonuclease III stimulates its activity

Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase

Single-molecule enzymatic dynamics

Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model.

Proteomics and models for enzyme cooperativity.

Cooperativity in enzyme function: equilibrium and kinetic aspects.

Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis.

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