WordNet

any of several complex proteins that are produced by cells and act as catalysts in specific biochemical reactions

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酵素

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1. グリコーゲン分枝酵素欠損症（糖原病IV型、アンダーセン病） glycogen branching enzyme deficiency glycogen storage disease iv andersen disease
2. 急性心筋梗塞におけるアンギオテンシン変換酵素阻害剤：作用機序 angiotensin converting enzyme inhibitors in acute myocardial infarction mechanisms of action
3. 心臓におけるアンギオテンシンⅡの作用 actions of angiotensin ii on the heart
4. 副腎酵素阻害剤および抗アドレナリン薬の薬理および毒性 pharmacology and toxicity of adrenal enzyme inhibitors and adrenolytic agents
5. 心不全におけるアンギオテンシン変換酵素阻害剤およびアンギオテンシン受容体拮抗剤：作用機序 angiotensin converting enzyme inhibitors and receptor blockers in heart failure mechanisms of action

English Journal

dNTP-dependent Conformational Transitions in the Fingers Subdomain of Klentaq1 DNA Polymerase: INSIGHTS INTO THE ROLE OF THE "NUCLEOTIDE-BINDING" STATE.

Rothwell PJ, Allen WJ, Sisamakis E, Kalinin S, Felekyan S, Widengren J, Waksman G, Seidel CA.SourceFrom the Chair for Molecular Physical Chemistry, Heinrich-Heine University, Universitätsstraβe 1, 40225 Düsseldorf, Germany.
The Journal of biological chemistry.J Biol Chem.2013 May 10;288(19):13575-91. doi: 10.1074/jbc.M112.432690. Epub 2013 Mar 22.
DNA polymerases are responsible for the accurate replication of DNA. Kinetic, single-molecule, and x-ray studies show that multiple conformational states are important for DNA polymerase fidelity. Using high precision FRET measurements, we show that Klentaq1 (the Klenow fragment of Thermus aquaticus
PMID 23525110

Electronic Measurements of Single-Molecule Processing by DNA Polymerase I (Klenow Fragment).

Olsen TJ, Choi Y, Sims PC, Gul OT, Corso BL, Dong C, Brown WA, Collins PG, Weiss GA.AbstractBioconjugating single molecules of the Klenow fragment of DNA polymerase I into electronic nanocircuits allowed electrical recordings of enzymatic function and dynamic variability with the resolution of individual nucleotide incorporation events. Continuous recordings of DNA polymerase processing multiple homopolymeric DNA templates extended over 600 s and through >10,000 bond forming events. An enzymatic processivity of 42 nucleotides for a template of the same length was directly observed. Statistical analysis determined key kinetic parameters for the enzyme's open and closed conformations. Consistent with these nanocircuit-based observations, the enzyme closed complex forms a phosphodiester bond in a highly efficient process >99.8% of the time with a mean duration of only 0.3 ms for all four dNTPs. The rate-limiting step for catalysis occurs during the enzyme open state, but with a nearly two-fold longer duration for dATP or dTTP incorporation than for dCTP or dGTP into complementary, homopolymeric DNA templates. Taken together, the results provide a wealth of new information complementing prior work on the mechanism and dynamics of DNA polymerase I.
Journal of the American Chemical Society.J Am Chem Soc.2013 Apr 30. [Epub ahead of print]
Bioconjugating single molecules of the Klenow fragment of DNA polymerase I into electronic nanocircuits allowed electrical recordings of enzymatic function and dynamic variability with the resolution of individual nucleotide incorporation events. Continuous recordings of DNA polymerase processing mu
PMID 23631761

Measuring and Modeling the Kinetics of Individual DNA-DNA Polymerase Complexes on a Nanopore.

Wang H, Hurt N, Dunbar WB.SourceDepartment of Applied Mathematics and Statistics, ‡Department of Chemistry and Biochemistry, and §Department of Computer Engineering, University of California , Santa Cruz, California 95064, United States.
ACS nano.ACS Nano.2013 Apr 16. [Epub ahead of print]
The assembly of a DNA-DNA polymerase binary complex is the precursory step in genome replication, in which the enzyme binds to the 3' junction created when a primer binds to its complementary substrate. In this study, we use an active control method for observing the binding interaction between Klen
PMID 23565679