nu·cle·o·tid·yl·trans·fer·as·es

(nū'klē-ō-tī'dĭl-trans'fĕr-ās'ĕz),

Enzymes that catalyze the transfer of transferring nucleotide residues (nucleotidyls) from nucleoside di- or triphosphates into dimer or polymer forms. Some nucleotidyltransferases bear specific names (for example, adenylyltransferases), trivial names indicating the linkage hydrolyzed in the synthesis (pyrophosphorylases, phosphorylases), or names indicating the material that is synthesized (for example, RNA or DNA polymerase).

Farlex Partner Medical Dictionary © Farlex 2012

DNA polymerase

Any of various enzymes that function in the replication and repair of DNA by catalyzing the linking of dATP, dCTP, dGTP, and dTTP in a specific order, using single-stranded DNA as a template.

DNA polymerase

a group of enzymes that are responsible for the polymerization of free NUCLEOTIDES on to the unwound DNA molecule during DNA REPLICATION. The first DNA polymerase was discovered by A. Kornberg in 1957 (for which work he received the Nobel Prize). There are several polymerases in any organism. For example, in E. coli, DNA polymerase III synthesizes both the leading and the lagging strands (see DNA, REPLICATION); DNA polymerase I fills in the gaps between Okazaki fragments. In EUKARYOTES, three DNA polymerases are involved in chromosome replication: polymerase α, δ and ɛ; mitochondrial DNA synthesis involves polymerase γ. Most DNA polymerases also have an EDITING function.

Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005

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References in periodicals archive

For the second question (use of proofreading enzymes), 18 laboratories replied that they did not use a DNA polymerase with 3'-5' exonuclease activity; 11 of these had reported homozygous results, 6 had reported heterozygous results, and 1 did not report a numeric result (only normal).

The Power of Proficiency Testing: Unraveling Single-Nucleotide Polymorphism Interference, With Potential Impact on Clinical Testing of Spinocerebellar Ataxia Type 3

Bakuchiol (1), belonging to meroterpene class of natural product, has been reported as the strongest DNA polymerase [alpha] inhibitor, found in P.

Inhibitory Mechanism Exhibited by Phenol-based Natural Products against DNA Polymerase [alpha] from Psoralea corylifolia by Molecular Docking

Structures of mismatch replication errors observed in a DNA polymerase. Cell 2004; 116:803-16.

The Effect of Single Mismatches on Primer Extension

Taq DNA polymerase is isolated from the thermophilic bacteria, Thermophilus aquaticus, and has a stable natural structure.

Development of Plant Expression Vector with Taq DNA Polymerase Gene to Yield Heat-tolerant Maize Lines

Caption: Figure 3: Effect of different concentrations of Taq DNA polymerase on the performance of thermostabilized multiplex PCR.

A Thermostabilized, One-Step PCR Assay for Simultaneous Detection of Klebsiella pneumoniae and Haemophilus influenzae

HBV DNA polymerase mutations and genotypes were measured using the INNO-LiPA assay kit (Shenzhen, China).

Prevalence of mutations in HBV DNA polymerase gene associated with nucleos(t)ide resistance in treatment-naive patients with Chronic Hepatitis B in Central China

As an enzyme for PCR, we used the following types of DNA-dependent DNA polymerases: Taq DNA polymerase, Tersus DNA polymerase, Deep Vent DNA polymerase and Phusion DNA polymerase.

Systematic comparison of the capability of modified nucleoside triphosphates to act as a substrate for thermostable DNA polymerases during PCR

For method validation purposes, we used Taq DNA polymerase, a Family A DNA polymerase and the enzyme used in the earliest PCR experiments [6].

Error rate comparison during polymerase chain reaction by DNA polymerase

The concentrations used for each DNA polymerase are specified in the respective figure legends.

Effects of stability of base pairs containing an oxazolone on DNA elongation

However, researchers have been trying to produce such enzyme from various versions of Taq DNA polymerase gene via genetic engineering.

ISOLATION, CHARACTERIZATION OF NOVEL FRAGMENT OF A GENE KLENTAQ WHICH ENCODES THERMUS AQUATICUS DNA POLYMERASE AND ITS THERMOSTABILITY STUDIES IN ESCHERICHIA COLI