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Polymerase: Human Pol alpha

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Polymerase	Reference	Property	Result	Context
Human Pol alpha	Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases.	3-5' Exonuclease (proofreading)	No
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	Incorporation of non-standard nucleotides	< 10%	Nucleotide analog: Acycloriboucleoside-5'-O-(1-Thiotriphosphate)
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	Incorporation of non-standard nucleotides	Unspecified	Nucleotide analog: 2',3'-Dideoxyribonucleotide nucleoside triphosphate
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	Cloned or native	Native organism
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	Tagged	Unspecified
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	Full length or truncated	Unspecified
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	K_M	1.5uM	Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Steady State (Activated DNA)
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	K_M	1.8uM	Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (activated DNA)
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	K_M	110uM	Reaction: Nucleotide incorporation; Substrate: TTP analog; Technique: Steady State (Running start primer template)
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	K_M	1.4uM	Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Steady State (Running start primer template)
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	K_M	2.1uM	Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Running start primer template)
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	V_max	2 /second	Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Steady State (Running start primer template)
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	V_max	0.06 /second	Reaction: Nucleotide incorporation; Substrate: TTP analog; Technique: Steady State (Running start primer template)
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	V_max	1.7 /second	Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Running start primer template)
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	Application name	PCR
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	K_d	120uM	Reaction: Nucleotide incorporation; Substrate: ddCTP; Technique: Steady State (Activated DNA)
Human Pol alpha	Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA.	K_d	650uM	Reaction: Nucleotide incorporation; Substrate: TTP analog; Technique: Steady State (Activated DNA)
Human Pol alpha	Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation.	K_M	0.2uM	Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Steady State
Human Pol alpha	Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation.	K_M	89uM	Reaction: Nucleotide incorporation; Substrate: ATP analog; Technique: Steady State
Human Pol alpha	Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation.	V_max	1.1 /minute	Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Steady State
Human Pol alpha	Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation.	V_max	1.7 /minute	Reaction: Nucleotide incorporation; Substrate: ATP analog; Technique: Steady State
Human Pol alpha	Biochemical and functional comparison of DNA polymerases alpha, delta, and epsilon from calf thymus.	3-5' Exonuclease (proofreading)	No
Human Pol alpha	Biochemical and functional comparison of DNA polymerases alpha, delta, and epsilon from calf thymus.	5-3' Exonuclease	No
Human Pol alpha	Biochemical and functional comparison of DNA polymerases alpha, delta, and epsilon from calf thymus.	RNase H	No
Human Pol alpha	Biochemical and functional comparison of DNA polymerases alpha, delta, and epsilon from calf thymus.	Processivity	450bp
Human Pol alpha	Biochemical and functional comparison of DNA polymerases alpha, delta, and epsilon from calf thymus.	Specific Activity	490 units/mg	Technique: Polymerase Assay (M13 DNA)
Human Pol alpha	Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells.	Full length or truncated	Full length
Human Pol alpha	Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells.	Processivity	11bp
Human Pol alpha	Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells.	K_M	44uM	Reaction: Polymerase-DNA interaction; Substrate: DNA template
Human Pol alpha	Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells.	K_M	39uM	Reaction: Polymerase-DNA interaction; Substrate: DNA template
Human Pol alpha	Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells.	K_M	4uM	Reaction: Nucleotide incorporation; Substrate: dTTP
Human Pol alpha	Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells.	K_M	2.3uM	Reaction: Nucleotide incorporation; Substrate: dCTP
Human Pol alpha	Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells.	K_M	1.2uM	Reaction: Nucleotide incorporation; Substrate: dGTP
Human Pol alpha	Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells.	K_M	3uM	Reaction: Nucleotide incorporation; Substrate: dATP
Human Pol alpha	Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells.	Nick Extension	No
Human Pol alpha	Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells.	Gap Filling	Yes
Human Pol alpha	Thermostable DNA polymerases.	3-5' Exonuclease (proofreading)	No
Human Pol alpha	Thermostable DNA polymerases.	5-3' Exonuclease	No
Human Pol alpha	Thermostable DNA polymerases.	Full length or truncated	Full length
Human Pol alpha	DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.	K_M	3.7uM	Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Gel shift
Human Pol alpha	DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.	K_M	4200uM	Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Gel shift
Human Pol alpha	DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.	K_M	1E+04uM	Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Gel shift
Human Pol alpha	DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.	K_M	1E+04uM	Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Gel shift
Human Pol alpha	DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.	K_M	35uM	Reaction: Nucleotide incorporation; Substrate: ATP analog; Technique: Gel shift
Human Pol alpha	DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.	V_max	12.9 /minute	Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Gel shift
Human Pol alpha	DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.	V_max	3.1 /minute	Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Gel shift
Human Pol alpha	DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.	V_max	1.7 /minute	Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Gel shift
Human Pol alpha	DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.	V_max	1.7 /minute	Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Gel shift
Human Pol alpha	DNA polymerase insertion fidelity. Gel assay for site-specific kinetics.	V_max	13 /minute	Reaction: Nucleotide incorporation; Substrate: ATP analog; Technique: Gel shift
Human Pol alpha	Evidence for interplay among yeast replicative DNA polymerases alpha, delta and epsilon from studies of exonuclease and polymerase active site mutations.	3-5' Exonuclease (proofreading)	No
Human Pol alpha	Evidence for interplay among yeast replicative DNA polymerases alpha, delta and epsilon from studies of exonuclease and polymerase active site mutations.	5-3' Exonuclease	No
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	3-5' Exonuclease (proofreading)	No
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	Cloned or native	Cloned in E. coli
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	Frameshift Error Rate	0.00031 errors/bp	Technique: Reversion
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	Frameshift Error Rate	4E-05 errors/bp	Technique: Forward mutational
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	Overall Error Rate	0.003 errors/bp	Technique: M13mp2 forward mutation assay
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	Overall Error Rate	5E-05 errors/bp	Technique: Forward mutational
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	Nucleotide Substitution Rate	1.3E-06 errors/bp	Technique: Reversion
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	Nucleotide Substitution Rate	1.1E-05 errors/bp	Technique: Forward mutational
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	Full length or truncated	Full length
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	Specific Activity	4.5E+06 units/mg
Human Pol alpha	Fidelity and error specificity of the alpha catalytic subunit of Escherichia coli DNA polymerase III.	Gap Filling	Yes
Human Pol alpha	Fidelity of DNA synthesis catalyzed by human DNA polymerase alpha and HIV-1 reverse transcriptase: effect of reaction pH.	Cloned or native	Insect cells
Human Pol alpha	Fidelity of DNA synthesis catalyzed by human DNA polymerase alpha and HIV-1 reverse transcriptase: effect of reaction pH.	Nucleotide Substitution Rate	2.38E-05 errors/bp	Technique: Reversion (pH 6.1)
Human Pol alpha	Fidelity of DNA synthesis catalyzed by human DNA polymerase alpha and HIV-1 reverse transcriptase: effect of reaction pH.	Nucleotide Substitution Rate	0.000154 errors/bp	Technique: Reversion (pH 7.8)
Human Pol alpha	Fidelity of DNA synthesis catalyzed by human DNA polymerase alpha and HIV-1 reverse transcriptase: effect of reaction pH.	Nucleotide Substitution Rate	0.000256 errors/bp	Technique: Reversion (pH 8.6)
Human Pol alpha	Fidelity of DNA synthesis catalyzed by human DNA polymerase alpha and HIV-1 reverse transcriptase: effect of reaction pH.	Full length or truncated	Full length
Human Pol alpha	Fidelity of DNA synthesis catalyzed by human DNA polymerase alpha and HIV-1 reverse transcriptase: effect of reaction pH.	Specific Activity	3.27E+04 units/mg
Human Pol alpha	Fidelity and processivity of DNA synthesis by DNA polymerase kappa, the product of the human DINB1 gene.	Nucleotide Substitution Rate	0.00016 errors/bp
Human Pol alpha	DEOXYNUCLEOTIDE-POLYMERIZING ENZYMES OF CALF THYMUS GLAND. I. LARGE SCALE PURIFICATION OF TERMINAL AND REPLICATIVE DEOXYNUCLEOTIDYL TRANSFERASES.	Optimal pH	pH 7