Literature summary for 4.2.99.18 extracted from

Miroshnikova, A.D.; Kuznetsova, A.A.; Vorobjev, Y.N.; Kuznetsov, N.A.; Fedorova, O.S.
Effects of mono- and divalent metal ions on DNA binding and catalysis of human apurinic/apyrimidinic endonuclease 1 (2016), Mol. Biosyst., 12, 1527-1539 .

Search for more literature for 4.2.99.18

Cloned(Commentary)

Cloned (Comment)	Organism
gene APE1, recombinant expression of enzyme in Escherichia coli strain Rosetta II(DE3)	Homo sapiens

General Stability

General Stability	Organism
Mg2+ ions stabilize the protein structure and the enzyme-substrate complex	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
Ca2+	Ca2+ cause a complete loss of catalytic activity of APE1 with retention of binding potential	Homo sapiens
Cu2+	Cu2+ ions abrogate the DNA binding ability of APE1, possibly, due to a strong interaction with DNA bases and the sugar-phosphate backbone	Homo sapiens
K+	initial DNA binding efficiency significantly decreases at a high concentration (5-250 mM) of monovalent K+ ions	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	stopped-flow fluorescence techniques to conduct a comparative kinetic analysis of the conformational transitions in human apurinic/apyrimidinic endonuclease 1 (APE1) and in DNA containing an abasic site in the course of their interaction. Influence of different concentrations of Mg2+ and other metal ions on stopped-flow kinetics, overview	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	activates, required and involved in catalytic mechanism, Mg2+ ions stabilize the protein structure and the enzyme-substrate complex. Analysis of enzyme-substrate complexes with bound Mg2+	Homo sapiens
Mn2+	activates	Homo sapiens
additional information	effects of monovalent (K+) and divalent (Mg2+, Mn2+, Ca2+, Zn2+, Cu2+, and Ni2+) metal ions on DNA binding and catalytic stages, circular dichroism spectra and calculation of the contact area between APE1 and DNA, overview. The first step of substrate binding (corresponding to formation of a primary enzyme-substrate complex) does not depend on the concentration (0.05-5.0 mM) or the nature of divalent metal ions. In contrast, the initial DNA binding efficiency significantly decreases at a high concentration (5-250 mM) of monovalent K+ ions, indicating the involvement of electrostatic interactions in this stage. The enzymatic activity of APE1 is increased in the ascending order Zn2+, Ni2+, Mn2+, and Mg2+	Homo sapiens
Ni2+	activates	Homo sapiens
Zn2+	activates	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P27695	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	fluorescent-labeled oligodeoxynucleotides substrates are used, overview	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	analysis of enzyme-substrate complexes with bound Mg2+	Homo sapiens

Synonyms

Synonyms	Comment	Organism
APE1	-	Homo sapiens
apurinic/apyrimidinic endonuclease 1	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.8	-	DNA binding assay at	Homo sapiens

General Information

General Information	Comment	Organism
additional information	stopped-flow fluorescence techniques are used to conduct a comparative kinetic analysis of the conformational transitions in human apurinic/apyrimidinic endonuclease 1 (APE1) and in DNA containing an abasic site in the course of their interaction. Analysis of enzyme-substrate complexes with bound Mg2+	Homo sapiens

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Release 2023.1 (January 2023)