Literature summary for 4.2.99.B1 extracted from

Sobol, R.W.; Prasad, R.; Evenski, A.; Baker, A.; Yang, X.P.; Horton, J.K.; Wilson, S.H.
The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity (2000), Nature, 405, 807-810.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in MB36.3 cell, wild-type, SV40 T-Ag transformed cell line haboring the lambda phage transgene lambdaLIZ	Mus musculus
MB38DELTA4, beta-pol null, sensitive to the methylating agent methylmethanesulfonate, SV40 T-Ag transformed cell line haboring the lambda phage transgene lambdaLIZ	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
D256A	site-directed mutagenesis, C-terminal polymerase domain, completely eliminates dRP lyase activity, proficient in DNA synthesis by the polymerase reaction	Mus musculus
K35A/K68A/K72A	site-directed mutagenesis, amino-terminal dRP lyase domain, completely eliminates dRP lyase activity, proficient in DNA synthesis by the polymerase reaction	Mus musculus
K35A/K68A/K72A/D256A	site-directed mutagenesis, amino-terminal dRP lyase domain, deficient in dRP lyase and polymerase activity	Mus musculus
additional information	an active-site deletion mutant of beta-pol, in which residues within the C-terminal portion, residues 263-335 that are required for DNA synthesis are deleted, completely deficient in single-nucleotide base excision repair DNA synthesis, but active in 5'-deoxyribose phosphate removal	Mus musculus
R283A	site-directed mutagenesis, C-terminal polymerase domain, deficient in base excision repair DNA synthesis activity of the polymerase, but has full dRP lyase activity	Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Mus musculus	removal of the 5'-deoxyribose phosphate group is a pivotal step in the base excision repair (BER) pathway in vivo	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
catalysis of the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site in DNA where a DNA-(apurinic or apyrimidinic site) lyase has already cleaved the C-O-P bond 3' to the apurinic or apyrimidinic site	removal of the 5'-deoxyribose phosphate group is a pivotal step in the base excision repair (BER) pathway in vivo.Two important enzymatic steps in mammalian single-nucleotide base excision repair are contributed by beta-pol: DNA resynthesis of the repair patch und lyase removal of 5'-deoxyribose phosphate	Mus musculus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
50-bp DNA containing a single abasic site preincised with AP endonuclease	-	Mus musculus	29-bp DNA fragment + 2-deoxy-D-ribose 5-phosphate	-	?
additional information	removal of the 5'-deoxyribose phosphate group is a pivotal step in the base excision repair (BER) pathway in vivo	Mus musculus	?	-	?

Synonyms

Synonyms	Comment	Organism
beta-pol	-	Mus musculus
DNA beta-polymerase	lyase activity	Mus musculus
dRP lyase	-	Mus musculus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Mus musculus

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Release 2023.1 (January 2023)