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Information on EC 4.2.99.B1 - DNA 5'-deoxyribose phosphate lyase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P53632

for references in articles please use BRENDA:EC4.2.99.B1
preliminary BRENDA-supplied EC number
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.99 Other carbon-oxygen lyases
                4.2.99.B1 DNA 5'-deoxyribose phosphate lyase
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P53632 not found.
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
Synonyms
beta-pol, neil2, drp lyase, polymerase iota, hsv-1 pol, 5'-drp lyase, dna beta-polymerase, atpolib, 5'-deoxyribose phosphate lyase, atpolia, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-deoxyribose-5-phosphate lyase
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Trf4
putative member of X family DNA polymerase, functional homolog of polbeta
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
Trf4 is able to form a Schiff base intermediate with a 5'-deoxyribose-5-phosphate substrate and to excise the abasic residue throuigh a dRP lyase activity and plays a role in single-nucleotide pathway of the base excision repair system. The dRP lyase reaction proceeds through a beta-elimination mechanism, verified by the addition of NaBH4 to trap the Schiff base intermediate, forming a covalent enzyme-DNA complex
SYSTEMATIC NAME
IUBMB Comments
DNA-(apurinic or apyrimidinic site) 5'-deoxy-D-ribose 5-phosphate-lyase
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
52-pb synthetic duplex DNA
? + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
labelled [32P]-uracil at position 22, pretreated with uracil DNA-glycosylase and Escherichia coli endonuclease IV
the percentage of total 2-deoxyribose 5-phosphate excised is calculated by dividing the amount of the dRP lyase product formed in each reaction by the sum of this product and the amount of the substrate DNA containing intact 5'-deoxyribose-5-phosphate
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K552A
site-directed mutagenesis matching the active site of polbeta. The mutant Trf4K552A is overexpressed in a trf4DELTA mutant. The overproduction of Trf4 wild-type increases methylmethane sulfonate resistance similar to that of of the wild-type. The Trf4K552A mutant exhibits hypersensitivity to methylmethane sulfonate, causing double-stranded DNA breaks
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified from recombinant protein of an Escherichia coli expression system
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gellon, L.; Carson, D.R.; Carson, J.P.; Demple, B.
Intrinsic 5'-deoxyribose-5-phosphate lyase activity in Saccharomyces cerevisiae Trf4 protein with a possible role in base excision DNA repair
DNA Repair
7
187-198
2008
Saccharomyces cerevisiae (P53632), Saccharomyces cerevisiae
Manually annotated by BRENDA team