Information on EC 2.6.99.1 - dATP(dGTP)-DNA purinetransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.6.99.1
-
RECOMMENDED NAME
GeneOntology No.
dATP(dGTP)-DNA purinetransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dATP + depurinated DNA = deoxyribose triphosphate + DNA
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitrogenous group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
dATP(dGTP):depurinated-DNA purine transferase
The purine residue is transferred on to the apurinic site forming a normal glycosylic bond. dATP reacts at sites of the double-stranded depurinated DNA that lack adenine, and dGTP at sites that lack guanine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dATP + depurinated DNA
deoxyribose triphosphate + purinated DNA
show the reaction diagram
dATP + depurinated poly(dA-dT)
deoxyribose triphosphate + purinated poly(dA-dT)
show the reaction diagram
-
dGTP cannot act as substrate
-
?
dGTP + depurinated DNA
deoxyribose triphosphate + purinated DNA
show the reaction diagram
dGTP + depurinated poly(dG-dC)
deoxyribose triphosphate + purinated poly(dG-dC)
show the reaction diagram
-
dATP cannot act as substrate
-
?
dTTP + depurinated DNA
deoxyribose triphosphate + purinated DNA
show the reaction diagram
-
lower activity than that of dATP and dGTP, incorporation is supressed in the presence of dATP
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
specific requirement, cannot be replaced by NH4+, Na+, Mg2+ or Mn2+
Li+
-
supports activity to a small degree
Mg2+
-
required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Caffeine
EDTA
-
complete inhibition at 1.3 mM
additional information
-
inhibited by high salt concentration e.g. 1 M NaCl
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cultured
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
-
glycerol density gradient centrifugation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
complete inactivation after 15 min at 60°C
-
sensitive to freezing and heating, extremely sensitive to dialysis
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable, activity retained for less than 1 week after purification, addition of phenylmethylsulfonyl fluoride or N-alpha-p-tosyl-L-lysine chloromethylketone hydrochloride can stabilize enzymatic fractions
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial, using DEAE-cellulose and phosphocellulose chromatography followed by glycerol gradient centrifugation
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