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Information on EC 2.7.7.7 - DNA-directed DNA polymerase and Organism(s) Thermococcus gorgonarius and UniProt Accession P56689

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.7 DNA-directed DNA polymerase
IUBMB Comments
Catalyses DNA-template-directed extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. Requires a primer, which may be DNA or RNA. See also EC 2.7.7.49 RNA-directed DNA polymerase.
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This record set is specific for:
Thermococcus gorgonarius
UNIPROT: P56689
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Word Map
The taxonomic range for the selected organisms is: Thermococcus gorgonarius
The enzyme appears in selected viruses and cellular organisms
Synonyms
dna polymerase alpha, dna polymerase beta, dna polymerase iii, pol beta, klenow fragment, dna polymerase delta, taq dna polymerase, pol delta, pol alpha, dna polymerase gamma, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxynucleate polymerase
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-
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deoxyribonucleate nucleotidyltransferase
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-
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deoxyribonucleic acid duplicase
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-
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deoxyribonucleic acid polymerase
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deoxyribonucleic duplicase
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deoxyribonucleic polymerase
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deoxyribonucleic polymerase I
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DNA duplicase
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DNA nucleotidyltransferase
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DNA nucleotidyltransferase (DNA-directed)
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DNA polmerase beta
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DNA polymerase
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DNA polymerase alpha
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DNA polymerase gamma
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-
-
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DNA polymerase I
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-
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DNA polymerase II
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-
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DNA polymerase III
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-
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DNA replicase
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-
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DNA-dependent DNA polymerase
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duplicase
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Klenow fragment
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nucleotidyltransferase, deoxyribonucleate
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Pol gamma
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-
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sequenase
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Taq DNA polymerase
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Taq Pol I
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Tca DNA polymerase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase (DNA-directed)
Catalyses DNA-template-directed extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. Requires a primer, which may be DNA or RNA. See also EC 2.7.7.49 RNA-directed DNA polymerase.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-90-2
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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
additional information
?
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the E664 residue (located in thumb domain) acts as a steric gate, which is involved in recognition of the DNA substrate by the enzyme
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DPOL_THEGO
773
0
89812
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor-diffusion technique at 4°C, 2.5 A resolution crystal structure
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jozwiakowski, S.K.; Keith, B.J.; Gilroy, L.; Doherty, A.J.; Connolly, B.A.
An archaeal family-B DNA polymerase variant able to replicate past DNA damage: occurrence of replicative and translesion synthesis polymerases within the B family
Nucleic Acids Res.
42
9949-9963
2014
Thermococcus gorgonarius (P56689)
Manually annotated by BRENDA team
Hopfner, K.P.; Eichinger, A.; Engh, R.A.; Laue, F.; Ankenbauer, W.; Huber, R.; Angerer, B.
Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius
Proc. Natl. Acad. Sci. USA
96
3600-3605
2014
Thermococcus gorgonarius (P56689)
Manually annotated by BRENDA team