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Information on EC 3.1.11.1 - exodeoxyribonuclease I and Organism(s) Saccharolobus solfataricus and UniProt Accession P26811

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This record set is specific for:
Saccharolobus solfataricus
UNIPROT: P26811 not found.
Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphodiesterase, dna polymerase i, exonuclease i, exonuclease 1, exo i, hexo1, polb1, 3'-to-5' exonuclease, sbcb15, drpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3'5' exonuclease
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-
-
0
DNA deoxyribophosphodiesterase
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-
-
0
dRPase
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-
-
0
E. coli exonuclease I
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-
-
0
Escherichia coli exonuclease I
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-
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0
exonuclease I
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-
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0
Sso polB1
297286
-
SSO0552
297286
locus name
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
0
CAS REGISTRY NUMBER
COMMENTARY hide
9037-46-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dsDNA + H2O
?
show the reaction diagram
the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA
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-
?
single-stranded DNA + H2O
?
show the reaction diagram
3'-5' exonuclease activity, degrades both single-stranded DNA and double-stranded DNA at similar rates
-
-
?
ssDNA + H2O
?
show the reaction diagram
the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NTP
the strong 3'-5' exonuclease activity of polB1 is inhibited by 50% in the presence of 0.002 mM dNTPs, but remains measurable at up to 0.6 mM dNTPs
additional information
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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
in view of the strong exonuclease activity of Sso polB1 on matched dsDNA, its is suggested that Sulfolobus solfataricus may have evolved mechanisms to regulate the exonuclease/polymerase ratio of the enzyme, thereby reducing the cost of proofreading at high temperature
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lou, H.; Duan, Z.; Sun, T.; Huang, L.
Cleavage of double-stranded DNA by the intrinsic 3-5 exonuclease activity of DNA polymerase B1 from the hyperthermophilic archaeon Sulfolobus solfataricus at high temperature
FEMS Microbiol. Lett.
231
111-117
2004
Saccharolobus solfataricus (P26811), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P26811), Saccharolobus solfataricus P2
Manually annotated by BRENDA team
Lou, H.; Duan, Z.; Huo, X.; Huang, L.
Modulation of hyperthermophilic DNA polymerase activity by archaeal chromatin proteins
J. Biol. Chem.
279
127-132
2003
Saccharolobus solfataricus (P26811), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P26811)
Manually annotated by BRENDA team
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