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Literature summary for 3.2.2.27 extracted from

  • Koulis, A.; Cowan, D.A.; Pearl, L.H.; Savva, R.
    Uracil-DNA glycosylase activities in hyperthermophilic micro-organisms (1996), FEMS Microbiol. Lett., 143, 267-271.
    View publication on PubMed
Search for more literature for 3.2.2.27

Inhibitors

Inhibitors Comment Organism Structure
uracil-DNA glycosylase inhibitor protein
-
 Pyrobaculum islandicum
uracil-DNA glycosylase inhibitor protein
-
 Pyrococcus furiosus
uracil-DNA glycosylase inhibitor protein
-
 Saccharolobus shibatae
uracil-DNA glycosylase inhibitor protein
-
 Saccharolobus solfataricus
uracil-DNA glycosylase inhibitor protein
-
 Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Pyrobaculum islandicum
-
-
-
Pyrococcus furiosus
-
-
-
Saccharolobus shibatae
-
-
-
Saccharolobus solfataricus
-
-
-
Thermotoga maritima
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.82
-
 pH 7.0, 80°C Pyrococcus furiosus
1.15
-
 pH 6.5, 80°C Pyrobaculum islandicum
1.2
-
 pH 6.5, 90°C Pyrobaculum islandicum
1.23
-
 pH 6.5, 100°C Pyrobaculum islandicum
1.33
-
 pH 7.0, 100°C Pyrococcus furiosus
1.67
-
 pH 7.0, 90°C Pyrococcus furiosus
1.78
-
 pH 5.8, 100°C Saccharolobus shibatae
2.67
-
 pH 5.8, 80°C Saccharolobus shibatae
2.9
-
 pH 5.8, 90°C Saccharolobus shibatae
9.05
-
 pH 6.0, 100°C Saccharolobus solfataricus
11.1
-
 pH 6.0, 80°C Saccharolobus solfataricus
11.9
-
 pH 6.0, 90°C Saccharolobus solfataricus
13.1
-
 pH 5.8, 90°C Thermotoga maritima
13.7
-
 pH 5.8, 100°C Thermotoga maritima
14.7
-
 pH 5.8, 80°C Thermotoga maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.8
-
-
 Saccharolobus shibatae
6
-
-
 Saccharolobus solfataricus
6.5
-
-
 Thermotoga maritima
6.5
-
-
 Pyrobaculum islandicum
7
-
-
 Pyrococcus furiosus

General Information

General Information Comment Organism
physiological function hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. One of the most common hydrolytic damage events is the deamination of cytosine to uracil. The enzyme excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Thus it restores and protects the template function of DNA Pyrococcus furiosus
physiological function hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. One of the most common hydrolytic damage events is the deamination of cytosine to uracil. The enzyme excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Thus it restores and protects the template function of DNA Saccharolobus solfataricus
physiological function hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. One of the most common hydrolytic damage events is the deamination of cytosine to uracil. The enzyme excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Thus it restores and protects the template function of DNA Saccharolobus shibatae
physiological function hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. One of the most common hydrolytic damage events is the deamination of cytosine to uracil. The enzyme excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Thus it restores and protects the template function of DNA Thermotoga maritima
physiological function hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. One of the most common hydrolytic damage events is the deamination of cytosine to uracil. The enzyme excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Thus it restores and protects the template function of DNA Pyrobaculum islandicum