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Literature summary 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

Inhibitors

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

Organism

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.2.27 0.82
-
pH 7.0, 80°C Pyrococcus furiosus
3.2.2.27 1.15
-
pH 6.5, 80°C Pyrobaculum islandicum
3.2.2.27 1.2
-
pH 6.5, 90°C Pyrobaculum islandicum
3.2.2.27 1.23
-
pH 6.5, 100°C Pyrobaculum islandicum
3.2.2.27 1.33
-
pH 7.0, 100°C Pyrococcus furiosus
3.2.2.27 1.67
-
pH 7.0, 90°C Pyrococcus furiosus
3.2.2.27 1.78
-
pH 5.8, 100°C Saccharolobus shibatae
3.2.2.27 2.67
-
pH 5.8, 80°C Saccharolobus shibatae
3.2.2.27 2.9
-
pH 5.8, 90°C Saccharolobus shibatae
3.2.2.27 9.05
-
pH 6.0, 100°C Saccharolobus solfataricus
3.2.2.27 11.1
-
pH 6.0, 80°C Saccharolobus solfataricus
3.2.2.27 11.9
-
pH 6.0, 90°C Saccharolobus solfataricus
3.2.2.27 13.1
-
pH 5.8, 90°C Thermotoga maritima
3.2.2.27 13.7
-
pH 5.8, 100°C Thermotoga maritima
3.2.2.27 14.7
-
pH 5.8, 80°C Thermotoga maritima

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.2.27 5.8
-
-
Saccharolobus shibatae
3.2.2.27 6
-
-
Saccharolobus solfataricus
3.2.2.27 6.5
-
-
Thermotoga maritima
3.2.2.27 6.5
-
-
Pyrobaculum islandicum
3.2.2.27 7
-
-
Pyrococcus furiosus

General Information

EC Number General Information Comment Organism
3.2.2.27 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
3.2.2.27 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
3.2.2.27 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
3.2.2.27 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
3.2.2.27 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