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Literature summary extracted from

  • Minko, I.G.; Kurtz, A.J.; Croteau, D.L.; Van Houten, B.; Harris, T.M.; Lloyd, R.S.
    Initiation of repair of DNA-polypeptide cross-links by the UvrABC nuclease (2005), Biochemistry, 44, 3000-3009.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.25.1 overexpression [Bacillus] caldotenax
3.1.25.1 overexpression Thermotoga maritima

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.25.1 Mg2+
-
 [Bacillus] caldotenax
3.1.25.1 Mg2+
-
 Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.25.1 damaged DNA containing nucleotide cross-links + H2O [Bacillus] caldotenax initiation of nucleotide excision repair of DNA-polypeptide cross-links by the UvrABC nuclease ?
-
 ?
3.1.25.1 damaged DNA containing nucleotide cross-links + H2O Thermotoga maritima initiation of nucleotide excision repair of DNA-polypeptide cross-links by the UvrABC nuclease ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.25.1 Thermotoga maritima
-
-
-
3.1.25.1 [Bacillus] caldotenax
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.25.1 additional information
-
-
 Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.25.1 damaged DNA containing nucleotide cross-links + H2O initiation of nucleotide excision repair of DNA-polypeptide cross-links by the UvrABC nuclease [Bacillus] caldotenax ?
-
 ?
3.1.25.1 damaged DNA containing nucleotide cross-links + H2O initiation of nucleotide excision repair of DNA-polypeptide cross-links by the UvrABC nuclease Thermotoga maritima ?
-
 ?
3.1.25.1 damaged DNA containing nucleotide cross-links + H2O initiation of nucleotide excision repair of DNA-polypeptide cross-links by the UvrABC nuclease, engineering of DNA-peptide or DNA-protein cross-links via linkage at an acrolein-derived gamma-hydroxypropanodeoxyguanosine adduct and an apurinic/apyrimidinic site, the linked peptides are KWKK and KFHEKHHSHRGY, and the protein is the 16 kDa T4 pyrimidine dimer glycosylase/apurinic/apyrimidinic site lyase, incision at the eighth phosphodiester bond 5' of the lesion [Bacillus] caldotenax ?
-
 ?
3.1.25.1 damaged DNA containing nucleotide cross-links + H2O initiation of nucleotide excision repair of DNA-polypeptide cross-links by the UvrABC nuclease, engineering of DNA-peptide or DNA-protein cross-links via linkage at an acrolein-derived gamma-hydroxypropanodeoxyguanosine adduct and an apurinic/apyrimidinic site, the linked peptides are KWKK and KFHEKHHSHRGY, and the protein is the 16 kDa T4 pyrimidine dimer glycosylase/apurinic/apyrimidinic site lyase, incision at the eighth phosphodiester bond 5' of the lesion Thermotoga maritima ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.25.1 UvrA
-
 [Bacillus] caldotenax
3.1.25.1 UvrABC nuclease
-
 [Bacillus] caldotenax
3.1.25.1 UvrABC nuclease
-
 Thermotoga maritima
3.1.25.1 UvrB
-
 [Bacillus] caldotenax
3.1.25.1 UvrC
-
 Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.25.1 55
-
 assay at [Bacillus] caldotenax
3.1.25.1 55
-
 assay at Thermotoga maritima

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.25.1 7.5
-
 assay at [Bacillus] caldotenax
3.1.25.1 7.5
-
 assay at Thermotoga maritima