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Literature summary for 3.1.22.1 extracted from

  • Cheng, Y.C.; Hsueh, C.C.; Lu, S.C.; Liao, T.H.
    Identification of three crucial histidine residues (His115, His132 and His297) in porcine deoxyribonuclease II (2006), Biochem. J., 398, 177-185.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
H109L extracellular, about 80% of wild-type activity Sus scrofa
H115 extracellular, very little catalytic activity that may be rescued by imidazole, correct protein folding Sus scrofa
H132L soluble, very little catalytic activity. Protein is improperly folded and degraded via the proteosomal pathway within 24 h Sus scrofa
H206L extracellular, about 66% of wild-type activity Sus scrofa
H207L extracellular, about 40% of wild-type activity Sus scrofa
H274L extracellular, about 45% of wild-type activity Sus scrofa
H297L extracellular, very little catalytic activity that may be rescued by imidazole, correct protein folding Sus scrofa
H322L extracellular, activity similar to wild-type Sus scrofa
H41L extracellular, about 60% of wild-type activity Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa O62855
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
138
-
mutant H207L, pH 4.7 Sus scrofa
172
-
mutant H274L, pH 4.7 Sus scrofa
219
-
mutant H206L, pH 4.7 Sus scrofa
220
-
mutant H41L, pH 4.7 Sus scrofa
287
-
mutant H109L, pH 4.7 Sus scrofa
321
-
wild-type, pH 4.7 Sus scrofa
331
-
mutant H322L, pH 4.7 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
calf thymus DNA + H2O
-
Sus scrofa 3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
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