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Literature summary for 3.1.21.1 extracted from

  • Mannherz, H.G.; Ballweber, E.; Hegyi, G.; Goody, R.S.
    Cross-linked long-pitch actin dimer forms stoichiometric complexes with gelsolin segment 1 and/or deoxyribonuclease I that nonproductively interact with myosin subfragment 1 (2008), Biochemistry, 47, 9335-9343.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
actin inhibition of DNase I activity by increasing concentrations of actin dimer. At equimolar actin subunit to DNase I concentration its DNA degrading is inhibited to only about 50%, whereas full inhibition is obtained when the dimer concentration is that of DNase I, i.e., at double monomer concentration, suggesting that only one monomer of the actin dimer is able to inhibit the DNase I activity, although both appear to be able to bind DNase I. Gelsolin segment 1 bound to the dimer inhibits DNase I more effectively than uncomplexed dimer and has a higher affinity to DNase I than dimer alone Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by chromatography on hydroxylapatite Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
salmon sperm DNA + H2O
-
Bos taurus 5'-phosphooligonucleotides + ?
-
?

Synonyms

Synonyms Comment Organism
deoxyribonuclease I
-
Bos taurus
DNase I
-
Bos taurus