Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Anissimova, M.V.; Baek, W.O.; Varlamov, V.P.; Mrabet, N.T.; Vijayalakshmi, M.A.
    Natural and chemically induced oligomeric ribonucleases: structural study by immobilized metal ion affinity electrophoresis and their functional relationship (2006), J. Mol. Recognit., 19, 287-298.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.6.1.18 pancreas
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.6.1.18 3
-
 enzyme monomer after lyophilization Bos taurus
4.6.1.18 6.08
-
 enzyme dimer form I Bos taurus
4.6.1.18 11.67
-
 enzyme dimer form I Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.18 poly(A)poly(U) + H2O
-
 Bos taurus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.6.1.18 More lyophilization of enzyme from 50% acetic acid solution leads to formation of two dimers and several oligomeric forms. Study on relationship between surface histidine topography in oligomeric forms and catalytic property. Comparison with seminal ribonucleases. Oligomerization also results in modification of the affinity toward the immobilized transition-metal chelate iminodiacetic acid-Cu(II) Bos taurus