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Literature summary for 4.6.1.18 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
Search for more literature for 4.6.1.18

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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