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

BRENDA support

Literature summary for 4.6.1.18 extracted from

  • Rodriguez, M.; Benito, A.; Ribo, M.; Vilanova, M.
    Characterization of the dimerization process of a domain-swapped dimeric variant of human pancreatic ribonuclease (2006), FEBS J., 273, 1166-1176.
    View publication on PubMed
Search for more literature for 4.6.1.18

Protein Variants

Protein Variants Comment Organism
additional information enzyme variant PM8, in which the sequence of the N-terminal domain has been substituted by that of bovine seminal ribonuclease and Pro101 has been substituted by Glu. At 29°C in 20% (v/v) ethanol, a significant portion of PM8 is in dimeric form without formation of higher oligomers. Dissociation constant of this dimer is 5 mM at 29°C. A decrease in temperature shifts the monomer-dimer equilibrium to dimer. Model for dimerization with an open interface formed first and then intersubunit interactions stabilize the hinge loop in a conformation that completely displaces the equilibrium between nonswapped and swapped dimers to swapped ones Homo sapiens
R4A/K6A/Q9E/D16G/S17N more exolytic cleavage preference than parental pancreatic ribonuclease Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.34
-
 poly (C) wild-type, 25°C, pH 5.0 Homo sapiens
0.435
-
 cyclic 2',3'-cytidine monophosphate mutant R4A/K6A/Q9E/D16G/S17N, 25°C, pH 5.0 Homo sapiens
0.44
-
 cyclic 2',3'-cytidine monophosphate wild-type, 25°C, pH 5.0 Homo sapiens
0.47
-
 poly (C) mutant R4A/K6A/Q9E/D16G/S17N, 25°C, pH 5.0 Homo sapiens

Organic Solvent Stability

Organic Solvent Comment Organism
Ethanol at 29°C in 20% (v/v) ethanol, a significant portion of enzyme variant PM8, in which the sequence of the N-terminal domain has been substituted by that of bovine seminal ribonuclease and Pro101 has been substituted by Glu is in dimeric form without appearance of higher oligomers Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P07998
-
-
Homo sapiens P07998 comparison of pancreatic ribonuclease and ribonuclease A
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclic 2',3'-cytidine monophosphate + H2O
-
 Homo sapiens 3'-CMP
-
 ?
additional information pancreatic ribonuclease does not act randomly and shows a more endonucleolytic pattern when compared with ribonuclease A. Pancreatic ribonuclease prefers the binding and cleavage of longer substrate molecules with the phosphodiester bond that is broken 8-11 nucleotides away from at least one of the ends of substrate Homo sapiens ?
-
 ?
poly (C) + H2O
-
 Homo sapiens 3'-CMP + 3'-phospho-oligo(C)
-
 ?

Subunits

Subunits Comment Organism
More enzyme variant PM8, in which the sequence of the N-terminal domain has been substituted by that of bovine seminal ribonuclease and Pro101 has been substituted by Glu. At 29°C in 20% (v/v) ethanol, a significant portion of PM8 is in dimeric form without formation of higher oligomers. Dissociation constant of this dimer is 5 mM at 29°C. A decrease in temperature shifts the monomer-dimer equilibrium to dimer. Model for dimerization with an open interface formed first and then intersubunit interactions stabilize the hinge loop in a conformation that completely displaces the equilibrium between nonswapped and swapped dimers to swapped ones Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.36
-
 cyclic 2',3'-cytidine monophosphate wild-type, 25°C, pH 5.0 Homo sapiens
0.45
-
 cyclic 2',3'-cytidine monophosphate mutant R4A/K6A/Q9E/D16G/S17N, 25°C, pH 5.0 Homo sapiens
13.3
-
 poly (C) wild-type, 25°C, pH 5.0 Homo sapiens
16
-
 poly (C) mutant R4A/K6A/Q9E/D16G/S17N, 25°C, pH 5.0 Homo sapiens