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Literature summary extracted from

  • Yakovlev, G.I.; Mitkevich, V.A.; Shaw, K.L.; Trevino, S.; Newsom, S.; Pace, C.N.; Makarov, A.A.
    Contribution of active site residues to the activity and thermal stability of ribonuclease Sa (2003), Protein Sci., 12, 2367-2373.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.24 E41K with almost the same activity as wild-type enzyme. Glu41 is not involved in substrate binding Aspergillus oryzae
4.6.1.24 E54Q dramatically less active than the wild-type enzyme Aspergillus oryzae
4.6.1.24 E74K less active than the wild-type enzyme due to a change in the orientation of the catalytic groups Aspergillus oryzae
4.6.1.24 H85Q dramatically less active than the wild-type enzyme Aspergillus oryzae
4.6.1.24 Q38A less active than the wild-type enzyme Aspergillus oryzae
4.6.1.24 R65A dramatically less active than the wild-type enzyme Aspergillus oryzae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.24 1510
-
 polyinosinic acid pH 6.5, 25ºC, wild-type enzyme Aspergillus oryzae
4.6.1.24 1600
-
 polyinosinic acid pH 6.5, 25ºC, E41K mutant Aspergillus oryzae
4.6.1.24 1700
-
 polyinosinic acid pH 6.5, 25ºC, E74K mutant Aspergillus oryzae
4.6.1.24 2000
-
 polyinosinic acid pH 6.5, 25ºC, R65A mutant Aspergillus oryzae
4.6.1.24 2500
-
 polyinosinic acid pH 6.5, 25ºC, Q38A mutant Aspergillus oryzae
4.6.1.24 3100
-
 polyinosinic acid pH 6.5, 25ºC, E54Q mutant Aspergillus oryzae
4.6.1.24 5500
-
 guanylyl-3',5'-uridine pH 6.5, 25ºC, wild-type enzyme Aspergillus oryzae
4.6.1.24 5700
-
 guanylyl-3',5'-uridine pH 6.5, 25ºC, E74K mutant Aspergillus oryzae
4.6.1.24 10000
-
 guanylyl-3',5'-uridine pH 6.5, 25ºC, E41K mutant Aspergillus oryzae

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.24 Aspergillus oryzae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.6.1.24 [RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment] the side chain carboxyl of Glu54 accepts a proton from the ribose 2'OH group and the protonated imidazole ring of His85 donates a proton to the leaving 5'O group. The positively charged side chain of Arg65 is to promote the formation of a negatively charged, pentacovalent intermediate state of the phosphate group Aspergillus oryzae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.24 GpU + H2O
-
 Aspergillus oryzae guanosine 3'-phosphate + uridine
-
 ?
4.6.1.24 guanylyl-3',5'-uridine + H2O GpU Aspergillus oryzae guanosine 3'-phosphate + uridine
-
 ?
4.6.1.24 polyinosinic acid + H2O polyI Aspergillus oryzae ?
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.6.1.24 additional information
-
 the reversibility of the thermal denaturation is generally between 90% and 95%. Q38A and E74K mutants are slightly more stable than the wild-type enzyme. E41K, E54A and R65A mutants are less stable than the wild-type enzyme Aspergillus oryzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6.1.24 6.5
-
-
 Aspergillus oryzae