Protein Variants | Comment | Organism |
---|---|---|
E41K | with almost the same activity as wild-type enzyme. Glu41 is not involved in substrate binding | Aspergillus oryzae |
E54Q | dramatically less active than the wild-type enzyme | Aspergillus oryzae |
E74K | less active than the wild-type enzyme due to a change in the orientation of the catalytic groups | Aspergillus oryzae |
H85Q | dramatically less active than the wild-type enzyme | Aspergillus oryzae |
Q38A | less active than the wild-type enzyme | Aspergillus oryzae |
R65A | dramatically less active than the wild-type enzyme | Aspergillus oryzae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1510 | - |
polyinosinic acid | pH 6.5, 25ºC, wild-type enzyme | Aspergillus oryzae | |
1600 | - |
polyinosinic acid | pH 6.5, 25ºC, E41K mutant | Aspergillus oryzae | |
1700 | - |
polyinosinic acid | pH 6.5, 25ºC, E74K mutant | Aspergillus oryzae | |
2000 | - |
polyinosinic acid | pH 6.5, 25ºC, R65A mutant | Aspergillus oryzae | |
2500 | - |
polyinosinic acid | pH 6.5, 25ºC, Q38A mutant | Aspergillus oryzae | |
3100 | - |
polyinosinic acid | pH 6.5, 25ºC, E54Q mutant | Aspergillus oryzae | |
5500 | - |
guanylyl-3',5'-uridine | pH 6.5, 25ºC, wild-type enzyme | Aspergillus oryzae | |
5700 | - |
guanylyl-3',5'-uridine | pH 6.5, 25ºC, E74K mutant | Aspergillus oryzae | |
10000 | - |
guanylyl-3',5'-uridine | pH 6.5, 25ºC, E41K mutant | Aspergillus oryzae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus oryzae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
[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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GpU + H2O | - |
Aspergillus oryzae | guanosine 3'-phosphate + uridine | - |
? | |
guanylyl-3',5'-uridine + H2O | GpU | Aspergillus oryzae | guanosine 3'-phosphate + uridine | - |
? | |
polyinosinic acid + H2O | polyI | Aspergillus oryzae | ? | - |
? |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
- |
Aspergillus oryzae |