Cloned (Comment) | Organism |
---|---|
mutants A105L, D107A, P125A, G127A, G144A, V165A and F190A are expressed in Escherichia coli. Mutants Y101A, F102A, L162A and G173A are expressed in Pichia pastoris | Momordica charantia |
Crystallization (Comment) | Organism |
---|---|
mutant Y101A in complex with 5'-UMP, resolution at 2.0 A | Momordica charantia |
Protein Variants | Comment | Organism |
---|---|---|
A105L | significant loss of activity, significant decrease in thermostability | Momordica charantia |
D107A | little effect on thermostability | Momordica charantia |
F102A | considerable less stable than the wild-type in guanidine-HCl, significant decrease in thermostability | Momordica charantia |
F190A | significant decrease in thermostability | Momordica charantia |
G127A | moderate decrease in thermostability | Momordica charantia |
G144A | moderate decrease in thermostability | Momordica charantia |
G173A | little effect on thermostability | Momordica charantia |
L162A | unstable | Momordica charantia |
P125A | moderate decrease in thermostability | Momordica charantia |
V165A | moderate decrease in thermostability | Momordica charantia |
Y101A | considerable less stable than the wild-type in guanidine-HCl, significant decrease in thermostability | Momordica charantia |
General Stability | Organism |
---|---|
the wild-type enzyme remains intact during incubation with chymotrypsin for 8 h (pH 8.0, 37°C). Trypsin causes a time-dependent decrease of the RNase MC1 band concomitant with the increase of one peptide. Mutant Y101A is completely degraded by chymotrypsin and trypsin after 2 h. Mutant F102A is also susceptible to protease degradation. In mutants A105L, D107A, P125A, G127A, G144A, V165A, F190A and G173A the degradation pattern is similar to the wild-type. | Momordica charantia |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
21190 | - |
monomer, calculated from amino acid sequence | Momordica charantia |
Organic Solvent | Comment | Organism |
---|---|---|
guanidine-HCl | mutants Y101A (guanidine-HCl concentration at the midpoint of the transition is 1.59 M) and F102A (guanidine-HCl concentration at the midpoint of the transition is 1.64 M) are considerable less stable than the wild-type (guanidine-HCl concentration at the midpoint of the transition is 2.57 M). In mutant P125A guanidine-HCl concentration at the midpoint of the transition is 2.11 M, in mutant G127A guanidine-HCl concentration at the midpoint of the transition is 2.12 M, in mutant G173A guanidine-HCl concentration at the midpoint of the transition is 2.56 M | Momordica charantia |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Momordica charantia | P23540 | bitter gourd | - |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cytidylyl-3',5'-uridine | 37°C, pH 5.5 | Momordica charantia | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ribonuclease MC1 | - |
Momordica charantia |
ribonuclease T2 | - |
Momordica charantia |
RNase MC1 | - |
Momordica charantia |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
47.2 | - |
Tm, mutant Y101A | Momordica charantia |
50.8 | - |
Tm, mutant F102A | Momordica charantia |
56.1 | - |
Tm, mutant F190A | Momordica charantia |
56.9 | - |
Tm, mutant A105L | Momordica charantia |
58.4 | - |
Tm, mutant V165A | Momordica charantia |
60.5 | - |
Tm, mutant G144A | Momordica charantia |
61.7 | - |
Tm, mutant G127A | Momordica charantia |
62.2 | - |
Tm, mutant P125A | Momordica charantia |
63.6 | - |
Tm, mutant D107A | Momordica charantia |
64.2 | - |
Tm, mutant G173A | Momordica charantia |
64.4 | - |
Tm, wild-type | Momordica charantia |