EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.97 | S132A |
active-site mutant |
95603 |
| 3.4.21.97 | A143Q |
all enzyme samples used in this experiments contain an additional mutation, A143Q. The mutation disables one of the internal cleavage sites but has little effects on the kinetic properties of the enzyme |
653320 |
| 3.4.21.97 | A133V |
I-site mutant |
95603 |
| 3.4.21.97 | more |
IC-assemblin and IC-assemblinHis mutants of assemblin, blocked for internal and cryptic site cleavage. Enzymatic activities of pPR mutants are indistinguishable from that of IC-assemblin |
681686 |
| 3.4.21.97 | A143V |
inability of the mutant virus to effect I-site cleavage in infected cells, mutation has no gross effect on the rate of virus production or on the amounts of extracellular virions, noninfectious enveloped particles and dense bodies |
653074 |
| 3.4.21.97 | H47A |
inactive mutant, active if coexpressed with AW5 which encodes the first 179 amino acids of assemblin with the addition of Ile, Gln, Thr |
95597 |
| 3.4.21.97 | S118A |
inactive mutant, active if coexpressed with AW5 which encodes the first 179 amino acids of assemblin with the addition of Ile, Gln, Thr |
95597 |
| 3.4.21.97 | S132A |
is inactive |
677592 |
| 3.4.21.97 | A143T/A144T |
mutant displays better stability than wild-type and has esterase activity toward specific small ester compounds, e.g., Boc-L-Ala-4-nitrophenol |
732540 |
| 3.4.21.97 | A143Q/L229R |
mutant enzyme A143Q/L229R shows approximately a 20% decrease in helical content relative to the mutant enzyme A143Q, mutant enzyme A143Q/L229R has significant lower thermal stability than the mutant enzyme A143Q |
653320 |
