Literature summary for 3.2.1.52 extracted from
Zhang, Y.; Ji, J.; Zhao, X.; Jin, R.; Li, J.; Wan, H.
Expression, purification and enzymatic properties of a beta-N-acetylhexosaminidase from brown planthopper, Nilaparvata lugens (2017), J. Asia Pac. Entomol., 20, 1340-1343 .
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
expressed in baculovirus-infected sf9 insect cells |
Nilaparvata lugens |
Inhibitors
Inhibitors |
Comment |
Organism |
Structure |
Ca2+ |
about 80% residual activity at 1 mM |
Nilaparvata lugens |
|
Cd2+ |
about 85% residual activity at 1 mM |
Nilaparvata lugens |
|
Co2+ |
about 90% residual activity at 1 mM |
Nilaparvata lugens |
|
Cu2+ |
about 80% residual activity at 1 mM |
Nilaparvata lugens |
|
E-64 |
about 70% residual activity at 1 mM |
Nilaparvata lugens |
|
Fe2+ |
about 30% residual activity at 1 mM |
Nilaparvata lugens |
|
Fe3+ |
about 55% residual activity at 1 mM |
Nilaparvata lugens |
|
leupeptin |
about 90% residual activity at 1 mM |
Nilaparvata lugens |
|
Mg2+ |
about 85% residual activity at 1 mM |
Nilaparvata lugens |
|
Mn2+ |
about 85% residual activity at 1 mM |
Nilaparvata lugens |
|
additional information |
not inhibited by aprotinin and trypsin |
Nilaparvata lugens |
|
phenylmethanesulfonyl fluoride |
about 35% residual activity at 1 mM |
Nilaparvata lugens |
|
Zn2+ |
about 85% residual activity at 1 mM |
Nilaparvata lugens |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Nilaparvata lugens |
A0A0C5CE51 |
brown planthopper |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
MagneHis protein purification system |
Nilaparvata lugens |
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
4-nitrophenyl N-acetyl-beta-D-glucosaminide + H2O |
- |
Nilaparvata lugens |
4-nitrophenol + N-acetyl-beta-D-glucosamine |
- |
? |
|
Subunits
Subunits |
Comment |
Organism |
? |
x * 70000, SDS-PAGE |
Nilaparvata lugens |
Synonyms
Synonyms |
Comment |
Organism |
Hex4 |
- |
Nilaparvata lugens |
Temperature Optimum [°C]
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
60 |
- |
- |
Nilaparvata lugens |
Temperature Range [°C]
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
30 |
70 |
about 45% activity at 30°C, about 75% activity at 40°C, about 95% activity at 50°C, 100% activity at 60°C, about 60% activity at 70°C |
Nilaparvata lugens |
Temperature Stability [°C]
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
50 |
- |
the recombinant enzyme exhibits thermal stability with more than 80-60% activity remaining at 50°C for at least 1 h |
Nilaparvata lugens |
pH Optimum
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
6 |
- |
- |
Nilaparvata lugens |
pH Range
pH Minimum |
pH Maximum |
Comment |
Organism |
4 |
7 |
about 70% activity at pH 4.0, about 90% activity at pH 5.0, 100% activity at pH 6.0. about 70% activity at pH 7.0 |
Nilaparvata lugens |