Literature summary extracted from
Grishin, A.V.; Lavrova, N.V.; Lyashchuk, A.M.; Strukova, N.V.; Generalova, M.S.; Ryazanova, A.V.; Shestak, N.V.; Boksha, I.S.; Polyakov, N.B.; Galushkina, Z.M.; Soboleva, L.A.; Vetchinin, S.S.; Pavlov, V.M.; Karyagina, A.S.; Lunin, V.G.
The influence of dimerization on the pharmacokinetics and activity of an antibacterial enzyme lysostaphin (2019), Molecules, 24, 1879 .
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.4.24.75 |
expressed in Escherichia coli M15 cells |
Staphylococcus simulans |
General Stability
EC Number |
General Stability |
Organism |
---|
3.4.24.75 |
lysostaphin fused it with an anti-parallel alpha-helical dimerization domain has a more favorable pharmacokinetic profile with increased terminal half-life compared to monomeric lysostaphin. However, the staphylolytic activity of dimerized lysostaphin is decreased. |
Staphylococcus simulans |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
3.4.24.75 |
Staphylococcus aureus cells + H2O |
Staphylococcus simulans |
Staphylococcus aureus ATCC 29213 |
fragments of elastin |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.24.75 |
Staphylococcus simulans |
P10547 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.4.24.75 |
WorkBeads 40S cation exchange column chromatography |
Staphylococcus simulans |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.24.75 |
pentaglycine + H2O |
pentaglycine peptide sc-471644A |
Staphylococcus simulans |
? |
- |
? |
|
3.4.24.75 |
Staphylococcus aureus cells + H2O |
Staphylococcus aureus ATCC 29213 |
Staphylococcus simulans |
fragments of elastin |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.4.24.75 |
? |
x * 29000, SDS-PAGE |
Staphylococcus simulans |
3.4.24.75 |
? |
x * 45000, lysostaphin fused it with an anti-parallel alpha-helical dimerization domain, SDS-PAGE |
Staphylococcus simulans |