Literature summary for 3.4.24.75 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 .

Search for more literature for 3.4.24.75

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli M15 cells	Staphylococcus simulans

General Stability

General Stability	Organism
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
Staphylococcus aureus cells + H2O	Staphylococcus simulans	Staphylococcus aureus ATCC 29213	fragments of elastin	-	?

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus simulans	P10547	-	-

Purification (Commentary)

Purification (Comment)	Organism
WorkBeads 40S cation exchange column chromatography	Staphylococcus simulans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pentaglycine + H2O	pentaglycine peptide sc-471644A	Staphylococcus simulans	?	-	?
Staphylococcus aureus cells + H2O	Staphylococcus aureus ATCC 29213	Staphylococcus simulans	fragments of elastin	-	?

Subunits

Subunits	Comment	Organism
?	x * 29000, SDS-PAGE	Staphylococcus simulans
?	x * 45000, lysostaphin fused it with an anti-parallel alpha-helical dimerization domain, SDS-PAGE	Staphylococcus simulans

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)