Photoinactivation of the < b > < i > Staphylococcus aureus < /i > < /b > Lactose-Specific EIICB Phosphotransferase Component with < b > < i > p < /i > < /b > -azidophenyl- β-D-Galactoside and Phosphorylation of the Covalently Bound Substrate

Conclusion: Phosphorylation of the –OH group at C6 ofp-nitrenephenyl- β-D-galactopyranoside covalently bound to EIICLac by the histidyl-phosphorylated [32P]P ∼EIIBLac domain is a likely explanation for the observed acid resistance. Placingp-nitrenephenyl- β-D-galactopyranoside into the active site of modelled EIICLac suggested that the nitrene binds to the -NH- group of Ser248, which would explain why no sequence data beyond Pro247could be obtained.J Mol Microbiol Biotechnol 2018;28:147 –158
Source: Journal of Molecular Microbiology and Biotechnology - Category: Microbiology Source Type: research