PENICILLIN ACYLASE FROM ESCHERICHIA-COLI - CATALYTICALLY ACTIVE SUBUNITS

Citation
Ve. Kabakov et al., PENICILLIN ACYLASE FROM ESCHERICHIA-COLI - CATALYTICALLY ACTIVE SUBUNITS, Biochemistry, 60(5), 1995, pp. 593-596
Citations number
18
Categorie Soggetti
Biology
Journal title
ISSN journal
00062979
Volume
60
Issue
5
Year of publication
1995
Pages
593 - 596
Database
ISI
SICI code
0006-2979(1995)60:5<593:PAFE-C>2.0.ZU;2-4
Abstract
Gel filtration under denaturing conditions was used to isolate the alp ha- and beta-subunits of penicillin acylase (PA). The refolded protein subunits were obtained on removing urea during dialysis. Preparations bf both renatured subunits were found to be catalytically active in t he reaction of hydrolysis of phenylacetic acid p-nitroanilide and this activity decreased with addition of the serine-specific inhibitor PMS F. Catalytic activity of the subunits was also measured in reversed mi celles of Aerosol OT (AOT) in octane, the light (alpha-subunit) being most catalytically active at w(0) = 11.9 and the heavy (beta-subunit) at w(0) = 17.5. The positions of the maxima were in good correlation b oth with theoretically calculated optimal hydration degrees and with; the earlier reported profile of enzymatic activity for native PA in re versed micelles.