Affinity and hydrophobic interactions of penicillin amidase.
Binding of penicillin amidase from E. coli 436 to aniline-, benzylamine- and phenylethylamine-Sepharose was studied. Binding of the enzyme to aniline-Sepharose was exclusively due to hydrophobic interactions. Benzylamine-Sepharose binds the enzyme due to affinity interactions in the absence of ammonium sulphate and due to hydrophobic interactions in the presence of ammonium sulphate. A conformational change in the penicillin amidase molecule due to ammonium sulphate there by exposing the side chain binding site as a hydrophobic core is suggested.
Mali
R S
RS
Sudhakaran
V K
VK
Shewale
J G
JG
D000581:Amidohydrolases / Q000378:metabolism*; D000814:Aniline Compounds / Q000378:metabolism*; D001596:Benzylamines / Q000378:metabolism*; D002846:Chromatography, Affinity; D010399:Penicillin Amidase / Q000378:metabolism*; D010627:Phenethylamines / Q000378:metabolism*
D000814:Aniline Compounds; D001596:Benzylamines; D010627:Phenethylamines; C029261:phenethylamine; C030796:benzylamine; D000581:Amidohydrolases; D010399:Penicillin Amidase; C023650:aniline