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Probing the substrate specificity of an enzyme catalyzing inactivation of streptogramin B antibiotics using LC–MS and LC–MS/MS
Author(s) -
Bateman Kevin P.,
Thibault Pierre,
Yang Keqian,
White Robert L.,
Vining Leo C.
Publication year - 1997
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/(sici)1096-9888(199711)32:10<1057::aid-jms558>3.0.co;2-d
Subject(s) - chemistry , moiety , virginiamycin , enzyme , stereochemistry , antibiotics , residue (chemistry) , depsipeptide , substrate (aquarium) , biochemistry , oceanography , geology
LC–MS and LC–MS/MS analyses indicated that an enzyme responsible for inactivating the antibiotic etamycin is specific for streptogramins and acts on both type B‐I and B‐II streptogramin subgroups. No enzymatic activity was detected for other cyclodepsipeptides such as surfactins and viscosin. It was demonstrated using analogs of etamycin that the picolinyl moiety is essential to obtain enzyme‐generated ring‐opened compounds. Because the picolinyl moiety is also essential for the biological activity of streptogramins, it is proposed that this residue is a distinctive topographic feature in the binding of this group of antibiotics to enzyme active sites. © 1997 John Wiley & Sons, Ltd.