Search

Your search keyword '"Müllegger J"' showing total 2 results
Start Over Author "Müllegger J" Topic bacillus subtilis
2 results on '"Müllegger J"'

1. Thioglycoligase-based assembly of thiodisaccharides: screening as beta-galactosidase inhibitors.

Author

Kim YW, Chen HM, Kim JH, Müllegger J, Mahuran D, and Withers SG

Subjects
Cloning, Molecular, Disaccharides chemistry, Glycosyltransferases chemistry, Thioglycosides chemistry, beta-Galactosidase genetics, beta-Galactosidase metabolism, Bacillus subtilis enzymology, Disaccharides chemical synthesis, Enzyme Inhibitors pharmacology, Glycosyltransferases metabolism, Ligases metabolism, Thioglycosides biosynthesis, beta-Galactosidase antagonists & inhibitors
Published
2007
Full Text
View/download PDF

2. Identification of the catalytic nucleophile in Family 42 beta-galactosidases by intermediate trapping and peptide mapping: YesZ from Bacillus subtilis.

Author

Shaikh FA, Müllegger J, He S, and Withers SG

Subjects
Amino Acid Sequence, Bacterial Proteins genetics, Base Sequence, Catalytic Domain, Cloning, Molecular, DNA Primers, Kinetics, Molecular Sequence Data, Peptide Mapping, Recombinant Proteins chemistry, Recombinant Proteins metabolism, Sequence Alignment, Sequence Homology, Amino Acid, Spectrometry, Mass, Electrospray Ionization, Thermus enzymology, beta-Galactosidase genetics, Bacillus subtilis metabolism, Bacterial Proteins chemistry, Bacterial Proteins metabolism, beta-Galactosidase chemistry, beta-Galactosidase metabolism
Abstract

The mechanism-based inhibitor 2,4-dinitrophenyl 2-deoxy-2-fluoro-beta-d-galactopyranoside (DNP2FGal) was used to inactivate the Family 42 beta-galactosidase (YesZ) from Bacillus subtilis via the trapping of a glycosyl-enzyme intermediate, thereby tagging the catalytic nucleophile in the active site. Proteolytic digestion of the inactivated enzyme and of a control sample of unlabeled enzyme, followed by comparative high-performance liquid chromatography and mass spectrometric analysis identified a labelled peptide of the sequence ETSPSYAASL. These data, combined with sequence alignments of this region with representative members of Family 42, unequivocally identify the catalytic nucleophile in this enzyme as Glu-295, thereby providing the first direct experimental proof of the identity of this residue within Family 42.

Published
2007
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results