Open AccessImmunological evidence for two types of PQQ‐dependent d ‐glucose dehydrogenase in bacterial membranes and the location of the enzyme in Escherichia coli
Author(s) -
Matsushita K.,
Shinagawa E.,
Inoue T.,
Adachi O.,
Ameyama M.
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01782.x
Subject(s) - escherichia coli , pseudomonas fluorescens , biochemistry , dehydrogenase , enzyme , biology , bacteria , pseudomonas , trypsin , bacterial outer membrane , acetobacter , microbiology and biotechnology , chemistry , fermentation , genetics , gene
Using an antibody raised against d ‐glucose dehydrogenase (EC 1.1.99.17) purified from Pseudomonas fluorescens , immuno‐cross‐reactivity with the enzymes from several bacterial strains and localization of the enzyme in Escherichia coli were examined. The antibody cross‐reacted with glucose dehydrogenases from various Gram‐negative bacteria examined. As a result, it became apparent that the enzymes from Gluconobacter, Acetobacter, Pseudomonas and Acinetobacter , which existed as holoenzymes in the membranes, had lower molecular weights than those from E. coli and Klebsiella , which were apoenzymes. Treatment with trypsin of right‐side out and inside‐out membrane vesicles from E. coli clearly demonstrated that d ‐glucose dehydrogenase was located on the outer surface of the cytoplasmic membrane of E. coli , as had been suggested for Pseudomonas .