Affiliation:
1. Department of Biology, Rice University, Houston, Texas 77001
Abstract
Guanosine diphosphate
d
-glucose:
d
-glucose-6-phosphate 1-glucosyl-transferase was purified approximately 100-fold from extracts of
Streptomyces hygroscopicus
. The purified enzyme catalyzed the transfer of glucose from guanosine diphosphate-
d
-glucose to glucose-6-phosphate to form trehalose phosphate and guanosine diphosphate. The enzyme was specific for these two substrates and was stimulated by the addition of magnesium ions. The product was characterized as α-α-trehalose-6-phosphate by its physical and chemical properties. The enzyme was present in a large number of
Streptomyces
species, suggesting that this group of organisms synthesized trehalose phosphate in a unique manner. This enzyme was not detected in fungi, since these organisms utilized uridine diphosphate-
d
-glucose as the glucosyl donor.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
31 articles.
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