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At least 793 records · Page 44Linked to original sources
PubMed1976

[Inhibition effects of extracellular glucosyltransferase from Streptococcus mutans].

The extracellular, gel-electrophoretically pure glucosyl transferase (GT) of Streptococcus mutans st.227 was incubated with various inhibitors and the synthetic product quantitatively determined. The GT activity was increased with low urea concentration (0.3 - 1.2 M) and inhibited with higher urea molarity. Sodium dodecyl sulfate and quarternary ammonium compounds (detergents) have a clear inhibiting effect starting with 0.005%, while NaF, KSCN, ethylene diamine tetra-acetic acid and sugar alcohols do not have any influence.

Enzyme Inhibitors↗
PubMed1978

[Phosphorylase and glucosyltransferases at the level of reactive astrocytes. A histochemical study].

Implantation of cobalt powder in the cerebral cortex of rat determines an epileptogenic focus where two types of reactive astrocytes are observed. The first type is mostly represented in the subcortical white matter but it does exist in the cortex around the implant. Phosphorylase and branching enzyme are both very active in these cells which are filled with glycogen. The second type is limited to the cortex and phosphorylase activity leads to an unbranched polysaccharid. These cells correspond to the "activated astrocytes" described by the authors in a previous paper and observed round irritative lesions which, in the cerebral cortex, produce epileptogenic foci.

1,4-alpha-Glucan Branching Enzyme↗
PubMed2006

Induction of a salicylic acid glucosyltransferase, AtSGT1, is an early disease response in Arabidopsis thaliana.

Endogenous salicylic acid (SA) and its predominant conjugates, SA 2-O-beta-D-glucoside (SAG) and the glucose ester of SA (SGE), increase dramatically during plant defense responses. Here I report the isolation and characterization of an Arabidopsis thaliana UDP-glucose:SA glucosyltransferase1 (AtSGT1) gene using a tobacco SGT gene previously reported, whose product catalyzes the formation of both SAG and SGE. The recombinant AtSGT1 protein had significant activities with SA and benzoic acid, and synthesized SAG and SGE. Northern blot analysis showed that AtSGT1 was rapidly induced both by exogenous SA and infection with the bacterial pathogen Pseudomonas syringae, indicating that pathogen-inducible AtSGT1 expression is an early disease response and may be involved in the accumulation of glucosyl SA during pathogenesis.

Amino Acid Sequence↗
PubMed1979

Properties of a soluble polyprenyl phosphate: UDP-D-glucose glucosyltransferase.

A soluble enzyme that catalyzes the transfer of D-glucose from UDP-D-glucose to dolichyl phosphate has been prepared by sonic oscillation of Acanthamoeba castellani cysts. The product of catalysis is dolichyl beta-D-glucosyl phosphate. The enzyme requires a divalent cation, either magnesium or manganese, and the presence of a reducing agent for maximum activity. Solanesyl phosphate and ficaprenyl phosphate are alternative substrates, apparently at lower rates, but GDP-D-glucose, UDP-D-glucuronic acid, UDP-N-acetyl-D-glucosamine, and UDP-D-xylose are not substrates. The temperature optimum is 30 degrees C, the pH optimum is pH 7.0, the Km for UDP-Glc is 9.1 microM and for dolichyl phosphate it is 4.5 microM. Uridine monophosphate and UDP are inhibitors of the reaction, UDP causing reversal and UMP being a competitive inhibitor of UDP-Glc with a Ki of 62 microM. The enzyme can be stored indefinitely below -20 degrees C, is stable for several days at 4 degrees C, but is half-inactivated within 2 h at 30 degrees C and completely inactivated within 10 min at 52 degrees C.

Amoeba↗