Phosphatase-Inert Glucosamine 6-Phosphate Mimics Serve as Actuators of theglmSRiboswitch

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Phosphatase-Inert Glucosamine 6-Phosphate Mimics Serve as Actuators of the glmS Riboswitch

The glmS riboswitch is unique among gene-regulating riboswitches and catalytic RNAs. This is because its own metabolite, glucosamine-6-phosphate (GlcN6P), binds to the riboswitch and catalytically participates in the RNA self-cleavage reaction, thereby providing a novel negative feedback mechanism. Given that a number of pathogens harbor the glmS riboswitch, artificial actuators of this potenti...

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N-Acetylation of glucosamine-6-phosphate in Leuconostoc mesenteroides.

A partially purified enzyme (120-fold) from Leuconostoc mesenteroides catalyzed the reversible N-acetylation of d-glucosamine-6-phosphate. Coenzyme A was not required and inhibited the reaction rate. Neither d-glucosamine nor N-acetyl-d-glucosamine served as a substrate for the reversible reaction. The enzyme preparation retained 50% of its original activity after 5 min at 100 C. The K(m) for a...

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Glucosamine 6-phosphate synthase of regenerating rat liver.

When rats were subjected to partial hepatectomy, glucosamine 6-phosphate synthase (EC 5.3.1.19) of the remaining liver underwent alterations both in activity and in molecular form. To study the molecular alterations, glucosamine 6-phosphate synthase was purified from regenerating as well as control liver and was analyzed by isoelectric focusing. Although control liver exhibited only one form of...

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ژورنال

عنوان ژورنال: ACS Chemical Biology

سال: 2014

ISSN: 1554-8929,1554-8937

DOI: 10.1021/cb500458f