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1 March 2002 Giardia intestinalis Glucosamine 6-Phosphate Isomerase: the Key Enzyme to Encystment Appears to be Controlled by Ubiquitin Attachment
ALEX B. LOPEZ, MOHAMMED T. HOSSAIN, HARRY VAN KEULEN
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Abstract

The cyst wall of the parasitic protozoan, Giardia intestinalis, is composed of a polymer of N-acetylgalactosamine, the precursor of which is synthesized by an inducible enzyme pathway. The first enzyme in this pathway, glucosamine 6-phosphate isomerase, is transcriptionally regulated. During encystment and in mature cysts this isomerase appears to be modified by ubiquitin attachment. Thus, it might be targeted for destruction by an ubiquitin-mediated pathway, suggesting that glucosamine 6-phosphate isomerase expression is tightly regulated.

ALEX B. LOPEZ, MOHAMMED T. HOSSAIN, and HARRY VAN KEULEN "Giardia intestinalis Glucosamine 6-Phosphate Isomerase: the Key Enzyme to Encystment Appears to be Controlled by Ubiquitin Attachment," The Journal of Eukaryotic Microbiology 49(2), 134-136, (1 March 2002). https://doi.org/10.1111/j.1550-7408.2002.tb00356.x
Received: 20 September 2001; Accepted: 23 December 2001; Published: 1 March 2002
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KEYWORDS
Competition inhibition
cyst wall
encystment
excystation
fusion protein
glutathione transferase
ubiquitin
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