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Giardia intestinalis Glucosamine 6‐Phosphate Isomerase: the Key Enzyme to Encystment Appears to be Controlled by Ubiquitin Attachment
Author(s) -
LOPEZ ALEX B.,
HOSSAIN MOHAMMED T.,
KEULEN HARRY
Publication year - 2002
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.2002.tb00356.x
Subject(s) - biology , giardia lamblia , enzyme , glucosamine , ubiquitin , biochemistry , isomerase , giardia , triosephosphate isomerase , microbiology and biotechnology , gene
. 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.