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Characterization of PurF‐like proteins from Sulfolobus solfataricus
Author(s) -
Belanger Maura Comeau,
Zilinskas Egidijus,
Sarisky Catherine A
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.790.1
Subject(s) - sulfolobus solfataricus , glutamine amidotransferase , gene , biochemistry , protein subunit , bacillus subtilis , chemistry , biology , genetics , computational biology , glutamine , archaea , amino acid , bacteria
The first step in purine biosynthesis converts PP 1 ‐ribose‐P (PPRP) and glutamine into β‐P‐ribosylamine (PRA) and glutamate. The enzyme that catalyzes this reaction is called phosphoribosylpyrophosphate amidotransferase (GPATase or PurF). This enzyme has been extensively characterized in both prokaryotes ( Bacillus subtilis ) and in eukaryotes (human) but has never been characterized in an archaeon. In Sulfolobus solfataricus , a well characterized archaeon, the gene most likely to code for the PurF protein is SSO0632. The neighboring gene, SSO0633, while similar to other PurF‐like genes, does not code for the necessary active site cysteine. Both genes have been successfully cloned in pMAL‐c5E vector. Protein expression and experimental characterization of these proteins will be discussed. Funding for this project was received from a Cottrell College Science Award.