PuuE allantoinase and the CE4 protein family (Bachelor thesis)
Μπούτρης, Νικηφόρος/ Boutris, Nikiforos
The PuuE enzyme is an allantoinase different in structure and amino acid sequence from typical allantoinases. Allantoinases catalyze the oxidation of allantoin, hydrolyzing the amide bond and producing allantoate. This reaction is one of several steps in the metabolic pathway of purine degradation. The degradation of allantoin releases molecules containing nitrogen, which provide sustenance to specific bacteria. Using a wide range of protein comparison tools, we studied the primary, secondary and tertiary structural differences of PuuE allantoinase and the members of the Carbohydrate Esterase family 4, CE4. We present that PuuE allantoinase shows similarities in structure and sequence with a subgroup of CE4 proteins. In particular, the presence of the NodB domain in both PuuE and CE4 proteins attracted our interest. The NodB domain is a disturbed a/b barrel, which is typically found in CE4 proteins. In the NodB domain, specific, conserved amino acid motifs are responsible for binding the metal ion of the active site, for forming the active site itself and for participating in crucial interactions with the substrate. The results of this study challenge the original classification of some proteins as CE4 family members and ask for further investigation in order their specific substrates and enzymatic family to be correctly identified.
Institution and School/Department of submitter: | Δημοκρίτειο Πανεπιστήμιο Θράκης. Σχολή Επιστημών Υγείας. Τμήμα Μοριακής Βιολογίας και Γενετικής |
Subject classification: | Proteins |
Keywords: | Allantoinase,CE4 protein family,NobB domain,Αλλαντοϊνάση,Οικογένεια πρωτεϊνών CE4,Επικράτεια NobB |
URI: | https://repo.lib.duth.gr/jspui/handle/123456789/18699 http://dx.doi.org/10.26257/heal.duth.17425 |
Appears in Collections: | ΤΜΗΜΑ ΜΟΡΙΑΚΗΣ ΒΙΟΛΟΓΙΑΣ & ΓΕΝΕΤΙΚΗΣ |
Files in This Item:
File | Description | Size | Format | |
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BoutrisN_2023.pdf | Πτυχιακή εργασία | 5.83 MB | Adobe PDF | View/Open |
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https://repo.lib.duth.gr/jspui/handle/123456789/18699
http://dx.doi.org/10.26257/heal.duth.17425
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