Εξειδίκευση τύπου :	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	Substrate Specificity of the Highly Thermostable Esterase EstDZ3
Δημιουργός/Συγγραφέας:	Papanikolaou, Angelos Chatzikonstantinou, Alexandra V Zarafeta, Dimitra Kourkoumelis, Nikolaos [EL] Σκρέτας, Γιώργος[EN] Skretas, George Pavlidis, Ioannis V Stamatis, Haralambos
Ημερομηνία:	2023-03-01
Γλώσσα:	Αγγλικά
ISSN:	1439-4227 1439-7633
DOI:	10.1002/cbic.202200642
Άλλο:	36545817
Περίληψη:	Esterases are among the most studied enzymes, and their applications expand into several branches of industrial biotechnology. Yet, despite the fact that information on their substrate specificity is crucial for selecting or designing the best fitted biocatalyst for the desired application, it cannot be predicted from their amino acid sequence. In this work, we studied the substrate scope of the newly discovered hydrolytic extremozyme, EstDZ3, against a library of esters with variable carbon chain lengths in an effort to understand the crucial amino acids for the substrate selectivity of this enzyme. EstDZ3 appears to be active against a wide range of esters with high selectivity towards medium- to long-carbon chain vinyl esters. In-silico studies of its 3D structure revealed that the selectivity might arise from the mainly hydrophobic nature of the active site's environment.
Τίτλος πηγής δημοσίευσης:	Chembiochem : a European journal of chemical biology
Τόμος/Κεφάλαιο:	24
Τεύχος:	5
Θεματική Κατηγορία:	[EL] Βιοτεχνολογία[EN] Biotechnology [EL] Βιοχημεία[EN] Biochemistry [EL] Δομική Βιολογία[EN] Structural Biology
Λέξεις-Κλειδιά:	Biocatalysis Esterases Molecular docking Molecular dynamics Regioselectivity
EU Grant:	RESEARCH-CREATE-INNOVATE
EU Grant identifier:	T2EDK‐03599
Κάτοχος πνευματικών δικαιωμάτων:	© 2022 The Authors. ChemBioChem published by Wiley-VCH GmbH
Ηλεκτρονική διεύθυνση στον εκδότη (link):	https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202200642
Εμφανίζεται στις συλλογές:	Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο