Evaluation of Porcine and <i<Aspergillus oryzae</i< α-Amylases as Possible Model for the Human Enzyme

α-amylases are ubiquitous enzymes belonging to the glycosyl hydrolase (GH13) family, whose members share a high degree of sequence identity, even between distant organisms. To understand the determinants of catalytic activity of α-amylases throughout evolution, and to investigate the use of homologo...
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Autor*in:	Mauro Marengo [verfasserIn] Davide Pezzilli [verfasserIn] Eleonora Gianquinto [verfasserIn] Alex Fissore [verfasserIn] Simonetta Oliaro-Bosso [verfasserIn] Barbara Sgorbini [verfasserIn] Francesca Spyrakis [verfasserIn] Salvatore Adinolfi [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	α-amylases human α-amylase porcine α-amylase

Übergeordnetes Werk:	In: Processes - MDPI AG, 2013, 10(2022), 780, p 780
Übergeordnetes Werk:	volume:10 ; year:2022 ; number:780, p 780

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/pr10040780

Katalog-ID:	DOAJ029650941

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callnumber-first	T - Technology
author	Mauro Marengo
spellingShingle	Mauro Marengo misc TP1-1185 misc QD1-999 misc α-amylases misc <i<Aspergillus oryzae</i< α-amylase misc human α-amylase misc porcine α-amylase misc Chemical technology misc Chemistry Evaluation of Porcine and <i<Aspergillus oryzae</i< α-Amylases as Possible Model for the Human Enzyme
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topic_title	TP1-1185 QD1-999 Evaluation of Porcine and <i<Aspergillus oryzae</i< α-Amylases as Possible Model for the Human Enzyme α-amylases <i<Aspergillus oryzae</i< α-amylase human α-amylase porcine α-amylase
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title	Evaluation of Porcine and <i<Aspergillus oryzae</i< α-Amylases as Possible Model for the Human Enzyme
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title_full	Evaluation of Porcine and <i<Aspergillus oryzae</i< α-Amylases as Possible Model for the Human Enzyme
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author_browse	Mauro Marengo Davide Pezzilli Eleonora Gianquinto Alex Fissore Simonetta Oliaro-Bosso Barbara Sgorbini Francesca Spyrakis Salvatore Adinolfi
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title_sort	evaluation of porcine and <i<aspergillus oryzae</i< α-amylases as possible model for the human enzyme
callnumber	TP1-1185
title_auth	Evaluation of Porcine and <i<Aspergillus oryzae</i< α-Amylases as Possible Model for the Human Enzyme
abstract	α-amylases are ubiquitous enzymes belonging to the glycosyl hydrolase (GH13) family, whose members share a high degree of sequence identity, even between distant organisms. To understand the determinants of catalytic activity of α-amylases throughout evolution, and to investigate the use of homologous enzymes as a model for the human one, we compared human salivary α-amylase, <i<Aspergillus oryzae</i< α-amylase and pancreatic porcine α-amylase, using a combination of in vitro and in silico approaches. Enzyme sequences were aligned, and structures superposed, whereas kinetics were spectroscopically studied by using commercial synthetic substrates. These three enzymes show strikingly different activities, specifically mediated by different ions, despite relevant structural homology. Our study confirms that the function of α-amylases throughout evolution has considerably diverged, although key structural determinants, such as the catalytic triad and the calcium-binding pocket, have been retained. These functional differences need to be carefully considered when α-amylases, from different organisms, are used as a model for the human enzymes. In this frame, particular focus is needed for the setup of proper experimental conditions.
abstractGer	α-amylases are ubiquitous enzymes belonging to the glycosyl hydrolase (GH13) family, whose members share a high degree of sequence identity, even between distant organisms. To understand the determinants of catalytic activity of α-amylases throughout evolution, and to investigate the use of homologous enzymes as a model for the human one, we compared human salivary α-amylase, <i<Aspergillus oryzae</i< α-amylase and pancreatic porcine α-amylase, using a combination of in vitro and in silico approaches. Enzyme sequences were aligned, and structures superposed, whereas kinetics were spectroscopically studied by using commercial synthetic substrates. These three enzymes show strikingly different activities, specifically mediated by different ions, despite relevant structural homology. Our study confirms that the function of α-amylases throughout evolution has considerably diverged, although key structural determinants, such as the catalytic triad and the calcium-binding pocket, have been retained. These functional differences need to be carefully considered when α-amylases, from different organisms, are used as a model for the human enzymes. In this frame, particular focus is needed for the setup of proper experimental conditions.
abstract_unstemmed	α-amylases are ubiquitous enzymes belonging to the glycosyl hydrolase (GH13) family, whose members share a high degree of sequence identity, even between distant organisms. To understand the determinants of catalytic activity of α-amylases throughout evolution, and to investigate the use of homologous enzymes as a model for the human one, we compared human salivary α-amylase, <i<Aspergillus oryzae</i< α-amylase and pancreatic porcine α-amylase, using a combination of in vitro and in silico approaches. Enzyme sequences were aligned, and structures superposed, whereas kinetics were spectroscopically studied by using commercial synthetic substrates. These three enzymes show strikingly different activities, specifically mediated by different ions, despite relevant structural homology. Our study confirms that the function of α-amylases throughout evolution has considerably diverged, although key structural determinants, such as the catalytic triad and the calcium-binding pocket, have been retained. These functional differences need to be carefully considered when α-amylases, from different organisms, are used as a model for the human enzymes. In this frame, particular focus is needed for the setup of proper experimental conditions.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
container_issue	780, p 780
title_short	Evaluation of Porcine and <i<Aspergillus oryzae</i< α-Amylases as Possible Model for the Human Enzyme
url	https://doi.org/10.3390/pr10040780 https://doaj.org/article/e2fb949d6c3544dab3e09145b43db89b https://www.mdpi.com/2227-9717/10/4/780 https://doaj.org/toc/2227-9717
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author2	Davide Pezzilli Eleonora Gianquinto Alex Fissore Simonetta Oliaro-Bosso Barbara Sgorbini Francesca Spyrakis Salvatore Adinolfi
author2Str	Davide Pezzilli Eleonora Gianquinto Alex Fissore Simonetta Oliaro-Bosso Barbara Sgorbini Francesca Spyrakis Salvatore Adinolfi
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up_date	2024-07-03T23:49:44.900Z
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Evaluation of Porcine and <i<Aspergillus oryzae</i< α-Amylases as Possible Model for the Human Enzyme

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