Initiation of glycogen biosynthesis in Escherichia coli studies of the properties of the enzymes involved

The properties of the enzymes involved in the initiation of glycogen biosynthesis in Escherichia coli were studied. It was found that the enzymic activities which transfer the glycosyl residues from UDPglucose or ADPglucose for the glucoprotein synthesis had differing stabilities upon storage at 4°C...

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Autores principales:	Barengo, R., Krisman, C.R.
Formato:	JOUR
Materias:	glycogen adenosine diphosphate glucose:protein glucosyltransferase animal experiment escherichia coli in vitro study uridine diphosphate glucose:protein glucosyltransferase Adenosine Diphosphate Glucose Escherichia coli Glucosyltransferases Glycogen Glycogen Synthase Kinetics Substrate Specificity Uridine Diphosphate Glucose
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_03044165_v540_n2_p190_Barengo
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_03044165_v540_n2_p190_Barengo
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spelling	todo:paper_03044165_v540_n2_p190_Barengo2023-10-03T15:20:49Z Initiation of glycogen biosynthesis in Escherichia coli studies of the properties of the enzymes involved Barengo, R. Krisman, C.R. glycogen adenosine diphosphate glucose:protein glucosyltransferase animal experiment escherichia coli in vitro study uridine diphosphate glucose:protein glucosyltransferase Adenosine Diphosphate Glucose Escherichia coli Glucosyltransferases Glycogen Glycogen Synthase Kinetics Substrate Specificity Uridine Diphosphate Glucose The properties of the enzymes involved in the initiation of glycogen biosynthesis in Escherichia coli were studied. It was found that the enzymic activities which transfer the glycosyl residues from UDPglucose or ADPglucose for the glucoprotein synthesis had differing stabilities upon storage at 4°C. The small amount of glycogen and the saccharide firmly bound to the membrane preparation, were degraded during the storage period. The activity measured in fresh and in stored preparations gave different time dependence curves. The stored preparation had a lag period which could be due to the transfer of the first glucose units to the protein. Both UDPglucose and ADPglucose: protein glucosyltransferases were affected in different ways by detergents. Based on the results presented, it may be concluded that both enzymatic activities are due to different enzymes. Furthermore, both enzymatic activities are different from that which transfers glucose from ADPglucose to glycogen. The following mechanism for the de novo synthesis is suggested. Glycogen in E. coli could be initiated by two different enzymes which transfer glucose to a protein acceptor either from UDPglucose or ADPglucose. Once the saccharide linked to the protein has reached a certain size it is almost exclusively enlarged by another ADPglucose-dependent enzyme. The participation of branching enzyme will produce a polysaccharide with the characteristics of glycogen. © 1978. Fil:Barengo, R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03044165_v540_n2_p190_Barengo
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	glycogen adenosine diphosphate glucose:protein glucosyltransferase animal experiment escherichia coli in vitro study uridine diphosphate glucose:protein glucosyltransferase Adenosine Diphosphate Glucose Escherichia coli Glucosyltransferases Glycogen Glycogen Synthase Kinetics Substrate Specificity Uridine Diphosphate Glucose
spellingShingle	glycogen adenosine diphosphate glucose:protein glucosyltransferase animal experiment escherichia coli in vitro study uridine diphosphate glucose:protein glucosyltransferase Adenosine Diphosphate Glucose Escherichia coli Glucosyltransferases Glycogen Glycogen Synthase Kinetics Substrate Specificity Uridine Diphosphate Glucose Barengo, R. Krisman, C.R. Initiation of glycogen biosynthesis in Escherichia coli studies of the properties of the enzymes involved
topic_facet	glycogen adenosine diphosphate glucose:protein glucosyltransferase animal experiment escherichia coli in vitro study uridine diphosphate glucose:protein glucosyltransferase Adenosine Diphosphate Glucose Escherichia coli Glucosyltransferases Glycogen Glycogen Synthase Kinetics Substrate Specificity Uridine Diphosphate Glucose
description	The properties of the enzymes involved in the initiation of glycogen biosynthesis in Escherichia coli were studied. It was found that the enzymic activities which transfer the glycosyl residues from UDPglucose or ADPglucose for the glucoprotein synthesis had differing stabilities upon storage at 4°C. The small amount of glycogen and the saccharide firmly bound to the membrane preparation, were degraded during the storage period. The activity measured in fresh and in stored preparations gave different time dependence curves. The stored preparation had a lag period which could be due to the transfer of the first glucose units to the protein. Both UDPglucose and ADPglucose: protein glucosyltransferases were affected in different ways by detergents. Based on the results presented, it may be concluded that both enzymatic activities are due to different enzymes. Furthermore, both enzymatic activities are different from that which transfers glucose from ADPglucose to glycogen. The following mechanism for the de novo synthesis is suggested. Glycogen in E. coli could be initiated by two different enzymes which transfer glucose to a protein acceptor either from UDPglucose or ADPglucose. Once the saccharide linked to the protein has reached a certain size it is almost exclusively enlarged by another ADPglucose-dependent enzyme. The participation of branching enzyme will produce a polysaccharide with the characteristics of glycogen. © 1978.
format	JOUR
author	Barengo, R. Krisman, C.R.
author_facet	Barengo, R. Krisman, C.R.
author_sort	Barengo, R.
title	Initiation of glycogen biosynthesis in Escherichia coli studies of the properties of the enzymes involved
title_short	Initiation of glycogen biosynthesis in Escherichia coli studies of the properties of the enzymes involved
title_full	Initiation of glycogen biosynthesis in Escherichia coli studies of the properties of the enzymes involved
title_fullStr	Initiation of glycogen biosynthesis in Escherichia coli studies of the properties of the enzymes involved
title_full_unstemmed	Initiation of glycogen biosynthesis in Escherichia coli studies of the properties of the enzymes involved
title_sort	initiation of glycogen biosynthesis in escherichia coli studies of the properties of the enzymes involved
url	http://hdl.handle.net/20.500.12110/paper_03044165_v540_n2_p190_Barengo
work_keys_str_mv	AT barengor initiationofglycogenbiosynthesisinescherichiacolistudiesofthepropertiesoftheenzymesinvolved AT krismancr initiationofglycogenbiosynthesisinescherichiacolistudiesofthepropertiesoftheenzymesinvolved
_version_	1782026649755189248

Initiation of glycogen biosynthesis in Escherichia coli studies of the properties of the enzymes involved

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