Enzymatic synthesis of polyprenol monophosphate mannose in insects

The microsomal fraction of insects was found to contain an enzyme which transfers mannose from guanosine diphosphate mannose to an endogenous or exogenous insect lipid and to other acceptors such as dolichol monophosphate or ficaprenol monophosphate. This activity depended on the presence of Triton...

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Autores principales:	Belocopitow, Enrique, Quesada Allué, Luis Alberto
Publicado:	1977
Materias:	dolichol phosphate mannose arthropod in vitro study microsome polyprenyl phosphate theoretical study Animal Cobalt Diptera Enzyme Activation Hexosephosphates Hexosyltransferases Hydrogen-Ion Concentration Kinetics Larva Magnesium Manganese Mannosyltransferases Microsomes Phospholipids Polyethylene Glycols Pupa Temperature Terpenes Triatoma Triatominae
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p127_Belocopitow http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p127_Belocopitow
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_03008177_v16_n2-3_p127_Belocopitow
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spelling	paper:paper_03008177_v16_n2-3_p127_Belocopitow2023-06-08T15:27:22Z Enzymatic synthesis of polyprenol monophosphate mannose in insects Belocopitow, Enrique Quesada Allué, Luis Alberto dolichol phosphate mannose arthropod in vitro study microsome polyprenyl phosphate theoretical study Animal Cobalt Diptera Enzyme Activation Hexosephosphates Hexosyltransferases Hydrogen-Ion Concentration Kinetics Larva Magnesium Manganese Mannosyltransferases Microsomes Phospholipids Polyethylene Glycols Pupa Temperature Terpenes Triatoma Triatominae The microsomal fraction of insects was found to contain an enzyme which transfers mannose from guanosine diphosphate mannose to an endogenous or exogenous insect lipid and to other acceptors such as dolichol monophosphate or ficaprenol monophosphate. This activity depended on the presence of Triton X-100 and magnesium ions, the optimal concentration of the latter being 10mM. The optimal temperature of the reaction was 25 °C and the maximal activity was obtained at pH 7.9. The mannolipid formed behaved as a monophosphodiester when chromatographed on DEAE-cellulose. Weak acid treatment of the product liberated mannose. Its behaviour both on thin layer and Sephadex G-150 chromatography would indicate the presence of a number of isoprenyl units similar to the dolichol and different from the ficaprenol derivative. Stability to phenol treatment indicated that the lipid fraction of the mannolipid is an ±-saturated polyprenol phosphate similar to dolichol monophosphate. © 1977 Dr. W. Junk b.v. Publishers. Fil:Belocopitow, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Quesada Allue, L.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1977 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p127_Belocopitow http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p127_Belocopitow
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	dolichol phosphate mannose arthropod in vitro study microsome polyprenyl phosphate theoretical study Animal Cobalt Diptera Enzyme Activation Hexosephosphates Hexosyltransferases Hydrogen-Ion Concentration Kinetics Larva Magnesium Manganese Mannosyltransferases Microsomes Phospholipids Polyethylene Glycols Pupa Temperature Terpenes Triatoma Triatominae
spellingShingle	dolichol phosphate mannose arthropod in vitro study microsome polyprenyl phosphate theoretical study Animal Cobalt Diptera Enzyme Activation Hexosephosphates Hexosyltransferases Hydrogen-Ion Concentration Kinetics Larva Magnesium Manganese Mannosyltransferases Microsomes Phospholipids Polyethylene Glycols Pupa Temperature Terpenes Triatoma Triatominae Belocopitow, Enrique Quesada Allué, Luis Alberto Enzymatic synthesis of polyprenol monophosphate mannose in insects
topic_facet	dolichol phosphate mannose arthropod in vitro study microsome polyprenyl phosphate theoretical study Animal Cobalt Diptera Enzyme Activation Hexosephosphates Hexosyltransferases Hydrogen-Ion Concentration Kinetics Larva Magnesium Manganese Mannosyltransferases Microsomes Phospholipids Polyethylene Glycols Pupa Temperature Terpenes Triatoma Triatominae
description	The microsomal fraction of insects was found to contain an enzyme which transfers mannose from guanosine diphosphate mannose to an endogenous or exogenous insect lipid and to other acceptors such as dolichol monophosphate or ficaprenol monophosphate. This activity depended on the presence of Triton X-100 and magnesium ions, the optimal concentration of the latter being 10mM. The optimal temperature of the reaction was 25 °C and the maximal activity was obtained at pH 7.9. The mannolipid formed behaved as a monophosphodiester when chromatographed on DEAE-cellulose. Weak acid treatment of the product liberated mannose. Its behaviour both on thin layer and Sephadex G-150 chromatography would indicate the presence of a number of isoprenyl units similar to the dolichol and different from the ficaprenol derivative. Stability to phenol treatment indicated that the lipid fraction of the mannolipid is an ±-saturated polyprenol phosphate similar to dolichol monophosphate. © 1977 Dr. W. Junk b.v. Publishers.
author	Belocopitow, Enrique Quesada Allué, Luis Alberto
author_facet	Belocopitow, Enrique Quesada Allué, Luis Alberto
author_sort	Belocopitow, Enrique
title	Enzymatic synthesis of polyprenol monophosphate mannose in insects
title_short	Enzymatic synthesis of polyprenol monophosphate mannose in insects
title_full	Enzymatic synthesis of polyprenol monophosphate mannose in insects
title_fullStr	Enzymatic synthesis of polyprenol monophosphate mannose in insects
title_full_unstemmed	Enzymatic synthesis of polyprenol monophosphate mannose in insects
title_sort	enzymatic synthesis of polyprenol monophosphate mannose in insects
publishDate	1977
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p127_Belocopitow http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p127_Belocopitow
work_keys_str_mv	AT belocopitowenrique enzymaticsynthesisofpolyprenolmonophosphatemannoseininsects AT quesadaallueluisalberto enzymaticsynthesisofpolyprenolmonophosphatemannoseininsects
_version_	1768546442908008448

Enzymatic synthesis of polyprenol monophosphate mannose in insects

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