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, E., Marechal, L.R., Quesada Allue, L.A.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p127_Belocopitow
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spelling todo:paper_03008177_v16_n2-3_p127_Belocopitow2023-10-03T15:17:42Z Enzymatic synthesis of polyprenol monophosphate mannose in insects Belocopitow, E. Marechal, L.R. Quesada Allue, L.A. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, E.
Marechal, L.R.
Quesada Allue, L.A.
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.
format JOUR
author Belocopitow, E.
Marechal, L.R.
Quesada Allue, L.A.
author_facet Belocopitow, E.
Marechal, L.R.
Quesada Allue, L.A.
author_sort Belocopitow, E.
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
url http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p127_Belocopitow
work_keys_str_mv AT belocopitowe enzymaticsynthesisofpolyprenolmonophosphatemannoseininsects
AT marechallr enzymaticsynthesisofpolyprenolmonophosphatemannoseininsects
AT quesadaalluela enzymaticsynthesisofpolyprenolmonophosphatemannoseininsects
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