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A novel Entamoeba histolytica inositol phosphate kinase catalyzes the formation of 5PP-Ins(1,2,3,4,6)P(5)

Standard

A novel Entamoeba histolytica inositol phosphate kinase catalyzes the formation of 5PP-Ins(1,2,3,4,6)P(5). / Löser, Benjamin; Nalaskowski, Marcus M; Fanick, Werner; Lin, Hongying; Tannich, Egbert; Mayr, Georg W.

in: MOL BIOCHEM PARASIT, Jahrgang 181, Nr. 1, 01.01.2012, S. 49-52.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Löser, B, Nalaskowski, MM, Fanick, W, Lin, H, Tannich, E & Mayr, GW 2012, 'A novel Entamoeba histolytica inositol phosphate kinase catalyzes the formation of 5PP-Ins(1,2,3,4,6)P(5)', MOL BIOCHEM PARASIT, Jg. 181, Nr. 1, S. 49-52. https://doi.org/10.1016/j.molbiopara.2011.09.008

APA

Löser, B., Nalaskowski, M. M., Fanick, W., Lin, H., Tannich, E., & Mayr, G. W. (2012). A novel Entamoeba histolytica inositol phosphate kinase catalyzes the formation of 5PP-Ins(1,2,3,4,6)P(5). MOL BIOCHEM PARASIT, 181(1), 49-52. https://doi.org/10.1016/j.molbiopara.2011.09.008

Vancouver

Löser B, Nalaskowski MM, Fanick W, Lin H, Tannich E, Mayr GW. A novel Entamoeba histolytica inositol phosphate kinase catalyzes the formation of 5PP-Ins(1,2,3,4,6)P(5). MOL BIOCHEM PARASIT. 2012 Jan 1;181(1):49-52. https://doi.org/10.1016/j.molbiopara.2011.09.008

Bibtex

@article{537005de36a34a6c939ac48d18b8933c,
title = "A novel Entamoeba histolytica inositol phosphate kinase catalyzes the formation of 5PP-Ins(1,2,3,4,6)P(5)",
abstract = "The parasitic protozoan Entamoeba histolytica is able to invade human tissues by secreting proteolytic enzymes. This secretion is regulated by inositol phosphate-mediated Ca(2+) release from internal stores. To further investigate the inositol phosphate metabolism of Entamoeba histolytica four putative inositol phosphate kinase genes (ehipk1-4) were identified and their expression analyzed by real-time quantitative PCR using RNA of trophozoites. Furthermore inositol phosphate kinase EhIPK1 was recombinantly expressed, purified and enzymatically characterized. Its main activity is the conversion of InsP(6) to 5PP-Ins(1,2,3,4,6)P(5), one of the main inositol phosphates found in Entamoeba histolytica. Remarkably, EhIPK1 possesses several additional enzymatic activities, e.g. the phosphorylation of the Ca(2+)-releasing second messenger Ins(1,4,5)P(3).We were able to identify several compounds with inhibitory potential against EhIPK1. Because of the important role of inositol phosphates in the invasion of human tissues by Entamoeba histolytica, inositol phosphate metabolizing enzymes are interesting targets for novel therapeutic approaches.",
keywords = "Amino Acid Sequence, Entamoeba histolytica, Enzyme Inhibitors, Gene Expression, Gene Expression Profiling, Inositol Phosphates, Molecular Sequence Data, Phosphotransferases (Alcohol Group Acceptor), Real-Time Polymerase Chain Reaction, Recombinant Proteins, Sequence Homology, Amino Acid, Substrate Specificity",
author = "Benjamin L{\"o}ser and Nalaskowski, {Marcus M} and Werner Fanick and Hongying Lin and Egbert Tannich and Mayr, {Georg W}",
note = "Copyright {\textcopyright} 2011 Elsevier B.V. All rights reserved.",
year = "2012",
month = jan,
day = "1",
doi = "10.1016/j.molbiopara.2011.09.008",
language = "English",
volume = "181",
pages = "49--52",
journal = "MOL BIOCHEM PARASIT",
issn = "0166-6851",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - A novel Entamoeba histolytica inositol phosphate kinase catalyzes the formation of 5PP-Ins(1,2,3,4,6)P(5)

AU - Löser, Benjamin

AU - Nalaskowski, Marcus M

AU - Fanick, Werner

AU - Lin, Hongying

AU - Tannich, Egbert

AU - Mayr, Georg W

N1 - Copyright © 2011 Elsevier B.V. All rights reserved.

PY - 2012/1/1

Y1 - 2012/1/1

N2 - The parasitic protozoan Entamoeba histolytica is able to invade human tissues by secreting proteolytic enzymes. This secretion is regulated by inositol phosphate-mediated Ca(2+) release from internal stores. To further investigate the inositol phosphate metabolism of Entamoeba histolytica four putative inositol phosphate kinase genes (ehipk1-4) were identified and their expression analyzed by real-time quantitative PCR using RNA of trophozoites. Furthermore inositol phosphate kinase EhIPK1 was recombinantly expressed, purified and enzymatically characterized. Its main activity is the conversion of InsP(6) to 5PP-Ins(1,2,3,4,6)P(5), one of the main inositol phosphates found in Entamoeba histolytica. Remarkably, EhIPK1 possesses several additional enzymatic activities, e.g. the phosphorylation of the Ca(2+)-releasing second messenger Ins(1,4,5)P(3).We were able to identify several compounds with inhibitory potential against EhIPK1. Because of the important role of inositol phosphates in the invasion of human tissues by Entamoeba histolytica, inositol phosphate metabolizing enzymes are interesting targets for novel therapeutic approaches.

AB - The parasitic protozoan Entamoeba histolytica is able to invade human tissues by secreting proteolytic enzymes. This secretion is regulated by inositol phosphate-mediated Ca(2+) release from internal stores. To further investigate the inositol phosphate metabolism of Entamoeba histolytica four putative inositol phosphate kinase genes (ehipk1-4) were identified and their expression analyzed by real-time quantitative PCR using RNA of trophozoites. Furthermore inositol phosphate kinase EhIPK1 was recombinantly expressed, purified and enzymatically characterized. Its main activity is the conversion of InsP(6) to 5PP-Ins(1,2,3,4,6)P(5), one of the main inositol phosphates found in Entamoeba histolytica. Remarkably, EhIPK1 possesses several additional enzymatic activities, e.g. the phosphorylation of the Ca(2+)-releasing second messenger Ins(1,4,5)P(3).We were able to identify several compounds with inhibitory potential against EhIPK1. Because of the important role of inositol phosphates in the invasion of human tissues by Entamoeba histolytica, inositol phosphate metabolizing enzymes are interesting targets for novel therapeutic approaches.

KW - Amino Acid Sequence

KW - Entamoeba histolytica

KW - Enzyme Inhibitors

KW - Gene Expression

KW - Gene Expression Profiling

KW - Inositol Phosphates

KW - Molecular Sequence Data

KW - Phosphotransferases (Alcohol Group Acceptor)

KW - Real-Time Polymerase Chain Reaction

KW - Recombinant Proteins

KW - Sequence Homology, Amino Acid

KW - Substrate Specificity

U2 - 10.1016/j.molbiopara.2011.09.008

DO - 10.1016/j.molbiopara.2011.09.008

M3 - SCORING: Journal article

C2 - 22001062

VL - 181

SP - 49

EP - 52

JO - MOL BIOCHEM PARASIT

JF - MOL BIOCHEM PARASIT

SN - 0166-6851

IS - 1

ER -