A novel Entamoeba histolytica inositol phosphate kinase catalyzes the formation of 5PP-Ins(1,2,3,4,6)P(5)
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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, Vol. 181, No. 1, 01.01.2012, p. 49-52.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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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 -