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Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase

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Standard

Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase. / Hurtado-Guerrrero, Ramón; Pena Diaz, Javier; Montalvetti, Andrea; Ruiz-Pérez, Luis M; González-Pacanowska, Dolores.

I: FEBS letters, Bind 510, Nr. 3, 16.01.2002, s. 141-4.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Hurtado-Guerrrero, R, Pena Diaz, J, Montalvetti, A, Ruiz-Pérez, LM & González-Pacanowska, D 2002, 'Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase', FEBS letters, bind 510, nr. 3, s. 141-4.

APA

Hurtado-Guerrrero, R., Pena Diaz, J., Montalvetti, A., Ruiz-Pérez, L. M., & González-Pacanowska, D. (2002). Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase. FEBS letters, 510(3), 141-4.

Vancouver

Hurtado-Guerrrero R, Pena Diaz J, Montalvetti A, Ruiz-Pérez LM, González-Pacanowska D. Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase. FEBS letters. 2002 jan 16;510(3):141-4.

Author

Hurtado-Guerrrero, Ramón ; Pena Diaz, Javier ; Montalvetti, Andrea ; Ruiz-Pérez, Luis M ; González-Pacanowska, Dolores. / Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase. I: FEBS letters. 2002 ; Bind 510, Nr. 3. s. 141-4.

Bibtex

@article{63577242398b475393488ad6b4d65385,
title = "Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase",
abstract = "A detailed kinetic analysis of the recombinant soluble enzyme 3-hydroxy-3-methylglutaryl CoA reductase (HMGR) from Trypanosoma cruzi has been performed. The enzyme catalyzes the normal anabolic reaction and the reductant is NADPH. It also catalyzes the oxidation of mevalonate but at a lower proportion compared to the anabolic reaction. We report that the catalytically active species of HMGR in solution is the tetrameric form. Fluvastatin inhibited competitively the enzyme while cerivastatin binds by a mechanism which is more accurately described by a biphasic process characteristic of a class of 'slow, tight-binding' inhibitors.",
keywords = "Animals, Binding, Competitive, Catalysis, Electrophoresis, Polyacrylamide Gel, Enzyme Activation, Fatty Acids, Monounsaturated, Hydroxymethylglutaryl CoA Reductases, Hydroxymethylglutaryl-CoA Reductase Inhibitors, Indoles, Kinetics, Mevalonic Acid, NADP, Oxidation-Reduction, Protein Structure, Quaternary, Pyridines, Trypanosoma cruzi",
author = "Ram{\'o}n Hurtado-Guerrrero and {Pena Diaz}, Javier and Andrea Montalvetti and Ruiz-P{\'e}rez, {Luis M} and Dolores Gonz{\'a}lez-Pacanowska",
year = "2002",
month = "1",
day = "16",
language = "English",
volume = "510",
pages = "141--4",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "3",

}

RIS

TY - JOUR

T1 - Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase

AU - Hurtado-Guerrrero, Ramón

AU - Pena Diaz, Javier

AU - Montalvetti, Andrea

AU - Ruiz-Pérez, Luis M

AU - González-Pacanowska, Dolores

PY - 2002/1/16

Y1 - 2002/1/16

N2 - A detailed kinetic analysis of the recombinant soluble enzyme 3-hydroxy-3-methylglutaryl CoA reductase (HMGR) from Trypanosoma cruzi has been performed. The enzyme catalyzes the normal anabolic reaction and the reductant is NADPH. It also catalyzes the oxidation of mevalonate but at a lower proportion compared to the anabolic reaction. We report that the catalytically active species of HMGR in solution is the tetrameric form. Fluvastatin inhibited competitively the enzyme while cerivastatin binds by a mechanism which is more accurately described by a biphasic process characteristic of a class of 'slow, tight-binding' inhibitors.

AB - A detailed kinetic analysis of the recombinant soluble enzyme 3-hydroxy-3-methylglutaryl CoA reductase (HMGR) from Trypanosoma cruzi has been performed. The enzyme catalyzes the normal anabolic reaction and the reductant is NADPH. It also catalyzes the oxidation of mevalonate but at a lower proportion compared to the anabolic reaction. We report that the catalytically active species of HMGR in solution is the tetrameric form. Fluvastatin inhibited competitively the enzyme while cerivastatin binds by a mechanism which is more accurately described by a biphasic process characteristic of a class of 'slow, tight-binding' inhibitors.

KW - Animals

KW - Binding, Competitive

KW - Catalysis

KW - Electrophoresis, Polyacrylamide Gel

KW - Enzyme Activation

KW - Fatty Acids, Monounsaturated

KW - Hydroxymethylglutaryl CoA Reductases

KW - Hydroxymethylglutaryl-CoA Reductase Inhibitors

KW - Indoles

KW - Kinetics

KW - Mevalonic Acid

KW - NADP

KW - Oxidation-Reduction

KW - Protein Structure, Quaternary

KW - Pyridines

KW - Trypanosoma cruzi

M3 - Journal article

C2 - 11801242

VL - 510

SP - 141

EP - 144

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 3

ER -

ID: 138821727