Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis

The kinetic properties of L-glutamate:glyoxylate transminase have been investigated. Glycine formation was linear with both protein concentration and incubation time. L-glutamate was the most effective amino donor. Optimal concentrations for L-glutamate and glyoxylate were 150-200 mM and 10-20 mM, r...

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Detalles Bibliográficos
Autores principales:	Lombardo, María Elisa, Araujo, Lidia Susana, Batlle, Alcira María del Carmen
Publicado:	1996
Materias:	5-aminolevulinic acid biosynthesis Euglena gracilis Glutamate:4,5-dioxovalerate trasaminase Glutamate:glyoxylate transaminase aminotransferase glutamic acid glycine glyoxylic acid valeric acid derivative article controlled study enzyme inhibition enzyme kinetics enzyme mechanism enzyme substrate complex euglena gracilis nonhuman priority journal transamination
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10111344_v36_n3_p241_Lombardo http://hdl.handle.net/20.500.12110/paper_10111344_v36_n3_p241_Lombardo
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_10111344_v36_n3_p241_Lombardo
record_format	dspace
spelling	paper:paper_10111344_v36_n3_p241_Lombardo2023-06-08T15:59:40Z Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis Lombardo, María Elisa Araujo, Lidia Susana Batlle, Alcira María del Carmen 5-aminolevulinic acid biosynthesis Euglena gracilis Glutamate:4,5-dioxovalerate trasaminase Glutamate:glyoxylate transaminase aminotransferase glutamic acid glycine glyoxylic acid valeric acid derivative article controlled study enzyme inhibition enzyme kinetics enzyme mechanism enzyme substrate complex euglena gracilis nonhuman priority journal transamination The kinetic properties of L-glutamate:glyoxylate transminase have been investigated. Glycine formation was linear with both protein concentration and incubation time. L-glutamate was the most effective amino donor. Optimal concentrations for L-glutamate and glyoxylate were 150-200 mM and 10-20 mM, respectively. Initial velocity studies suggested a ping-pong reaction mechanism with a K(m) value of 89.90-66.50 mM for L-glutamate and of 12.50-10.75 mM for glyoxylate. A competitive parabolic substrate inhibition by glyoxylate at concentrations greater than 20 mM was observed. A pure linear non-competitive inhibition between glyoxylate and 4,5-dioxovaleric acid (1.1-2.8 mM) was found. We show here that in vivo different enzymes exist for the transamination of glyoxylate and DOVA. Fil:Lombardo, M.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Araujo, L.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1996 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10111344_v36_n3_p241_Lombardo http://hdl.handle.net/20.500.12110/paper_10111344_v36_n3_p241_Lombardo
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	5-aminolevulinic acid biosynthesis Euglena gracilis Glutamate:4,5-dioxovalerate trasaminase Glutamate:glyoxylate transaminase aminotransferase glutamic acid glycine glyoxylic acid valeric acid derivative article controlled study enzyme inhibition enzyme kinetics enzyme mechanism enzyme substrate complex euglena gracilis nonhuman priority journal transamination
spellingShingle	5-aminolevulinic acid biosynthesis Euglena gracilis Glutamate:4,5-dioxovalerate trasaminase Glutamate:glyoxylate transaminase aminotransferase glutamic acid glycine glyoxylic acid valeric acid derivative article controlled study enzyme inhibition enzyme kinetics enzyme mechanism enzyme substrate complex euglena gracilis nonhuman priority journal transamination Lombardo, María Elisa Araujo, Lidia Susana Batlle, Alcira María del Carmen Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis
topic_facet	5-aminolevulinic acid biosynthesis Euglena gracilis Glutamate:4,5-dioxovalerate trasaminase Glutamate:glyoxylate transaminase aminotransferase glutamic acid glycine glyoxylic acid valeric acid derivative article controlled study enzyme inhibition enzyme kinetics enzyme mechanism enzyme substrate complex euglena gracilis nonhuman priority journal transamination
description	The kinetic properties of L-glutamate:glyoxylate transminase have been investigated. Glycine formation was linear with both protein concentration and incubation time. L-glutamate was the most effective amino donor. Optimal concentrations for L-glutamate and glyoxylate were 150-200 mM and 10-20 mM, respectively. Initial velocity studies suggested a ping-pong reaction mechanism with a K(m) value of 89.90-66.50 mM for L-glutamate and of 12.50-10.75 mM for glyoxylate. A competitive parabolic substrate inhibition by glyoxylate at concentrations greater than 20 mM was observed. A pure linear non-competitive inhibition between glyoxylate and 4,5-dioxovaleric acid (1.1-2.8 mM) was found. We show here that in vivo different enzymes exist for the transamination of glyoxylate and DOVA.
author	Lombardo, María Elisa Araujo, Lidia Susana Batlle, Alcira María del Carmen
author_facet	Lombardo, María Elisa Araujo, Lidia Susana Batlle, Alcira María del Carmen
author_sort	Lombardo, María Elisa
title	Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis
title_short	Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis
title_full	Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis
title_fullStr	Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis
title_full_unstemmed	Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis
title_sort	kinetic studies on the glutamate:glyoxylate transaminase of euglena gracilis
publishDate	1996
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10111344_v36_n3_p241_Lombardo http://hdl.handle.net/20.500.12110/paper_10111344_v36_n3_p241_Lombardo
work_keys_str_mv	AT lombardomariaelisa kineticstudiesontheglutamateglyoxylatetransaminaseofeuglenagracilis AT araujolidiasusana kineticstudiesontheglutamateglyoxylatetransaminaseofeuglenagracilis AT batllealciramariadelcarmen kineticstudiesontheglutamateglyoxylatetransaminaseofeuglenagracilis
_version_	1768542045746495488

Kinetic studies on the glutamate:glyoxylate transaminase of Euglena gracilis

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