Glutamate:4,5‐dioxovaleric acid transaminase from Euglena gracilis Kinetic studies

The kinetic properties of the enzyme l‐glutamate:4,5‐dioxovaleric acid aminotransferase (Glu: DOVA transaminase) from Euglena gracilis have been studied. 5‐Aminolevulinic acid formation was linear with time for at least 45 min at 37°C and l‐glutamate was the most effective amino‐group donor. Linewea...

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Publicado:	1989
Materias:	aminolevulinate aminotransferase aminotransferase animal article darkness enzyme specificity enzyme stability enzymology Euglena gracilis growth, development and aging isolation and purification kinetics Animal Darkness Enzyme Stability Kinetics Substrate Specificity Support, Non-U.S. Gov't Transaminases
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v182_n3_p657_LOMBARDO http://hdl.handle.net/20.500.12110/paper_00142956_v182_n3_p657_LOMBARDO
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00142956_v182_n3_p657_LOMBARDO
record_format	dspace
spelling	paper:paper_00142956_v182_n3_p657_LOMBARDO2023-06-08T14:36:41Z Glutamate:4,5‐dioxovaleric acid transaminase from Euglena gracilis Kinetic studies aminolevulinate aminotransferase aminotransferase animal article darkness enzyme specificity enzyme stability enzymology Euglena gracilis growth, development and aging isolation and purification kinetics Animal Darkness Enzyme Stability Euglena gracilis Kinetics Substrate Specificity Support, Non-U.S. Gov't Transaminases The kinetic properties of the enzyme l‐glutamate:4,5‐dioxovaleric acid aminotransferase (Glu: DOVA transaminase) from Euglena gracilis have been studied. 5‐Aminolevulinic acid formation was linear with time for at least 45 min at 37°C and l‐glutamate was the most effective amino‐group donor. Lineweaver‐Burk double‐reciprocal plots suggested a ping‐pong reaction mechanism, with Km values for l‐glutamate and DOVA of 1.92 mM and 0.48 mM respectively. Competitive parabolic substrate inhibition by DOVA at concentrations greater than 3.5–4.5 mM was observed. Glyoxylate (4–10 mM) was found to be a competitive inhibitor with respect to DOVA, whereas at low concentrations (0–4 mM) noncompetitive plots were obtained. An analysis of the possible enzyme forms involved, was carried out. In more crude preparations most of the enzyme is found to be in the form of an enzyme‐glutamate complex. Copyright © 1989, Wiley Blackwell. All rights reserved 1989 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v182_n3_p657_LOMBARDO http://hdl.handle.net/20.500.12110/paper_00142956_v182_n3_p657_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	aminolevulinate aminotransferase aminotransferase animal article darkness enzyme specificity enzyme stability enzymology Euglena gracilis growth, development and aging isolation and purification kinetics Animal Darkness Enzyme Stability Euglena gracilis Kinetics Substrate Specificity Support, Non-U.S. Gov't Transaminases
spellingShingle	aminolevulinate aminotransferase aminotransferase animal article darkness enzyme specificity enzyme stability enzymology Euglena gracilis growth, development and aging isolation and purification kinetics Animal Darkness Enzyme Stability Euglena gracilis Kinetics Substrate Specificity Support, Non-U.S. Gov't Transaminases Glutamate:4,5‐dioxovaleric acid transaminase from Euglena gracilis Kinetic studies
topic_facet	aminolevulinate aminotransferase aminotransferase animal article darkness enzyme specificity enzyme stability enzymology Euglena gracilis growth, development and aging isolation and purification kinetics Animal Darkness Enzyme Stability Euglena gracilis Kinetics Substrate Specificity Support, Non-U.S. Gov't Transaminases
description	The kinetic properties of the enzyme l‐glutamate:4,5‐dioxovaleric acid aminotransferase (Glu: DOVA transaminase) from Euglena gracilis have been studied. 5‐Aminolevulinic acid formation was linear with time for at least 45 min at 37°C and l‐glutamate was the most effective amino‐group donor. Lineweaver‐Burk double‐reciprocal plots suggested a ping‐pong reaction mechanism, with Km values for l‐glutamate and DOVA of 1.92 mM and 0.48 mM respectively. Competitive parabolic substrate inhibition by DOVA at concentrations greater than 3.5–4.5 mM was observed. Glyoxylate (4–10 mM) was found to be a competitive inhibitor with respect to DOVA, whereas at low concentrations (0–4 mM) noncompetitive plots were obtained. An analysis of the possible enzyme forms involved, was carried out. In more crude preparations most of the enzyme is found to be in the form of an enzyme‐glutamate complex. Copyright © 1989, Wiley Blackwell. All rights reserved
title	Glutamate:4,5‐dioxovaleric acid transaminase from Euglena gracilis Kinetic studies
title_short	Glutamate:4,5‐dioxovaleric acid transaminase from Euglena gracilis Kinetic studies
title_full	Glutamate:4,5‐dioxovaleric acid transaminase from Euglena gracilis Kinetic studies
title_fullStr	Glutamate:4,5‐dioxovaleric acid transaminase from Euglena gracilis Kinetic studies
title_full_unstemmed	Glutamate:4,5‐dioxovaleric acid transaminase from Euglena gracilis Kinetic studies
title_sort	glutamate:4,5‐dioxovaleric acid transaminase from euglena gracilis kinetic studies
publishDate	1989
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v182_n3_p657_LOMBARDO http://hdl.handle.net/20.500.12110/paper_00142956_v182_n3_p657_LOMBARDO
_version_	1768542721067188224

Glutamate:4,5‐dioxovaleric acid transaminase from Euglena gracilis Kinetic studies

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