Delta aminolaevulinate dehydratase: its mechanism of action

1. 1. Taking into account available experimental data. a mechanism of action for aminolaevulinate dehydratase is proposed. 2. 2. Besides the formation of a Schiff base between the substrate and the enzyme, the existence of a minimal functional dimer necessary for activity is also considered, as well...

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Detalles Bibliográficos
Autores principales: Del C. Batlle, A.M., Stella, A.M.
Formato: JOUR
Materias:
porphobilinogen synthase
nonbiological model
Histidine
Lysine
Macromolecular Systems
Models, Biological
Porphobilinogen
Porphobilinogen Synthase
Pyrroles
Sulfhydryl Compounds
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0020711X_v9_n12_p861_DelCBatlle
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_0020711X_v9_n12_p861_DelCBatlle
record_format dspace
spelling todo:paper_0020711X_v9_n12_p861_DelCBatlle2023-10-03T14:18:14Z Delta aminolaevulinate dehydratase: its mechanism of action Del C. Batlle, A.M. Stella, A.M. porphobilinogen synthase nonbiological model Histidine Lysine Macromolecular Systems Models, Biological Porphobilinogen Porphobilinogen Synthase Pyrroles Sulfhydryl Compounds 1. 1. Taking into account available experimental data. a mechanism of action for aminolaevulinate dehydratase is proposed. 2. 2. Besides the formation of a Schiff base between the substrate and the enzyme, the existence of a minimal functional dimer necessary for activity is also considered, as well as certain characteristics of the type of interactions involved in the inter-subunit contact sites and the role of histidine residues in the transport of protons from and to the active center. © 1978. Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0020711X_v9_n12_p861_DelCBatlle
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic porphobilinogen synthase
nonbiological model
Histidine
Lysine
Macromolecular Systems
Models, Biological
Porphobilinogen
Porphobilinogen Synthase
Pyrroles
Sulfhydryl Compounds
spellingShingle porphobilinogen synthase
nonbiological model
Histidine
Lysine
Macromolecular Systems
Models, Biological
Porphobilinogen
Porphobilinogen Synthase
Pyrroles
Sulfhydryl Compounds
Del C. Batlle, A.M.
Stella, A.M.
Delta aminolaevulinate dehydratase: its mechanism of action
topic_facet porphobilinogen synthase
nonbiological model
Histidine
Lysine
Macromolecular Systems
Models, Biological
Porphobilinogen
Porphobilinogen Synthase
Pyrroles
Sulfhydryl Compounds
description 1. 1. Taking into account available experimental data. a mechanism of action for aminolaevulinate dehydratase is proposed. 2. 2. Besides the formation of a Schiff base between the substrate and the enzyme, the existence of a minimal functional dimer necessary for activity is also considered, as well as certain characteristics of the type of interactions involved in the inter-subunit contact sites and the role of histidine residues in the transport of protons from and to the active center. © 1978.
format JOUR
author Del C. Batlle, A.M.
Stella, A.M.
author_facet Del C. Batlle, A.M.
Stella, A.M.
author_sort Del C. Batlle, A.M.
title Delta aminolaevulinate dehydratase: its mechanism of action
title_short Delta aminolaevulinate dehydratase: its mechanism of action
title_full Delta aminolaevulinate dehydratase: its mechanism of action
title_fullStr Delta aminolaevulinate dehydratase: its mechanism of action
title_full_unstemmed Delta aminolaevulinate dehydratase: its mechanism of action
title_sort delta aminolaevulinate dehydratase: its mechanism of action
url http://hdl.handle.net/20.500.12110/paper_0020711X_v9_n12_p861_DelCBatlle
work_keys_str_mv AT delcbatlleam deltaaminolaevulinatedehydrataseitsmechanismofaction
AT stellaam deltaaminolaevulinatedehydrataseitsmechanismofaction
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