Delta-aminolevulinate dehydratase from free-living Rhizobium

1. 1. δ-Aminolevulinate-dehydratase (ALA-D) from Rhizobium japonicum and Rhizobium meliloti was isolated and some properties were studied. 2. 2. The enzyme from both strains require DTT to maintain full activity and a concentration of about 8 mM is necessary for its maximum expression. Thiol inactiv...

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Guardado en:
Detalles Bibliográficos
Publicado: 1992
Materias:
porphobilinogen synthase
article
enzyme kinetics
nonhuman
ph
rhizobium
Bradyrhizobium japonicum
Rhizobium
Sinorhizobium meliloti
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v24_n11_p1841_DeBonis
http://hdl.handle.net/20.500.12110/paper_0020711X_v24_n11_p1841_DeBonis
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_0020711X_v24_n11_p1841_DeBonis
record_format dspace
spelling paper:paper_0020711X_v24_n11_p1841_DeBonis2023-06-08T14:41:13Z Delta-aminolevulinate dehydratase from free-living Rhizobium porphobilinogen synthase article enzyme kinetics nonhuman ph rhizobium Bradyrhizobium japonicum Rhizobium Sinorhizobium meliloti 1. 1. δ-Aminolevulinate-dehydratase (ALA-D) from Rhizobium japonicum and Rhizobium meliloti was isolated and some properties were studied. 2. 2. The enzyme from both strains require DTT to maintain full activity and a concentration of about 8 mM is necessary for its maximum expression. Thiol inactivating compounds and heavy metals ions such as Pb2+ and Cd2+ inactivate ALA-D. 3. 3. The enzyme exhibits Michaelis-Menten kinetics and has an apparent Km of 0.095 and 0.1-0.37 mM for Rhizobium japonicum and Rhizobium meliloti respectively. 4. 4. For both strains the pH profiles show a well denned maximum at about 7.2-7.6 and a second broad peak or shoulder in the range of pH 9-10. 5. 5. ALA-D from Rhizobium does not appear to be a heat stable enzyme as it happens to be in other sources. © 1992. 1992 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v24_n11_p1841_DeBonis http://hdl.handle.net/20.500.12110/paper_0020711X_v24_n11_p1841_DeBonis
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
article
enzyme kinetics
nonhuman
ph
rhizobium
Bradyrhizobium japonicum
Rhizobium
Sinorhizobium meliloti
spellingShingle porphobilinogen synthase
article
enzyme kinetics
nonhuman
ph
rhizobium
Bradyrhizobium japonicum
Rhizobium
Sinorhizobium meliloti
Delta-aminolevulinate dehydratase from free-living Rhizobium
topic_facet porphobilinogen synthase
article
enzyme kinetics
nonhuman
ph
rhizobium
Bradyrhizobium japonicum
Rhizobium
Sinorhizobium meliloti
description 1. 1. δ-Aminolevulinate-dehydratase (ALA-D) from Rhizobium japonicum and Rhizobium meliloti was isolated and some properties were studied. 2. 2. The enzyme from both strains require DTT to maintain full activity and a concentration of about 8 mM is necessary for its maximum expression. Thiol inactivating compounds and heavy metals ions such as Pb2+ and Cd2+ inactivate ALA-D. 3. 3. The enzyme exhibits Michaelis-Menten kinetics and has an apparent Km of 0.095 and 0.1-0.37 mM for Rhizobium japonicum and Rhizobium meliloti respectively. 4. 4. For both strains the pH profiles show a well denned maximum at about 7.2-7.6 and a second broad peak or shoulder in the range of pH 9-10. 5. 5. ALA-D from Rhizobium does not appear to be a heat stable enzyme as it happens to be in other sources. © 1992.
title Delta-aminolevulinate dehydratase from free-living Rhizobium
title_short Delta-aminolevulinate dehydratase from free-living Rhizobium
title_full Delta-aminolevulinate dehydratase from free-living Rhizobium
title_fullStr Delta-aminolevulinate dehydratase from free-living Rhizobium
title_full_unstemmed Delta-aminolevulinate dehydratase from free-living Rhizobium
title_sort delta-aminolevulinate dehydratase from free-living rhizobium
publishDate 1992
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v24_n11_p1841_DeBonis
http://hdl.handle.net/20.500.12110/paper_0020711X_v24_n11_p1841_DeBonis
_version_ 1768543452676489216

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