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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Autores principales: De Bonis, A.F., Rossetti, M.V., Del C. Batlle, A.M.
Formato: JOUR
Materias:
porphobilinogen synthase
article
enzyme kinetics
nonhuman
ph
rhizobium
Bradyrhizobium japonicum
Rhizobium
Sinorhizobium meliloti
Acceso en línea: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 todo:paper_0020711X_v24_n11_p1841_DeBonis
record_format dspace
spelling todo:paper_0020711X_v24_n11_p1841_DeBonis2023-10-03T14:18:07Z Delta-aminolevulinate dehydratase from free-living Rhizobium De Bonis, A.F. Rossetti, M.V. Del C. Batlle, A.M. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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
De Bonis, A.F.
Rossetti, M.V.
Del C. Batlle, A.M.
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.
format JOUR
author De Bonis, A.F.
Rossetti, M.V.
Del C. Batlle, A.M.
author_facet De Bonis, A.F.
Rossetti, M.V.
Del C. Batlle, A.M.
author_sort De Bonis, A.F.
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
url http://hdl.handle.net/20.500.12110/paper_0020711X_v24_n11_p1841_DeBonis
work_keys_str_mv AT debonisaf deltaaminolevulinatedehydratasefromfreelivingrhizobium
AT rossettimv deltaaminolevulinatedehydratasefromfreelivingrhizobium
AT delcbatlleam deltaaminolevulinatedehydratasefromfreelivingrhizobium
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