Biosynthesis of porphyrins in Rhodopseudomonas palustris-VI. The effect of metals, thiols and other reagents on the activity of uroporphyrinogen decarboxylase

Autores
Koopmann, G.E.; Del C. Batlle, A.M.
Año de publicación
1987
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
1. 1. The effect of several metals and reagents on the decarboxylation rate of uroporphyrinogen I by using a 16-fold purified preparation of Uroporphyrinogen Decarboxylase from Rhodopseudomonas palustris, was studied. 2. 2. 1 mM Hg2+ and Cu2+ were strong inhibitors, 1 mM Zn2+ and Fe2+ under certain conditions and 1 mM Fe3+ and Cr3+ also inactivated the enzyme, but Pb2+, Cd2+, and Al3+ did not. Metals inhibition was reversed by 1 mM GSH or CvSH. 3. 3. 0.1 mM DTNB and PCMB, 1 mM pyridoxal phosphate and 100 mM chloral hydrate, as well as 1 mM 2-methoxy-5-nitrotropone and 0.2 mM diethylpyrocarbonate inhibited Uroporphyrinogen Decarboxylase; while GSH, CySH, N-ethylmaleimide, sodium thioglycolate, 1,4-dithioerythritol, EDTA and O-phenantroline did not modify activity. 4. 4. Data obtained would indicate that one cysteine, one or two histidine residues and probably a lysine group are required for enzyme activity. © 1987.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Int. J. Biochem. 1987;19(4):373-377
Materia
4 chloromercuribenzoic acid
5,5' dithiobis(2 nitrobenzoic acid)
Carboxy Lyases
carboxylyase
copper
ferrous ion
mercury
metal
p Chloromercuribenzoic Acid
porphyrin
thiol derivative
uroporphyrinogen decarboxylase
zinc
article
biosynthesis
metabolism
Rhodopseudomonas
Carboxy-Lyases
Chloromercuribenzoates
Copper
Dithionitrobenzoic Acid
Ferrous Compounds
Mercury
Metals
p-Chloromercuribenzoic Acid
Porphyrins
Rhodopseudomonas
Sulfhydryl Compounds
Support, Non-U.S. Gov't
Uroporphyrinogen Decarboxylase
Zinc
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_0020711X_v19_n4_p373_Koopmann

id BDUBAFCEN_f468258b55228eff7dffe79c18c07067
oai_identifier_str paperaa:paper_0020711X_v19_n4_p373_Koopmann
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Biosynthesis of porphyrins in Rhodopseudomonas palustris-VI. The effect of metals, thiols and other reagents on the activity of uroporphyrinogen decarboxylaseKoopmann, G.E.Del C. Batlle, A.M.4 chloromercuribenzoic acid5,5' dithiobis(2 nitrobenzoic acid)Carboxy Lyasescarboxylyasecopperferrous ionmercurymetalp Chloromercuribenzoic Acidporphyrinthiol derivativeuroporphyrinogen decarboxylasezincarticlebiosynthesismetabolismRhodopseudomonasCarboxy-LyasesChloromercuribenzoatesCopperDithionitrobenzoic AcidFerrous CompoundsMercuryMetalsp-Chloromercuribenzoic AcidPorphyrinsRhodopseudomonasSulfhydryl CompoundsSupport, Non-U.S. Gov'tUroporphyrinogen DecarboxylaseZinc1. 1. The effect of several metals and reagents on the decarboxylation rate of uroporphyrinogen I by using a 16-fold purified preparation of Uroporphyrinogen Decarboxylase from Rhodopseudomonas palustris, was studied. 2. 2. 1 mM Hg2+ and Cu2+ were strong inhibitors, 1 mM Zn2+ and Fe2+ under certain conditions and 1 mM Fe3+ and Cr3+ also inactivated the enzyme, but Pb2+, Cd2+, and Al3+ did not. Metals inhibition was reversed by 1 mM GSH or CvSH. 3. 3. 0.1 mM DTNB and PCMB, 1 mM pyridoxal phosphate and 100 mM chloral hydrate, as well as 1 mM 2-methoxy-5-nitrotropone and 0.2 mM diethylpyrocarbonate inhibited Uroporphyrinogen Decarboxylase; while GSH, CySH, N-ethylmaleimide, sodium thioglycolate, 1,4-dithioerythritol, EDTA and O-phenantroline did not modify activity. 4. 4. Data obtained would indicate that one cysteine, one or two histidine residues and probably a lysine group are required for enzyme activity. © 1987.Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1987info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p373_KoopmannInt. J. Biochem. 1987;19(4):373-377reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:42:55Zpaperaa:paper_0020711X_v19_n4_p373_KoopmannInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:42:56.23Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Biosynthesis of porphyrins in Rhodopseudomonas palustris-VI. The effect of metals, thiols and other reagents on the activity of uroporphyrinogen decarboxylase
title Biosynthesis of porphyrins in Rhodopseudomonas palustris-VI. The effect of metals, thiols and other reagents on the activity of uroporphyrinogen decarboxylase
spellingShingle Biosynthesis of porphyrins in Rhodopseudomonas palustris-VI. The effect of metals, thiols and other reagents on the activity of uroporphyrinogen decarboxylase
Koopmann, G.E.
4 chloromercuribenzoic acid
5,5' dithiobis(2 nitrobenzoic acid)
Carboxy Lyases
carboxylyase
copper
ferrous ion
mercury
metal
p Chloromercuribenzoic Acid
porphyrin
thiol derivative
uroporphyrinogen decarboxylase
zinc
article
biosynthesis
metabolism
Rhodopseudomonas
Carboxy-Lyases
Chloromercuribenzoates
Copper
Dithionitrobenzoic Acid
Ferrous Compounds
Mercury
Metals
p-Chloromercuribenzoic Acid
Porphyrins
Rhodopseudomonas
Sulfhydryl Compounds
Support, Non-U.S. Gov't
Uroporphyrinogen Decarboxylase
Zinc
title_short Biosynthesis of porphyrins in Rhodopseudomonas palustris-VI. The effect of metals, thiols and other reagents on the activity of uroporphyrinogen decarboxylase
title_full Biosynthesis of porphyrins in Rhodopseudomonas palustris-VI. The effect of metals, thiols and other reagents on the activity of uroporphyrinogen decarboxylase
title_fullStr Biosynthesis of porphyrins in Rhodopseudomonas palustris-VI. The effect of metals, thiols and other reagents on the activity of uroporphyrinogen decarboxylase
title_full_unstemmed Biosynthesis of porphyrins in Rhodopseudomonas palustris-VI. The effect of metals, thiols and other reagents on the activity of uroporphyrinogen decarboxylase
title_sort Biosynthesis of porphyrins in Rhodopseudomonas palustris-VI. The effect of metals, thiols and other reagents on the activity of uroporphyrinogen decarboxylase
dc.creator.none.fl_str_mv Koopmann, G.E.
Del C. Batlle, A.M.
author Koopmann, G.E.
author_facet Koopmann, G.E.
Del C. Batlle, A.M.
author_role author
author2 Del C. Batlle, A.M.
author2_role author
dc.subject.none.fl_str_mv 4 chloromercuribenzoic acid
5,5' dithiobis(2 nitrobenzoic acid)
Carboxy Lyases
carboxylyase
copper
ferrous ion
mercury
metal
p Chloromercuribenzoic Acid
porphyrin
thiol derivative
uroporphyrinogen decarboxylase
zinc
article
biosynthesis
metabolism
Rhodopseudomonas
Carboxy-Lyases
Chloromercuribenzoates
Copper
Dithionitrobenzoic Acid
Ferrous Compounds
Mercury
Metals
p-Chloromercuribenzoic Acid
Porphyrins
Rhodopseudomonas
Sulfhydryl Compounds
Support, Non-U.S. Gov't
Uroporphyrinogen Decarboxylase
Zinc
topic 4 chloromercuribenzoic acid
5,5' dithiobis(2 nitrobenzoic acid)
Carboxy Lyases
carboxylyase
copper
ferrous ion
mercury
metal
p Chloromercuribenzoic Acid
porphyrin
thiol derivative
uroporphyrinogen decarboxylase
zinc
article
biosynthesis
metabolism
Rhodopseudomonas
Carboxy-Lyases
Chloromercuribenzoates
Copper
Dithionitrobenzoic Acid
Ferrous Compounds
Mercury
Metals
p-Chloromercuribenzoic Acid
Porphyrins
Rhodopseudomonas
Sulfhydryl Compounds
Support, Non-U.S. Gov't
Uroporphyrinogen Decarboxylase
Zinc
dc.description.none.fl_txt_mv 1. 1. The effect of several metals and reagents on the decarboxylation rate of uroporphyrinogen I by using a 16-fold purified preparation of Uroporphyrinogen Decarboxylase from Rhodopseudomonas palustris, was studied. 2. 2. 1 mM Hg2+ and Cu2+ were strong inhibitors, 1 mM Zn2+ and Fe2+ under certain conditions and 1 mM Fe3+ and Cr3+ also inactivated the enzyme, but Pb2+, Cd2+, and Al3+ did not. Metals inhibition was reversed by 1 mM GSH or CvSH. 3. 3. 0.1 mM DTNB and PCMB, 1 mM pyridoxal phosphate and 100 mM chloral hydrate, as well as 1 mM 2-methoxy-5-nitrotropone and 0.2 mM diethylpyrocarbonate inhibited Uroporphyrinogen Decarboxylase; while GSH, CySH, N-ethylmaleimide, sodium thioglycolate, 1,4-dithioerythritol, EDTA and O-phenantroline did not modify activity. 4. 4. Data obtained would indicate that one cysteine, one or two histidine residues and probably a lysine group are required for enzyme activity. © 1987.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description 1. 1. The effect of several metals and reagents on the decarboxylation rate of uroporphyrinogen I by using a 16-fold purified preparation of Uroporphyrinogen Decarboxylase from Rhodopseudomonas palustris, was studied. 2. 2. 1 mM Hg2+ and Cu2+ were strong inhibitors, 1 mM Zn2+ and Fe2+ under certain conditions and 1 mM Fe3+ and Cr3+ also inactivated the enzyme, but Pb2+, Cd2+, and Al3+ did not. Metals inhibition was reversed by 1 mM GSH or CvSH. 3. 3. 0.1 mM DTNB and PCMB, 1 mM pyridoxal phosphate and 100 mM chloral hydrate, as well as 1 mM 2-methoxy-5-nitrotropone and 0.2 mM diethylpyrocarbonate inhibited Uroporphyrinogen Decarboxylase; while GSH, CySH, N-ethylmaleimide, sodium thioglycolate, 1,4-dithioerythritol, EDTA and O-phenantroline did not modify activity. 4. 4. Data obtained would indicate that one cysteine, one or two histidine residues and probably a lysine group are required for enzyme activity. © 1987.
publishDate 1987
dc.date.none.fl_str_mv 1987
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p373_Koopmann
url http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p373_Koopmann
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Int. J. Biochem. 1987;19(4):373-377
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
_version_ 1844618735130771456
score 13.070432