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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_0020711X_v19_n4_p373_Koopmann
Ver los metadatos del registro completo
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paperaa:paper_0020711X_v19_n4_p373_Koopmann |
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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 |