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PMID: 6975621 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides.

The Biochemical journal ·Vol. 195 ·No. 1 ·1981-04-01 ·Pages 177-81

Jordan PM, Berry A

Abstract

Highly stable labelled complexes are formed between porphobilinogen deaminase and stoicheiometric amounts of [14C]porphobilinogen. On completion of the catalytic cycle by the addition of excess of substrate, the complexes yield labelled product and display all the properties expected from covalently bound enzyme intermediates involved in the deaminase catalytic sequence.

MeSH Terms
Ammonia-Lyases/metabolism Chemical Phenomena Chemistry Chromatography, Gel Hydroxylamines/pharmacology Hydroxymethylbilane Synthase/metabolism Macromolecular Substances Porphobilinogen/metabolism,pharmacology Pyrroles/pharmacology Rhodobacter sphaeroides/enzymology Sodium Dodecyl Sulfate/pharmacology
Chemicals
Hydroxylamines Macromolecular Substances Pyrroles Sodium Dodecyl Sulfate Porphobilinogen Hydroxymethylbilane Synthase Ammonia-Lyases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Jordan P M
Berry A
References (13)
13 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1981-04-01
Pages
177-81
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1162869
Subset
IM
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