Suicide inactivation in adenosylcobalamin-dependent enzymes
Date
2006
Authors
Sandala, Gregory
Journal Title
Journal ISSN
Volume Title
Publisher
CSIRO Publishing
Abstract
Adenosylcobalamin (AdoCbl) dependent enzymes exploit organic radicals for rearrangement of adjacent groups. Their dependence on radicals for catalysis results in the possibility of irreversible inactivation. An allylic analogue of AdoCbl has been synthesized and its corresponding activity assessed with AdoCbl-dependent diol dehydratase (DDH). Suicide inactivation of Ethanolamine ammonia lyase (EAL), an AdoCbl-dependent enzyme that catalyses the irreversible deamination of vicinal amino alcohols to produce their corresponding aldehydes, by substrate analoguehydroxyethylhydrazine (HEH) has been postulated to result from the failure of Adȯ to be regenerated due to inability of the hydrazinium radical cation to capture a hydrogen atom from Ado-H.
Description
Keywords
Keywords: Aldehydes; Catalysis; Enzymes; Hydrogen; Positive ions; Adenosylcobalamin-dependent enzymes; AdoCbl-dependent diol dehydratase (DDH); Analoguehydroxyethylhydrazine (HEH); Ethanolamine ammonia lyase (EAL); Enzyme kinetics
Citation
Collections
Source
Australian Journal of Chemistry
Type
Journal article
Book Title
Entity type
Access Statement
License Rights
DOI
Restricted until
2037-12-31
Downloads
File
Description