Ethanolamine Deaminase, a Cobamide Coenzyme-dependent Enzyme
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چکیده
منابع مشابه
Purification and properties of dioldehydrase, and enzyme requiring a cobamide coenzyme.
The conversion of propanediol to propionaldehyde and ethylene glycol to acetaldehyde has been shown to occur in crude extracts of A erobacter aerogenes (ATCC 8724) (I), and the requirement of a cobamide coenzyme has been demonstrated. Subsequently, several similar reactions which also require a cobamide coenzyme were reported. Extracts of Lactobacillus (2) carry out the conversion of glycerol t...
متن کاملDemonstration of cobamide coenzyme in Ascaris suum.
I. Cobamide coenzyme was extracted from the body wall of adult female Ascaris suum maintained in Ellison's medium containing vitamin B11• 2. The identification of the coenzyme in purified fractions was based on (a) specific spectral changes following treatment of the preparation with light and cyanide, (b) coenzyme activity in the glutamate mutase reaction and (c) inactivation of the coenzyme a...
متن کاملLysine fermentation to fatty acids and ammonia: a cobamide coenzyme-dependent process.
This is a balanced oxidation-reduction process and, as judged by isotope experiments, differs from the established pathways of lysine degradation occurring in animals, Neurospora, and certain bacteria. Numerous technical problems encountered in attempts to study the reaction in cell-free extracts of C. sticklundii prompted us to isolate a new Clostridiumr from soil enrichment cultures containin...
متن کاملStudies on the mechanism of hydrogen transfer in the cobamide coenzyme-dependent dioldehydrase reaction.
When dl-1 ,2-propanediol-l-3H is converted to propionaldehyde in the presence of dioldehydrase and cobamide coenzyme, tritium is transferred to the coenzyme. The tritiated coenzyme so obtained transfers tritium to the reaction product when reacted with dl-1,2-propanediol and apoenzyme. The coenzyme is tritiated exclusively at the C-5’ position of the adenosyl moiety. The location of tritium was...
متن کاملMicrobial Metabolism of Amino Alcohols
1. Kinetic studies of ethanolamine ammonia-lyase formation by Escherichia coli suggested that coenzyme B12 (5'-deoxyadenosylcobalamin), with ethanolamine, is a co-inducer. 2. Enzymic and immunological tests failed to show the formation of complementary enzyme components induced separately by ethanolamine and cobalamin respectively. 3. Although specific for ethanolamine as the substrate, enzyme ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)93512-x