Glycine decarboxylase in Rhodopseudomonas spheroides and in rat liver mitochondria

1. Glycine decarboxylase and glycine-bicarbonate exchange activities were detected in extracts of Rhodopseudomonas spheroides and in rat liver mitochondria and their properties were studied. 2. The glycine decarboxylase activity from both sources is stimulated when glyoxylate is added to the assay s...

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Bibliographic Details
Published in:Biochemical journal 1970-08, Vol.118 (5), p.819-830
Main Author: Tait, G H
Format: Article
Language:English
Subjects:
Alcohol Oxidoreductases - analysis
Animals
Bicarbonates - metabolism
Carbon Isotopes
Carboxy-Lyases - analysis
Culture Media
Enzyme Induction
Glycine - metabolism
Glyoxylates - pharmacology
L-Serine Dehydratase - analysis
Mitochondria, Liver - enzymology
Oxidoreductases - analysis
Rats
Rhodopseudomonas - enzymology
Transferases - analysis
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Summary:1. Glycine decarboxylase and glycine-bicarbonate exchange activities were detected in extracts of Rhodopseudomonas spheroides and in rat liver mitochondria and their properties were studied. 2. The glycine decarboxylase activity from both sources is stimulated when glyoxylate is added to the assay system. 3. Several proteins participate in these reactions and a heat-stable low-molecular-weight protein was purified from both sources. 4. These enzyme activities increase markedly when R. spheroides is grown in the presence of glycine, glyoxylate, glycollate, oxalate or serine. 5. All the enzymes required to catalyse the conversion of glycine into acetyl-CoA via serine and pyruvate were detected in extracts of R. spheroides; of these glycine decarboxylase has the lowest activity. 6. The increase in the activity of glycine decarboxylase on illumination of R. spheroides in a medium containing glycine, and the greater increase when ATP is also present in the medium, probably accounts for the increased incorporation of the methylene carbon atom of glycine into fatty acids found previously under these conditions (Gajdos, Gajdos-Török, Gorchein, Neuberger & Tait, 1968). 7. The results are compared with those obtained by other workers on the glycine decarboxylase and glycine-bicarbonate exchange activities in other systems.
ISSN:0264-6021
0306-3283
1470-8728
DOI:10.1042/bj1180819