Microbial growth on C1 compounds. 5. Enzyme activities in extracts of Pseudomonas AM1
- 1 May 1963
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 87 (2) , 386-396
- https://doi.org/10.1042/bj0870386
Abstract
Tetrahydrofolate formylase, methylene-tetrahydrofolate dehydrogenase, serine hydroxy-methyltransferase, glycerate dehydrogenase, glyoxylate reductase, malate synthase, citrate synthase, isocitrate dehydrogenase and malate dehydrogenase are found in extracts of methanol-, formate-and succinate-grown Pseudomonas AM 1. No glyoxylate carboligase, isocitrate lyase or malate dehydrogenase (decarboxylating) could be detected. Transamination of serine with [alpha]-oxoglutarate and pyruvate was observed. Cell-free extracts with suitable cofactors, catalyze the conversion of formate and glycine to serine and glycerate. Extracts catalyze phosphorylation of glycerate to phosphoglycerate in the presence of ATP. Enzyme activity is higher in methanol- or formate-grown cells than in the succinate-grown cells.This publication has 43 references indexed in Scilit:
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