A malate dehydrogenase (MDH) was characterized from the cyanobacterium Coccochloris penio-cyst&. The enzyme was purified approximately 180-fold and had a molecular weight of about 90 000. The enzyme had a pH optimum of pH 6.7 to 7.5; a Km (malate) of 5.6 mM and Kms for NAD and NADP of 24 gM and 178g
Formation and metabolism of glycolate in the cyanobacteriumCoccochloris peniocystis
β Scribed by Eric G. Norman; Brian Colman
- Publisher
- Springer
- Year
- 1992
- Tongue
- English
- Weight
- 691 KB
- Volume
- 157
- Category
- Article
- ISSN
- 0302-8933
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The rate of glycolate excretion by Coccochloris peniocystis Kiitz. cells incubated under conditions of low bicarbonate concentration and high light intensity was linear for only the initial 15 rain of incubation and no additional glycolate accumulated in the medium after 20 rain. Excretion was maxim
The linked utilization of glycollate and L-serine has been studied in peroxisomal preparations from leaves of spinach beet (Beta vulgaris L.). The generation of glycine from glycollate was found to be balanced by the production of hydroxypyruvate from serine and similarly by 2-oxoglutarate when L-gl
Suspensions of Chlorella vulgaris were allowed to photosynthesise with two concentrations of (14)CO2 (101 and 543 ppm) in 80% oxygen, and the incorporation of (14)C into glycolate and 3-phosphoglyceric acid (3-PGA) was followed. The relative specific activity (RSA) of the glycolate formed at both CO
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