Glycolate Pathway in Algae
نویسندگان
چکیده
منابع مشابه
Glycolate pathway in algae.
No glycolate oxidase activity could be detected by manometric, isotopic, or spectrophotometric techniques in cell extracts from 5 strains of algae grown in the light with CO(2). However, NADH:glyoxylate reductase, phosphoglycolate phosphatase and isocitrate dehydrogenase were detected in the cell extracts. The serine formed by Chlorella or Chlamydomonas after 12 seconds of photosynthetic (14)CO...
متن کاملGlycolate oxidase activity in algae.
The g1lycolate oxidase reactioni by x-hich gly colate is oxidized to glyoxylate (3, 10) is catailyzed by a flavoprotein (18) th,at is widely distributed in higher plants (12) and fungi (4). Its presence is g,elleralllly assumed in all phoiosynithetic tissuies, since glycolate is an early product of photosynthesis (14), yet this substrate is tusually found in oiily minute amounits. The oxidation...
متن کاملEffect of glycidate, an inhibitor of glycolate synthesis in leaves, on the activity of some enzymes of the glycolate pathway.
Under conditions where glycolate synthesis was inhibited at least 50% in tobacco (Nicotiana tabacum L.) leaf discs treated with glycidate (2,3-epoxypropionate), the ribulose diphosphate carboxylase activity in extracts and the inhibition of the activity by 100% oxygen were unaffected by the glycidate treatment. [1-(14)C]Glycidate was readily taken into leaf discs and was bound to leaf proteins,...
متن کاملMetabolic engineering of a xylose pathway for biotechnological production of glycolate in Escherichia coli
BACKGROUND Glycolate is a valuable chemical with extensive applications in many different fields. The traditional methods to synthesize glycolate are quite expensive and toxic. So, the biotechnological production of glycolate from sustainable feedstocks is of interest for its potential economic and environmental advantages. D-Xylose is the second most abundant sugar in nature and accounts for 1...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1967
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.42.3.371