Regulation of the lysine biosynthesis in Pichia guilliermondii.
The regulatory properties of four enzymes (homocitrate synthase, alpha-aminoadipate reductase, saccharopine reductase, saccharopine dehydrogenase) involved in the lysine biosynthesis of Pichia guilliermondii were investigated and compared with the regulatory patterns found in other yeast species. The first enzyme of the pathway, homocitrate synthase, is feedback-inhibited by L-lysine. Some other amino acids (alpha-aminoadipate, glutamate, tryptophan, leucine) and lysine analogues are also inhibitors of one or more enzymes. It is shown that only the synthesis of homocitrate synthase is weakly repressed by L-lysine.
Schmidt
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Sektion Biologie, Ernst-Moritz-Arndt-Universität Greifswald, GDR.
Bode
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Birnbaum
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D000445:Aldehyde Oxidoreductases / Q000096:biosynthesis; D000494:Allosteric Regulation; D002850:Chromatography, Gel; D050647:L-Aminoadipate-Semialdehyde Dehydrogenase; D008239:Lysine / Q000096:biosynthesis*; D007652:Oxo-Acid-Lyases / Q000096:biosynthesis; D010843:Pichia / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D004718:Saccharomycetales / Q000201:enzymology*; D012443:Saccharopine Dehydrogenases / Q000096:biosynthesis
D000445:Aldehyde Oxidoreductases; D050647:L-Aminoadipate-Semialdehyde Dehydrogenase; D012443:Saccharopine Dehydrogenases; C021365:homocitrate synthase; D007652:Oxo-Acid-Lyases; D008239:Lysine