Saccharopine: an Intermediate of L-Lysine Biosynthesis and Degradation in Pyricularia oryzae

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Biosynthesis and degradation of saccharopine, an intermediate of lysine metabolism.

Lysine-2-oxoglutarate reductase was prepared from ox liver and its characteristics were examined. Its activity was totally inhibited in the presence of NH(4)Cl. Under conditions that inhibit saccharopine formation, and in the presence of NADP(+), ox liver mitochondria were found to catalyse the hydrolysis of saccharopine to lysine and alpha-oxoglutarate. The enzyme involved was named saccharopi...

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Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase.

Two pathways of lysine biosynthesis are known to exist in nature. The diaminopimelic acid pathway, studied in detail in Escherichia coli (l), is the route of lysine biosynthesis in bacteria, certain lower fungi, algae, and higher plants (2). In other classes of lower fungi, in higher fungi, and in Euglena, lysine is synthesized in a different manner, involving the intermediate cu-aminoadipic ac...

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Saccharopine, an Intermediate of the Aminoadipic Acid Pathway of Lysine Biosynthesis. Ii. Studies in Saccharomyces Cereviseae.

Previous studies with wild yeast strains (Torulopsis utilis and Saccharomyces cerevisiae) have provided circumstantial evidence for the involvement of oc-aminoadipic-6-semialdehyde (1, 2) and saccharopine (3) in lysine biosynthesis from or-aminoadipic acid. Evidence drawn from appropriat’e nutrit.ional studies, accumulation of aminoadipic acid metabolites, and enzymatic analysis with a series o...

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Saccharopine, an Intermediate of the Aminoadipic Acid Pathway of Lysine Biosynthesis*

Two pathways of lysine biosynthesis are known to exist in nature. The diaminopimelic acid pathway, studied in detail in Escherichia coli (l), is the route of lysine biosynthesis in bacteria, certain lower fungi, algae, and higher plants (2). In other classes of lower fungi, in higher fungi, and in Euglena, lysine is synthesized in a different manner, involving the intermediate cu-aminoadipic ac...

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The reaction of pyridoxal 5'-phosphate with an essential lysine residue of saccharopine dehydrogenase (L-lysine-forming).

Saccharopine dehydrogenase (EC 1.5.1.7) from bakers’ yeast was reversibly inactivated by pyridoxal and pyridoxal 5’-phosphate. The inactivation by pyridoxal 5’-phosphate was accompanied by the appearance of a peak at 428 nm, which was shifted to 325 nm upon reduction with NaBH4. Paper chromatography of an acid hydrolysate of the pyridoxal 5’-phosphate-treated, NaBH4-reduced enzyme showed the pr...

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ژورنال

عنوان ژورنال: Microbiology

سال: 1980

ISSN: 1350-0872,1465-2080

DOI: 10.1099/00221287-120-1-11