A glutamic-α-ketoadipic transaminase in saccharomyces

Piediscalzi, Nicholas; Fjellstedt, Thorsten A.; Ogur, Maurice

doi:10.1016/0006-291x(68)90671-2

Cited by 8 publications

(3 citation statements)

References 3 publications

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“…Aminotransferase activity has been identified in Torulopsis utilis, N. crassa, S. cerevisiae and a S. cerevisiae threonine auxotroph, thr5. 30,31 The majority of information on this step comes from early studies conducted by Matsuda and Ogur in S. cerevisiae. 32,33 The aminoadipate aminotransferase activity is associated with two isozymes that are separable by ion exchange and size exclusion column chromatography.…”

Section: A-aminoadipate Aminotransferasementioning

confidence: 99%

Lysine biosynthesis and metabolism in fungi

Zabriskie¹,

Jackson²

2000

Nat. Prod. Rep.

152

120

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Introduction: lysine biosynthesis 1.1 The a-aminoadipate pathway to l-lysine 2 Enzymes of the a-aminoadipate pathway 2.1 Homocitrate synthase 2.2 Homoaconitate hydratase 2.3 Homoisocitrate dehydrogenase 2.4 a-Aminoadipate aminotransferase 2.5 a-Aminoadipate reductase 2.6 Saccharopine reductase 2.7 Saccharopine dehydrogenase 3 Role of pipecolic acid in lysine biosynthesis 4 Lysine catabolism 5 Role of a-aminoadipate pathway intermediates in secondary metabolism 6 The a-aminoadipate pathway in archaea and bacteria 7 Conclusion 8 Acknowledgements 9 References

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Section: A-aminoadipate Aminotransferasementioning

confidence: 99%

Lysine biosynthesis and metabolism in fungi

Zabriskie¹,

Jackson²

2000

Nat. Prod. Rep.

152

120

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“…L-a-Aminoadipate aminotransferase activity has been identified in S. cerevisiae and Torulopsis utilis. 133,134 In S. cerevisiae, two isozymes were isolated. 135,136 Isozyme I is localised in the mitochondria, while isozyme II is localised in cytosol.…”

Section: Classical Dap Pathwaymentioning

confidence: 99%

Convergent strategies in biosynthesis

et al. 2011

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“…Incubation of enzyme preparations with radioactive substrates. Enzymatic conversion of either labeled a-AAA or labeled lysine to saccharopine was studied by adapting a system previously described (18).…”

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confidence: 99%

Effects of Supersuppressor Genes on Enzymes Controlling Lysine Biosynthesis in Saccharomyces

Fjellstedt

Ogur

1970

J Bacteriol

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Yeast supersuppressor genes capable of masking the effects of several lysine mutant genes (lyl1l, lyg..ily,I1) were studied with respect to their effects on the respective enzymes (saccharopine dehydrogenase, saccharopine reductase, and a-aminoadipic acid reductase). In all strains tested, the supersuppressors functioned by allowing enzyme synthesis not found in the unsuppressed mutant. Studies by optical methods of saccharopine dehydrogenase and saccharopine reductase extracted from suppressed ly1 l and lyg-l cells, respectively, revealed that the Km values for these enzymes were significantly greater than those found in wild type. Saccharopine dehydrogenase from suppressed IY9-l cells was found to have K,, values similar to wild type. These findings are consistent with the inference that a supersuppressor may act by enabling nonsense codons to be read, producing altered enzyme protein. Recent findings that lysine degradation in mammals may involve saccharopine and that the human diseases, hyperlysinemia and saccharopinuria, may be due to metabolic blocks in this route of lysine degradation suggest the ly1 l and lyg9l yeast mutants as models for the human condition and its possible euphenic treatment.

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A glutamic-α-ketoadipic transaminase in saccharomyces

Cited by 8 publications

References 3 publications

Lysine biosynthesis and metabolism in fungi

Lysine biosynthesis and metabolism in fungi

Convergent strategies in biosynthesis

Effects of Supersuppressor Genes on Enzymes Controlling Lysine Biosynthesis in Saccharomyces

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