(Q28611254)

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Tryptophan degradation in Saccharomyces cerevisiae: characterization of two aromatic aminotransferases

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3 February 2017

Tryptophan degradation in Saccharomyces cerevisiae: characterization of two aromatic aminotransferases (English)

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3 February 2017

Saccharomyces cerevisiae

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3

R. Hütter

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3 February 2017

2

P. Niederberger

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3 February 2017

P. Kradolfer

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3 February 2017

language of work or name

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11 December 1982

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3 February 2017

Archives of Microbiology

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133

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3

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242–248

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Distinct kynureninase and hydroxykynureninase activities in microorganisms: occurrence and properties of a single physiologically discrete enzyme in yeast.

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PubMed

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12 December 2020

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Metabolic products of microorganisms. 91. Tryptanthrin, a tryptophan derived antibiotic from Candida lipolytica

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12 December 2020

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Permeabilization of microorganisms by Triton X-100

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12 December 2020

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Regulation of tryptophan biosynthesis in Saccharomyces cerevisiae: mode of action of 5-methyl-tryptophan and 5-methyl-tryptophan-sensitive mutants.

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Optimal conditions for selecting specific auxotrophs of Saccharomyces cerevisiae using temperature-sensitive suicide mutants

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Tryptophan biosynthesis in Saccharomyces cerevisiae: control of the flux through the pathway

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Biological role of the general control of amino acid biosynthesis in Saccharomyces cerevisiae

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[Regulation of the biosynthesis of aromatic amino acids in Saccharomyces cerevisiae. 2. Repression, induction and activation]

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12 December 2020

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Determination of tryptophan by manually operated and Autoanalyzer methods based on the formation of norharman

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12 December 2020

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Free tryptophan pool and tryptophan biosynthetic enzymes in Saccharomyces cerevisiae

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12 December 2020

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[On the regulation of nicotinic acid biosynthesis in Saccharomyces cerevisiae]

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12 December 2020

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Protein measurement with the Folin phenol reagent

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12 December 2020

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Identifiers

DOI

10.1007/BF00415010

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3 February 2017

Springer Nature article ID

10.1007/bf00415010

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(Q28611254)

Tryptophan degradation in Saccharomyces cerevisiae: characterization of two aromatic aminotransferases

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