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Volume 138, Issue 11

Purification and characterization of a dual function 3-dehydroquinate dehydratase from Free

Abstract

Studies on hydroaromatic metabolism in the actinomycete revealed that the organism grows rapidly on quinate (but not on shikimate) as sole carbon- and energy source. Quinate is initially converted into the shikimate pathway intermediate 3-dehydroquinate by an inducible NAD-dependent quinate/shikimate dehydrogenase. 3-Dehydroquinate dehydratase subsequently converts 3-dehydroquinate into 3-dehydroshikimate, which is used partly for the biosynthesis of aromatic amino acids, and is partly catabolized via protocatechuate and the β-ketoadipate pathway. Enzyme studies and analysis of mutants clearly showed that the single 3-dehydroquinate dehydratase present in has a dual function, the first example of a 3-dehydroquinate dehydratase enzyme involved in both the catabolism of quinate and the biosynthesis of aromatic amino acids. This enzyme was purified over 1700-fold to homogeneity. Its further characterization indicated that it is a Type II 3-dehydroquinate dehydratase, a thermostable enzyme with a large oligomeric structure (native 135 × 10) and a subunit of 12 × 10. Characterization of aromatic amino acid auxotrophic mutants of suggested that genes encoding 3-dehydroquinate synthase and 3-dehydroquinate dehydratase are genetically linked but their transcription results in the synthesis of two separate proteins.

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© Society for General Microbiology, 1992
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1992-11-01
2025-05-13
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/content/journal/micro/10.1099/00221287-138-11-2449
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Purification and characterization of a dual function 3-dehydroquinate dehydratase from Amycolatopsis methanolica
Microbiology 138, 2449 (1992); https://doi.org/10.1099/00221287-138-11-2449
/content/journal/micro/10.1099/00221287-138-11-2449
/content/journal/micro/10.1099/00221287-138-11-2449
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