Die Synthese der 5‐Dehydro‐chinasäure

Grewe, Rudolf; Jesehke, Jürgen‐Peter

doi:10.1002/cber.19560890908

Cited by 46 publications

(21 citation statements)

References 13 publications

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“…2) The chemical aromatization of amino-DHS by acid, base, or buffer treatment proceeds in the same way as that of DHS (61,62), i.e. it produces exclusively protocatechuic acid (63).…”

Section: Discussionmentioning

confidence: 99%

3-Amino-5-hydroxybenzoic Acid Synthase, the Terminal Enzyme in the Formation of the Precursor of mC7N Units in Rifamycin and Related Antibiotics

Kim

Fryhle

et al. 1998

Journal of Biological Chemistry

112

116

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The biosynthesis of ansamycin antibiotics, like rifamycin B, involves formation of 3-amino-5-hydroxybenzoic acid (AHBA) by a novel variant of the shikimate pathway. AHBA then serves as the starter unit for the assembly of a polyketide which eventually links back to the amino group of AHBA to form the macrolactam ring. The terminal enzyme of AHBA formation, which catalyzes the aromatization of 5-deoxy-5-amino-3-dehydroshikimic acid, has been purified to homogeneity from Amycolatopsis mediterranei, the encoding gene has been cloned, sequenced, and overexpressed in Escherichia coli. The recombinant enzyme, a (His) 6 fusion protein, as well as the native one, are dimers containing one molecule of pyridoxal phosphate per subunit. Mechanistic studies showed that the enzyme-bound pyridoxal phosphate forms a Schiff's base with the amino group of 5-deoxy-5-amino-3-dehydroshikimic acid and catalyzes both an ␣,␤-dehydration and a stereospecific 1,4-enolization of the substrate. Inactivation of the gene encoding AHBA synthase in the A. mediterranei genome results in loss of rifamycin formation; production of the antibiotic is restored when the mutant is supplemented with AHBA.

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“…2) The chemical aromatization of amino-DHS by acid, base, or buffer treatment proceeds in the same way as that of DHS (61,62), i.e. it produces exclusively protocatechuic acid (63).…”

Section: Discussionmentioning

confidence: 99%

3-Amino-5-hydroxybenzoic Acid Synthase, the Terminal Enzyme in the Formation of the Precursor of mC7N Units in Rifamycin and Related Antibiotics

Kim

Fryhle

et al. 1998

Journal of Biological Chemistry

112

116

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“…A preliminary report of this work was presented at the international symposium "The Biochemistry of Plant Phenolics" of the Phytochemical Society of Europe, Ghent (Belgium), August 28 to 31, 1984. 2Abbreviations: SORase, shikimate oxidoreductase (EC 1. (14). The materials used for gelelectrophoresis and isoelectric focusing were purchased from Serva (Heidelberg, F.R.G.…”

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confidence: 99%

Localization, Purification, and Characterization of Shikimate Oxidoreductase-Dehydroquinate Hydrolyase from Stroma of Spinach Chloroplasts

Fiedler

Schultz²

1985

Plant Physiol.

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The stroma of chloroplasts is probably the sole site of the shikimate pathway enzymes shikimate oxidoreductase/dehydroquinate hydrolyase (SORase/DHQase) in spinach leaves. (a) The (Fig. 1). We have used an essentially different approach to provide evidence that-in spinach leaves-two crucial enzymic activities SORase and DHQase of the shikimate pathway are restricted to the soluble chloroplast extract. It was proposed that the activities of SORase and DHQase in higher plants were on a single polypeptide (20). This bifunctional protein catalyzes the conversion ofdehydroquinate into dehydroshikimate(DHQase activity) and sequentially the synthesis of shikimate from dehydroshikimate (SORase activity). The two enzymic activities were found exclusively in the stroma ofspinach chloroplasts as demonstrated in this paper and the preceding abstract (13). To understand the structural/functional relationships ofthe multiple forms requires the ability to isolate them in a purified state.We have improved the previously reported purification procedure (12) to achieve the apparent homogeneity and stability which was necessary for the characterization of SORase/ DHQase. The purification procedure of a shikimate pathway enzyme from the chloroplast stroma is described here for the first time. Furthermore we investigated the regulatory properties of these enzymes.

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“…The deprotection and hydrolysis steps were carefully monitored by thin layer chromatography, because prolonged exposure of the dehydroquinates 4 and 5 to strongly acidic or basic conditions readily led to the elimination of the hydroxyl group at C-1 to form dehydroshikimate, which is susceptible to aromatization. [7] In conclusion, we report a convenient and reproducible method for the preparation of dehydroquinic acid 6 and its corresponding methyl ester 4. 1).…”

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confidence: 87%

“…[2,3] Therefore, a convenient synthetic source of dehydroquinic acid 6, and its corresponding methyl ester 4, is required for use in enzyme inhibition assays [3] and to provide convenient starting materials for the preparation of new inhibitors. Literature methods for the synthesis of dehydroquinic acid, notably oxidation of quinic acid 1 using a platinum-oxygen system [5,6] or nitric acid, [7,8] are difficult to reproduce, invariably require tedious purification, and afford the desired acid in variable yield. Literature methods for the synthesis of dehydroquinic acid, notably oxidation of quinic acid 1 using a platinum-oxygen system [5,6] or nitric acid, [7,8] are difficult to reproduce, invariably require tedious purification, and afford the desired acid in variable yield.…”

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confidence: 99%

A Convenient Method for the Synthesis of Dehydroquinic Acid

Sann

Abell²,

Abell

2003

Synthetic Communications

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Die Synthese der 5‐Dehydro‐chinasäure

Abstract: 2080G r e w e , Jeschke: 8ynthe.m der 5-Dehydro-dinaeiiure EJahrg.89 SOC. 77,4943 [1965].

Cited by 46 publications

References 13 publications

3-Amino-5-hydroxybenzoic Acid Synthase, the Terminal Enzyme in the Formation of the Precursor of mC7N Units in Rifamycin and Related Antibiotics

3-Amino-5-hydroxybenzoic Acid Synthase, the Terminal Enzyme in the Formation of the Precursor of mC7N Units in Rifamycin and Related Antibiotics

Localization, Purification, and Characterization of Shikimate Oxidoreductase-Dehydroquinate Hydrolyase from Stroma of Spinach Chloroplasts

A Convenient Method for the Synthesis of Dehydroquinic Acid

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