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Literature DB >> 687649

Purification and characterization of 3-dehydroquinate hydrolase and shikmate oxidoreductase. Evidence for a bifunctional enzyme.

Abstract

The basis for the physical association of 3-dehydroquinate dehydratase (3-dehydroquinate hydrolyase, EC 4.2.1.10) and shikimate dehydrogenase (shikimate: NADP+ 3-oxidoreductase, EC 1.1.1.25) in higher plants was investigated. The enzymes were extracted from the moss Physcomitrella patens and were purified to homogeneity. Determinations of subunit sizes were made by sodium dodecyl sulfate gel electrophoresis and gel exclusion chromatography in 6 M guanidinium chloride. Results from these studies demonstrate that both enzyme activities are carried out by a single polypeptide.

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Year: 1978 PMID： 687649 DOI： 10.1016/0005-2744(78)90310-8

Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002

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Cited

14 in total

1. The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains.

Authors: K Duncan; R M Edwards; J R Coggins
Journal: Biochem J Date: 1987-09-01 Impact factor: 3.857

2. Localization, purification, and characterization of shikimate oxidoreductase-dehydroquinate hydrolyase from stroma of spinach chloroplasts.

Authors: E Fiedler; G Schultz
Journal: Plant Physiol Date: 1985-09 Impact factor: 8.340

8. A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding.

Authors: Samuel H Light; George Minasov; Ludmilla Shuvalova; Scott N Peterson; Michael Caffrey; Wayne F Anderson; Arnon Lavie
Journal: Biochemistry Date: 2011-02-21 Impact factor: 3.162

9. Cytosolic and plastid forms of 5-enolpyruvylshikimate-3-phosphate synthase in Euglena gracilis are differentially expressed during light-induced chloroplast development.

Authors: C Reinbothe; B Ortel; B Parthier; S Reinbothe
Journal: Mol Gen Genet Date: 1994-12-01

10. Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase.

Authors: I A Anton; J R Coggins
Journal: Biochem J Date: 1988-01-15 Impact factor: 3.857

Purification and characterization of 3-dehydroquinate hydrolase and shikmate oxidoreductase. Evidence for a bifunctional enzyme.

1. The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains.

2. Localization, purification, and characterization of shikimate oxidoreductase-dehydroquinate hydrolyase from stroma of spinach chloroplasts.

3. The Shikimate Pathway: Early Steps in the Biosynthesis of Aromatic Compounds.

4. Purification and properties of 5-enolpyruvylshikimate 3-phosphate synthase from seedlings of Pisum sativum L.

5. The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor.

6. The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase.

7. Isolation of a bifunctional domain from the pentafunctional arom enzyme complex of Neurospora crassa.

8. A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding.

9. Cytosolic and plastid forms of 5-enolpyruvylshikimate-3-phosphate synthase in Euglena gracilis are differentially expressed during light-induced chloroplast development.

10. Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase.