The Metabolism of Quinate in Pea Roots (Purification and Partial Characterization of a Quinate Hydrolyase) | Zendy

Carola Leuschner | Zendy; Klaus M. Herrmann | Zendy; Gernot Schultz | Zendy

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The Metabolism of Quinate in Pea Roots (Purification and Partial Characterization of a Quinate Hydrolyase)

Author(s) -

Carola Leuschner,

Klaus M. Herrmann,

Gernot Schultz

Publication year - 1995

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.108.1.319

Subject(s) - shikimate pathway , biochemistry , pisum , enzyme , bovine serum albumin , biosynthesis , chemistry , tryptophan , amino acid

A quinate (QA) hydrolyase was isolated from pea (Pisum sativum L.) roots. The enzyme converts QA into shikimate by elimination of water. The enzymatic reaction is independent of cofactors and divalent cations. The QA hydrolyase was purified about 1,600-fold to apparent electrophoretic homogeneity in three steps, including bovine serum albumin-affinity chromatography. The enzyme forms oligomers and/or complexes with bovine serum albumin and ovalbumin. The monomer molecular weight of the enzyme is about 15,000. The hydrolyase shows regular Michaelis-Menten kinetics with a Km, of 2.0 mM for QA. Compartmentation studies reveal that the QA hydrolyase is localized in plastids. The QA hydrolyase may function in channeling imported QA into the shikimate pathway to support aromatic amino acid biosynthesis in plastids.

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