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

• Published in: Journal of general microbiology Vol. 138; no. 11; pp. 2449 - 2457
• Main Authors: Euverink, G.J.W, Hessels, G.I, Vrijbloed, J.W, Coggins, J.R, Dijkhuizen, L
• Format: Journal Article
• Language: English
• Published: England Soc General Microbiol 01.11.1992
• Subjects: 3-dehydroquinate dehydratase; Actinomycetales; Actinomycetales - enzymology; actinomycetes; Amino Acid Sequence; amino acid sequences; Amycolatopsis methanolica; aromatic amino acids; biochemical pathways; characterization; enzyme activity; hydro-lyases; Hydro-Lyases - isolation & purification; Kinetics; metabolism; Molecular Sequence Data; Molecular Weight; Mutagenesis; mutants; physicochemical properties; protein synthesis; purification; quinic acid; Quinic Acid - analogs & derivatives; Quinic Acid - metabolism; sequence alignment; Sequence Homology, Amino Acid; shikimic acid; Shikimic Acid - metabolism; structure-activity relationships; transcription (genetics)

Studies on hydroaromatic metabolism in the actinomycete Amycolatopsis methanolica 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+...