Purification and characterization of 3-dehydroquinate hydrolase and shikmate oxidoreductase. Evidence for a bifunctional enzyme.
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.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D006836:Hydro-Lyases / Q000302:isolation & purification* / Q000378:metabolism; D008722:Methods; D009097:Multienzyme Complexes / Q000302:isolation & purification*; D010455:Peptides / Q000302:isolation & purification / Q000378:metabolism; D010944:Plants / Q000201:enzymology*; D011801:Quinic Acid / Q000031:analogs & derivatives; D012765:Shikimic Acid
D009097:Multienzyme Complexes; D010455:Peptides; D011801:Quinic Acid; D012765:Shikimic Acid; D000429:Alcohol Oxidoreductases; C022641:Shikimate dehydrogenase; D006836:Hydro-Lyases; C020000:3-dehydroquinate dehydratase