2922-42-1Relevant articles and documents
Mechanistic studies on type I and type II dehydroquinase with (6R)- and (6S)-6-fluoro-3-dehydroquinic acids
Parker, Emily J.,Bello, Concepcion Gonzalez,Coggins, John R.,Hawkins, Alastair R.,Abell, Chris
, p. 231 - 234 (2000)
(6R)- and (6S)-6-Fluoro-3-dehydroquinic acids are shown to be substrates for type I and type II dehydroquinases. Their differential reactivity provides insight into details of the reaction mechanism and enables a novel enzyme-substrate imine to be trapped
High shikimate production from quinate with two enzymatic systems of acetic acid bacteria
Adachi, Osao,Ano, Yoshitaka,Toyama, Hirohide,Matsushita, Kazunobu
, p. 2579 - 2582 (2008/02/12)
3-Dehydroshikimate was formed with a yield of 57-77% from quinate via 3-dehydroquinate by two successive enzyme reactions, quinoprotein quinate dehydrogenase (QDH) and 3-dehydroquinate dehydratase, in the cytoplasmic membranes of acetic acid bacteria. 3-Dehydroshikimate was then reduced to shikimate (SKA) with NADP-dependent SKA dehydrogenase (SKDH) from the same organism. When SKDH was coupled with NADP-dependent D-glucose dehydrogenase (GDH) in the presence of excess D-glucose as an NADPH regenerating system, SKDH continued to produce SKA until 3-dehydroshikimate added initially in the reaction mixture was completely converted to SKA. Based on the data presented, a strategy for high SKA production was proposed.
Purification and characterization of membrane-bound quinoprotein quinate dehydrogenase
Adachi, Osao,Yoshihara, Nozomi,Tanasupawat, Somboon,Toyama, Hirohide,Matsushita, Kazunobu
, p. 2115 - 2123 (2007/10/03)
Several bacterial strains carrying quinoprotein quinate dehydrogenase (QDH) were screened through acetic acid bacteria and other bacteria. Strong enzyme activity was found in the membrane fraction of Gluconobacter melanogenus IFO 3294, G. oxydans IFO 3292
