A Novel 3-Dehydroquinate Dehydratase Catalyzing Extracellular Formation of 3-Dehydroshikimate by Oxidative Fermentation ofGluconobacter oxydansIFO 3244

Conversion of Quinate to 3-Dehydroshikimate by Ca-Alginate-Immobilized Membrane ofGluconobacter oxydansIFO 3244 and Subsequent Asymmetric Reduction of 3-Dehydroshikimate to Shikimate by Immobilized Cytoplasmic NADP-Shikimate Dehydrogenase

“…DQA was measured with membrane-bound DQA dehydratase (mDQD). 14) DSA and SKA were measured with NADP-dependent SKDH. 15) DSA formation from quinate was measured by reading the absorbance at 234 nm with a double-beam spectrophotometer (Hitachi Model U2000, Tokyo).…”

“…An affinity complex formed with BD and the mixture of SKDH and GDH reacted freely with DSA on filters of two different pore sizes, 50,000 and 100,000 (Millipore Japan, Tokyo) in the presence of a catalytic amount of NADP and an excess D-glucose, as found previously. 2,14) Judging from the molecular sizes of SKDH and GDH, a pore size of 50,000 kept the enzymes on the filter during filtration. The molecularweight cut-off filters, Ultra Filter Q0500 043E and Q0500 076E (Advantec MFS, Tokyo) with a pore size of 50,000, was also used in a similar manner.…”

Genome-Scale Metabolic Reconstruction of Acetobacter pasteurianus 386B, a Candidate Functional Starter Culture for Cocoa Bean Fermentation

“…The aromatic amino acids L-phenylalanine, L-tyrosine, and L-tryptophan share a common initial pathway, which produces chorismate from erythrose 4-phosphate (Yang and Pittard, 2008). Comparative genomics revealed that the gene with locus tag APA386B_1330, encoding a dehydroquinate dehydratase (EC 4.2.1.10), had an ortholog in G. oxydans 621H (locus tag GOX0437) that has been identified as encoding a periplasmic enzyme involved in the oxidation of quinate (Adachi et al, 2008). The cytoplasmic dehydroquinate dehydratase of G. oxydans 621H (locus tag GOX1351) could not be found in the A. pasteurianus 386B genome.…”

Solubilization, Purification, and Properties of Membrane-BoundD-Glucono-δ-lactone Hydrolase fromGluconobacter oxydans

“…The abundance of MGL in the membrane fraction reflected a typical profile of a membrane-bound enzyme to cytoplasmic enzymes in acetic acid bacteria. 14,[21][22][23] Regarding SGL in the same G. oxydans IFO 3244, the enzyme activity was too weak to purify, resulting in poor yield after many steps of purification, as seen in some cases of SGL purification. 10,13) Thus, purification of SGL from G. oxydans remains to be done in future.…”