Separation and some properties of D-galactonate pathway enzymes from Mycobacterium sp. 607.
D-galactonate-grown cells of Mycobacterium sp. 607 can utilize D-galactonate by a pathway involving D-galactonate dehydratase, 2-keto-3-deoxy-galactonate kinase and 6-phospho-2-keto-3-deoxygalactonate aldolase. The enzymes have been separated by ion-exchange chromatography on DEAE-cellulose or ultrafiltration on Sephadex G-100. Partial characterization on the kinase and the aldolase have been described.
D000446:Aldehyde-Lyases / Q000302:isolation & purification / Q000378:metabolism*; D006836:Hydro-Lyases / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009161:Mycobacterium / Q000201:enzymology*; D010770:Phosphotransferases / Q000302:isolation & purification / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor); D013400:Sugar Acids / Q000378:metabolism
D013400:Sugar Acids; C012991:galactonic acid; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C032243:2-dehydro-3-deoxygalactonokinase; D000446:Aldehyde-Lyases; C022366:6-phospho-2-keto-3-deoxy-galactonate aldolase; D006836:Hydro-Lyases; C019607:galactonate dehydratase