title: Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39.
abstract: L-allo-Threonine aldolase (L-allo-threonine acetaldehyde-lyase), which exhibited specificity for L-allo-threonine but not for L-threonine, was purified from a cell-free extract of Aeromonas jandaei DK-39. The purified enzyme catalyzed the aldol cleavage reaction of L-allo-threonine (K(m) = 1.45 mM, Vmax = 45.2 mumol min-1 mg-1). The activity of the enzyme was inhibited by carbonyl reagents, which suggests that pyridoxal-5'-phosphate participates in the enzymatic reaction. The enzyme does not act on either L-serine or L-threonine, and thus it can be distinguished from serine hydroxy-methyltransferase (L-serine:tetrahydrofolate 5,10-hydroxy-methyltransferase, EC 2.1.2.1) or L-threonine aldolase (EC 4.1.2.5).
authors.affiliation: Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Kataoka
authors.forename: M
authors.initials: M
authors.lastname: Wada
authors.forename: K
authors.initials: K
authors.lastname: Nishi
authors.forename: H
authors.initials: H
authors.lastname: Yamada
authors.forename: S
authors.initials: S
authors.lastname: Shimizu
mesh_terms: D000333:Aeromonas / Q000201:enzymology*; D000595:Amino Acid Sequence; D012696:Glycine Hydroxymethyltransferase / Q000737:chemistry / Q000302:isolation & purification* / Q000502:physiology; D008969:Molecular Sequence Data; D013379:Substrate Specificity
chemical_list: D012696:Glycine Hydroxymethyltransferase