Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39.
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).
Kataoka
M
M
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Japan.
Wada
M
M
Nishi
K
K
Yamada
H
H
Shimizu
S
S
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
D012696:Glycine Hydroxymethyltransferase