Activities | Families | Sequences | Fold types | References | Help
B6db references: 97372540

type Journal Article
authors Kataoka, M.; Wada, M.; Nishi, K.; Yamada, H.; Shimizu, S.
title Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39
journal FEMS Microbiol Lett
sel unselected
ui 97372540
year (1997)
volume 151
number 2
pages 245-8.
keywords Aeromonas/*enzymology
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 or L-threonine aldolase (EC
last changed 2008/01/31 19:10

B6db references