|
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 |
Activity |
4.1.2.49 |
sel |
selected |
ui |
97372540 b |
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 2.1.2.1) or L-threonine aldolase (EC 4.1.2.5). |
last changed |
2017/07/11 17:50 |
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