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B6db references: 10481099.

type Journal Article
authors Wada, M.; Matsumoto, T.; Nakamori, S.; Sakamoto, M.; Kataoka, M.; Liu, J. Q.; Itoh, N.; Yamada, H.; Shimizu, S.
title Purification and characterization of a novel enzyme, L-threo-3- hydroxyaspartate dehydratase, from Pseudomonas sp. T62
journal FEMS Microbiol Lett
sel selected
ui 10481099
year (1999)
volume 179
number 1
pages 147-51
keywords Amino Acid Sequence
abstract L-threo-3-Hydroxyaspartate dehydratase (L-threo-3-hydroxyaspartate hydro-lyase), which exhibited specificity for L-threo-3- hydroxyaspartate (K(m)=0.74 mM, V(max)=37.5 micromol min(-1) (mg protein)(-1)) but not for D-threo or D, L-erythro-3-hydroxyaspartate, was purified from a cell-free extract of Pseudomonas sp. T62. The activity of the enzyme was inhibited by hydroxylamine and EDTA, which suggests that pyridoxal 5'-phosphate and divalent cations participate in the enzyme reaction. The NH(2)-terminal amino acid sequence showed significant similarity to the Saccharomyces cerevisiae YKL218c gene product, a hypothetical threonine dehydratase. However, the purified enzyme showed no threonine dehydratase activity.
last changed 2009/06/26 15:55

B6db references