Open AccessPurification and characterization of l ‐ allo ‐threonine aldolase from Aeromonas jandaei DK‐39
Author(s) -
Kataoka Michihiko,
Wada Masaru,
Nishi Kenichi,
Yamada Hideaki,
Shimizu Sakayu
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb12577.x
Subject(s) - threonine , aldolase a , serine , biochemistry , enzyme , chemistry , pyridoxal phosphate , aldolase b , fructose bisphosphate aldolase , cofactor
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, V max =45.2 μmol 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).