Purification and characterization of human brain serine racemase expressed in moderately halophilic bacteria.
We have successfully expressed an active human brain serine racemase (hSR) with His-tag using moderate halophile. The purified His-hSR showed high elimination and racemization activities on L-serine: the elimination activity was 2.6-fold higher than racemization activity. Both enzyme activities showed an optimum reaction pH at around 9.0 and were stimulated 5- to 7-fold by such divalent cations as Mg++, Mn++ and Ca++.
Nagayoshi
Chizuru
C
Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan. tokunaga@chem.agri.kagoshima-u.ac.jp
Ishibashi
Matsujiro
M
Tokunaga
Masao
M
D001483:Base Sequence; D001921:Brain / Q000201:enzymology*; D002413:Cations, Divalent / Q000737:chemistry; D002846:Chromatography, Affinity; D003001:Cloning, Molecular; D020632:Halomonas / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D018272:Porins / Q000235:genetics; D011401:Promoter Regions, Genetic / Q000235:genetics; D055550:Protein Stability; D019998:Racemases and Epimerases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012694:Serine / Q000031:analogs & derivatives / Q000378:metabolism; D000099300:Serine Racemase
D002413:Cations, Divalent; D018272:Porins; D019998:Racemases and Epimerases; D012694:Serine; D000099300:Serine Racemase; C036040:serine O-sulfate