Purification and properties of ornithine racemase from Clostridium sticklandii.
Ornithine racemase has been purified to homogeneity from Clostridium sticklandii, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This is the first racemase known to be highly specific to ornithine. This PLP-dependent enzyme has an M(r) of 92, 000, with a K(m) for L-ornithine of 0.77 +/- 0.05 mM and a k(cat) of 980 +/- 20 s(-1).
Chen
H P
HP
Department of Biochemistry, China Medical College, Taichung 404, Taiwan. hpchen@mail.cmc.edu
Lin
C F
CF
Lee
Y J
YJ
Tsay
S S
SS
Wu
S H
SH
D000591:Amino Acid Isomerases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002384:Catalysis / Q000187:drug effects; D003013:Clostridium / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008970:Molecular Weight; D009952:Ornithine / Q000378:metabolism*; D011732:Pyridoxal Phosphate / Q000378:metabolism / Q000494:pharmacology; D019998:Racemases and Epimerases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity; D013816:Thermodynamics
D011732:Pyridoxal Phosphate; D009952:Ornithine; D019998:Racemases and Epimerases; D000591:Amino Acid Isomerases; C406208:ornithine racemase