Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Leodis Davis"'
Autor:
Huaxiang Tong, Leodis Davis
Publikováno v:
Biochemistry. 34:3362-3367
A study of protons associated with low-barrier hydrogen bonds in 2-amino-3-ketobutyrate-CoA ligase (AKB-ligase, EC 2.3.1.29) by NMR is reported. Three resonances are observed in the range of delta H = 15-20 ppm when the NMR spectrum of AKB-ligase is
Publikováno v:
Journal of the American Chemical Society. 99:4467-4471
Autor:
Leodis Davis, Gordon F. Kapke
Publikováno v:
Biochemical and Biophysical Research Communications. 65:765-769
Summary The microbial toxin trans L ¯ ¯ ‐2‐amino‐4‐methoxy‐3‐butenoic acid and its parent vinylglycine are deaminated to alpha ketoacids by sheep liver serine threonine dehydratase. The ability of the dehydratase to deaminate the above
Publikováno v:
Biochemistry. 14:1108-1115
Galactose oxidase is a metalloenzyme containing a single copper atom per molecule. The mechanism of action of galactose oxidase is studied in this paper by investigating substrate specificity and activation by peroxidase, and probing the copper site
Autor:
Leodis Davis, Gordon F. Kapke
Publikováno v:
Biochemistry. 15:3745-3749
Products, substrates, and inhibitors of the threonine dehydratase from sheep liver (EC 4.2.1.16) have been investigated by proton nuclear magnetic resonance and optical rotation. The alpha-ketobutyrates produced from L-threonine and L-allothreonine i
Autor:
David E. Metzler, Leodis Davis
Publikováno v:
Journal of Biological Chemistry. 237:1883-1889
Autor:
Leodis Davis, Edward Dixon
Publikováno v:
Archives of Biochemistry and Biophysics. 119:155-158
The action of sheep liver threonine dehydratase has been investigated with l -allothreonine as the substrate. The enzyme has previously been reported to utilize l -allothreonine as substrate [Davis, L., and Metzler, D. E., J. Biol. Chem. 237 , 1883 (
Autor:
Leodis Davis, Ihor Bekersky
Publikováno v:
Biochemical and Biophysical Research Communications. 32:134-137
Autor:
Leodis Davis
Publikováno v:
Analytical Biochemistry. 12:36-40
The enzymic conversion of β-hydroxy α-amino acids to α-keto acids by ThrDH (sheep liver) was followed by a direct spectrophotometric method at 230 mμ. The assay was more sensitive to changes in keto acid concentrations than the 2,4-dinitrophenylh