![]()
|
|
||||||||
J. Biol. Chem., Vol. 260, Issue 10, 5913-5918, 05, 1985
M Ray and S Ray
L-Threonine dehydrogenase, which forms aminoacetone from L-threonine and
NAD, has been extensively purified from goat liver. A feedback inhibition
of this enzyme has been observed with methylglyoxal. Kinetic data and other
experiments indicate that methylglyoxal acts at a site other than the
active site of the enzyme. The enzyme contains a single subunit of Mr
89,000. The apparent Km values of the enzyme for L- threonine and NAD were
found to be 5.5 and 1 mM, respectively.
L-Threonine dehydrogenase from goat liver. Feedback inhibition by methylglyoxal
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
T. Kazuoka, S. Takigawa, N. Arakawa, Y. Hizukuri, I. Muraoka, T. Oikawa, and K. Soda Novel Psychrophilic and Thermolabile L-Threonine Dehydrogenase from Psychrophilic Cytophaga sp. Strain KUC-1 J. Bacteriol., August 1, 2003; 185(15): 4483 - 4489. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |