Catalytically active monomers of E. coli glyceraldehyde-3-phosphate dehydrogenase.
Monomeric forms of E. coli glyceraldehyde-3-phosphate dehydrogenase have been prepared using two different experimental approaches: (1) covalent immobilization of a tetramer on a solid support via a single subunit with subsequent dissociation of non-covalently bound subunits in the presence of urea, and (2) entrapment of monomeric species into reversed micelles of Aerosol OT in octane. Isolated monomers were shown to be catalytically active, exhibiting KM values close to the parameters characteristic of the tetrameric forms. Like tetramers, isolated monomers did not use NADP7 as a coenzyme.
Levashov
P A
PA
Department of Chemistry, Moscow State University, Russia.
Muronetz
V I
VI
Klyachko
N L
NL
Nagradova
N K
NK
D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008823:Micelles; D011487:Protein Conformation
D008823:Micelles; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases