[HTML][HTML] Hybrid tetramers of porcine liver fructose-1, 6-bisphosphatase reveal multiple pathways of allosteric inhibition
SW Nelson, RB Honzatko, HJ Fromm - Journal of Biological Chemistry, 2002 - ASBMB
Fructose-1, 6-bisphosphatase is a square planar tetramer of identical subunits, which
exhibits cooperative allosteric inhibition of catalysis by AMP. Protocols for in vitrosubunit
exchange provide three of five possible hybrid tetramers of fructose-1, 6-bisphosphatase in
high purity. The two hybrid types with different subunits in the top and bottom halves of the
tetramer co-purify. Hybrid tetramers, formed from subunits unable to bind AMP and subunits
with wild-type properties, differ from the wild-type enzyme only in regard to their properties of …
exhibits cooperative allosteric inhibition of catalysis by AMP. Protocols for in vitrosubunit
exchange provide three of five possible hybrid tetramers of fructose-1, 6-bisphosphatase in
high purity. The two hybrid types with different subunits in the top and bottom halves of the
tetramer co-purify. Hybrid tetramers, formed from subunits unable to bind AMP and subunits
with wild-type properties, differ from the wild-type enzyme only in regard to their properties of …