TY - JOUR
T1 - Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates
AU - Farrar, William W.
AU - Plowman, Kent
PY - 1975/1/1
Y1 - 1975/1/1
N2 - The initial velocity, product inhibition, and isotopic exchange data show that the substrates of bovine heart mitochondrial acetyl-CoA synthetase add to the enzyme in an ordered fashion, with MgATP adding first followed by the addition of acetate, then the release of MgPPi immediately before the addition of CoA.
AB - The initial velocity, product inhibition, and isotopic exchange data show that the substrates of bovine heart mitochondrial acetyl-CoA synthetase add to the enzyme in an ordered fashion, with MgATP adding first followed by the addition of acetate, then the release of MgPPi immediately before the addition of CoA.
UR - http://www.scopus.com/inward/record.url?scp=32844454720&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=32844454720&partnerID=8YFLogxK
U2 - 10.1016/0020-711X(75)90069-5
DO - 10.1016/0020-711X(75)90069-5
M3 - Article
AN - SCOPUS:32844454720
VL - 6
SP - 537
EP - 542
JO - International Journal of Biochemistry and Cell Biology
JF - International Journal of Biochemistry and Cell Biology
SN - 1357-2725
IS - 8
ER -