TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 272, No. 9, Issue of February 28, pp. 5445–5451, 1997 © 1997 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Side Reactions Catalyzed by Ribulose-bisphosphate Carboxylase in the Presence and Absence of Small Subunits* (Received for publication, September 4, 1996, and in revised form, December 12, 1996) Matthew K. Morell‡, Jean-Marc Wilkin§, Heather J. Kane, and T. John Andrews¶ From the Molecular Plant Physiology Group, Research School of Biological Sciences, Australian National University, P.O. Box 475, Canberra, Australian Capital Territory 2601, Australia The large subunit core of ribulose-bisphosphate car- the addition of CO to ribulose-P , producing two molecules of 2 2 boxylase from Synechococcus PCC 6301 expressed in P-glycerate using a multistep reaction sequence involving at Escherichia coli in the absence of its small subunits least three enzyme-bound catalytic intermediates (Scheme 1) retains a trace of carboxylase activity (about 1% of the (for reviews, see Refs. 1–3). Two of these intermediates, the k of the holoenzyme) (Andrews, T. J (1988) J. Biol. cat first and the third, are strong nucleophiles by virtue of their Chem. 263, 12213–12219). During steady-state catalysis enediol character. Both are susceptible to side 
TI - Side Reactions Catalyzed by Ribulose-bisphosphate Carboxylase in the Presence and Absence of Small Subunits
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.272.9.5445
DA - 1997-02-01
UR - https://www.deepdyve.com/lp/unpaywall/side-reactions-catalyzed-by-ribulose-bisphosphate-carboxylase-in-the-BuRn1XN8yB
DP - DeepDyve
ER -