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A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding
C.A. Kettleborough, A.L. Phillips, A.J. Keys and M.A. Parry
Vol. 184, No. 1 (1991), pp. 35-39
Published by: Springer
Stable URL: http://www.jstor.org/stable/23381011
Page Count: 5
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Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 184.108.40.206) from Anacystis nidulans was used to generate novel enzymes. Two conserved residues, threonine 4 and lysine 11 in the N-terminus were changed. The substitution of threonine 4 with serine or valine had little effect on the kinetic parameters. The substitution of lysine 11 with leucine, which is non-polar, increased the Km for ribulose-1,5-bisphosphate from 82 to 190 μM but its replacement with glutamine, which has polar properties, had no appreciable effect.
Planta © 1991 Springer