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J Biol Chem, Vol. 273, Issue 41, 26705-26713, October 9, 1998
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From the Prenyltransferases catalyze the consecutive
condensations of isopentenyl diphosphate to produce linear polyprenyl
diphosphates. Each enzyme forms the final product with a specific chain
length. The product specificity of an enzyme is thought to be
determined by the structure around the unknown path through which the
product elongates in the enzyme. To explore the path, we introduced a few mutations at the 5th, the 8th, and/or the 11th positions before the
first aspartate-rich motif of geranylgeranyl-diphosphate synthase or
farnesyl-diphosphate synthase. The side chains of these amino acids are
situated on the same side of an Department of Biochemistry and Engineering,
-helix. In
geranylgeranyl-diphosphate synthase, a single mutated enzyme (F77S)
mainly produces a C25 product (Ohnuma, S.-I.,
Hirooka, K., Hemmi, H., Ishida, C., Ohto, C., and Nishino, T. (1996)
J. Biol. Chem. 271, 18831-18837). A double mutated
enzyme (L74G and F77G) mainly produces a C35 compound with
significant amounts of C30 and C40. A triple
mutated enzyme (I71G, L74G, and F77G) mainly produces a C40
compound with C35 and C45. Mutated
farnesyl-diphosphate synthases also show similar patterns. These
findings indicate that the elongating product passages on a surface of
the side chains of the mutated amino acids, the original bulky amino
acids had blocked the elongation, and the path is conserved in
prenyltransferases. Moreover, the fact that some double and triple
mutated enzymes can also form small amounts of products longer than
C50 indicates that the paths in these mutated enzymes can
partially access the outer surface of the enzymes.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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