Appeal No. 2005-1383
Application No. 09/364,847
Since “[i]t is desirable for economic reasons to be able to produce [the
aforementioned] polymers [PHAs] in transgenic crop species [specification, p. 3,
lines 5-6]” or microorganisms, the specification discloses methods of making fusion
proteins which comprise the two “catalytically active enzymes which act on a substrate
in successive reactions in a polyhydroxyalkanoate [PHA] biosynthetic pathway” [claim 1]
which are “selected from the group consisting of β-ketothiolases, acyl-CoA reductases,
polyhydroxyalkanoate synthases, poly (3-hydroxybutyrate) synthases, phasins, enoyl-
CoA hydratases, and beta-hydroxyacyl-ACP::coenzyme-A transferases [claim 1],”
wherein the enzymes are said to be separated by a peptide linker.
Discussion
I. Written description
The examiner acknowledges that the specification teaches the structure of several
different fusion proteins. Answer, p. 5. The examiner further acknowledges that “the
specification provides references (pages 8-11) that are asserted to disclose other
naturally occurring nucleic acid sequences of genes from microorganisms encoding the
enzymes recited in claims 1 and 2.” Id. However, the examiner argues that “the genera
of enzymes recited in the claims are not [] limited to those enzymes encoded by the
naturally occurring genes disclosed in the specification.” Id. The examiner further
argues that “the genera of enzymes as recited in claims 1 and 2 encompass species
from any source, including species that have not been described in the specification,
and further encompass mutant enzymes . . . that have not been disclosed in the
specification.” Id. According to the examiner,
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