Appeal No. 2007-0083
Application No. 10/174,574
We do not necessarily agree with the Examiner’s broadly stated
position – that sequence similarity is not evidence of function and therefore
cannot form the basis of patentable utility. We do, however, agree that the
evidence of record shows that PRO270 is unlikely to share the activity of
thioredoxin and therefore, in this case, the sequence similarity between
PRO270 and thioredoxin is not sufficient to establish the utility of PRO270.
Holmgren1 states that “[t]hioredoxin and glutaredoxin are small
proteins containing an active site with a redox-active disulfide; they function
in electron transfer via a simple and elegant mechanism, the reversible
oxidation of two vicinal protein-SH groups to a disulfide bridge.” Abstract.
Holmgren also states:
Thioredoxin has been isolated and sequenced from a wide
variety of prokaryotic and eukoaryotic [sic] species. . . . All
species have at least one thioredoxin with an Mr around 12,000
and the same active site, Cys-Gly-Pro-Cys. . . . The active site
region is highly conserved with the consensus sequence: Val-
Asp-Phe-Xaa-Ala-Xaa-Trp-Cys-Gly-Pro-Cys-(Lys)-(Met)-(Ile)-
Xaa-Pro.
Page 13964, right-hand column.
Holmgren’s disclosure regarding the thioredoxin active site is
supported by Meng,2 which states that thioredoxin (TRX) “is characterized
by two cysteine residues within the conserved active site sequence, CGPC,”
which is identical to Holmgren’s Cys-Gly-Pro-Cys sequence. Meng, page
1 Holmgren, “Minireview: Thioredoxin and glutaredoxin,” J. Biol. Chem.,
Vol. 264, pp. 13963-13966 (1989).
2 Meng et al., “Cloning and identification of a novel cDNA coding
thioredoxin-related transmembrane protein 2,” Biochem. Genetics, Vol. 41,
pp. 99-106 (2003).
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