Appeal No. 2007-0083
Application No. 10/174,574
105. Meng also teaches that “[m]any TRX-like proteins are members of the
TRX superfamily and have the CGHC [i.e., Cys-Gly-His-Cys] sequence.”
Id.
As the Examiner has pointed out, “PRO270 lacks a Cys-Gly-Pro-Cys
active site.” Examiner’s Answer, page 8. It also does not contain a Cys-
Gly-His-Cys sequence. See SEQ ID NO:32: amino acids 160-166 form the
sequence VEFFANW, which roughly matches the first part of the consensus
sequence disclosed by Holmgren (VDFXAXW) but the next four amino
acids are SNDC, not CGPC or CGHC. See also the Appeal Brief, page 10
(“Meng . . . disclosed a protein ‘thioredoxin-related transmembrane protein
2’ or ‘TMX2’ that is 100% identical to PRO270, excluding a 12 amino acid
insert absent in the TMX2 polypeptide”) and Meng, page 105 (“TMX2
protein does not have the CGPC or CGHC sequence”).
The two cysteine (Cys or C) residues in the active site carry the –SH
groups that are reversibly oxidized to form a disulfide bridge, the “simple
and elegant mechanism” of electron transfer described by Holmgren. Thus,
PRO270 lacks the specific amino acids that are known in the art to be the
basis of thioredoxin’s activity.
We agree with the Examiner that the evidence shows that, despite the
overall similarity of PRO270 and thioredoxin, PRO270 is unlikely to have
the same activity as thioredoxin. Therefore, thioredoxin’s activity cannot be
relied on as a basis for the patentable utility of PRO270.
Appellants argue that “members of the thioredoxin family (1) have a
specific function in mediating the transfer of electrons and (2) that this
mediation has been shown to be applicable to a variety of specific
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