Appeal No. 2003-1307 Page 4
Application No. 09/420,785
Furthermore, regarding appellants’ claim 25, we note that claim 1 of the
‘627 patent is drawn to:
A method for transamidating a peptide substrate having a P1
amino acid residue with a positively charged side chain and a P3
amino acid residue with a positively charged side chain, the method
comprising:
reacting the peptide substrate with a nucleophile in the
presence of a modified carboxypeptidase Y,
wherein the modified carboxypeptidase comprises at least
one substitution in an S1 subsite with an amino acid having a
negatively charged side chain and at least one substitution of an
amino acid residue capable of interacting with a peptide substrate
P3 residue wherein the substitution introduces an amino acid
having a negatively charged side chain wherein at least one
substitution in the S1 subsite and at least one substitution of an
amino acid residue capable of interacting with a peptide substrate
P3 residue are different.
Claim 1 of the ‘627 patent appears to be of substantially greater scope than
claim 25 now on appeal. Note, in contrast to appellants’ claim 25, claim 1 of the
‘627 patent does not require that the “modified carboxypeptidase Y is derived
from the peptide having the sequence of SEQ ID NO: 4.”
We also note that the L178 and M398L substitutions are accounted for in
at least claims 2 and 7 of the ‘627 patent:
2. The method of claim 1, wherein the modified carboxypeptidase comprises
at least one substitution in the S1 subsite at amino acid residue L178….
7. The method of claim 1, wherein the modified carboxypeptidase further
comprises at least one substitution in an S1’ subsite selected from the
group consisting of … M398L….
As discussed above, the specific L178S substitution is disclosed at page 10,
lines 4-5 of appellants’ specification.
Based on this evidence, we are unable to agree with the examiner’s
conclusion (Answer, page 8), “absent structural limitations on a modified
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