Appeal No. 2001-0762 Page 4
Application No. 08/343,585
has a D-amino acid residue sequence corresponding to an L-amino acid residue
sequence defined by the natural L-enzyme. As disclosed at page 14 of
appellants’ specification:
Many enzymes … have been the subject of mutation of their
natural amino acid residue sequence such that they no longer
correspond in amino acid residue sequence to the sequence of a
natural isolate, and yet still retain an enzymatic activity. Thus, in
another embodiment, the invention contemplates D-enzymes
having amino acid residue sequences that correspond to known
enzymes.
Therefore, as we understand appellants’ claimed invention, the sequence
of the claimed enzyme must be the same as that of the natural enzyme
but for the use of D-amino acids and glycine.
The only reference relied upon by the examiner that comes close to
meeting the requirements of the claimed invention is Zawadzke. According to
the examiner (Answer, page 5), Zawadzke teaches “the chemical synthesis of
all-D-rubredoxin.” The examiner notes (id.), “that the protein has a ‘relatively
high hydrogenase-like activity of its Ni2+ complex[‘] … [and therefore] can be
considered an honorary enzyme….” According to the examiner (id.), while
Zawadzke does not teach the reaction of this D-enzyme with chiral substrates,
the D-form of rubredoxin can be used “to solve the crystallographic phase
problem.”
In response, appellants argue (Brief, page 6) that while “Zawadzke cites a
prior art reference (Saint Martin) which observes that a non-naturally occurring
Ni2+ complex of the native L-rubredoxin has a ‘hydrogenase-like activity’ …
[Zawadzke] does not disclose or suggest that either of his synthetic D-[]or L-
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