Appeal No. 2005-1383 Application No. 09/364,847 polymerase gene which is involved in PHA biosynthesis, col. 22, lines 12-15)(see, pAeP1 and pLAP1); or (ii) a promoter derived from A. eutrophus (the PHB polymerase or phbC promoter), the PHA polymerase structural gene (derived from P. oleovorans) and the ORF2 and ORF3 regions of the PHA polymerase gene (see, pAeP2 and pLAP2, and Figure 3). Accordingly, we find that this section of the patent also describes fusion plasmids encoding catalytically active enzymes which act on a substrate in successive reactions in a PHA biosynthetic pathway (viz., pAeP1 and pLAP1). In addition to the cloned and characterized genes discussed above, Peoples suggests a protein fusion comprising two catalytically active enzymes in the PHA and PHB biosynthetic pathways; i.e., a fusion of the PHA and PHB polymerase structural genes. Peoples, col. 23, lines 20-22. Peoples does not suggest a protein fusion of the catalytically active enzymes which act on substrate in successive reactions in a PHA biosynthetic pathway discussed above; this suggestion comes from Bülow. To that end we find, and the appellants do not disagree, that Bülow suggests the construction of fusion proteins comprising two or more enzymes involved in sequential reactions. Bülow discloses that the use of enzymes catalyzing sequential reactions “is a feature of many biotechnological production processes and biochemical analyses.” Bülow, p. 226, col. 1, first sentence; see also, the entire para. Bülow further discloses the importance of “generating physical proximity between the enzymes (e.g. by co- immobilization of two or more enzymes to a matrix or support) [as it] often provides . . . highly attractive properties [such as] stabilization and re-usability of the biocatalyst, [as well as] improv[ing] the kinetic characteristics of the reaction.” Id., para. bridging 15Page: Previous 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 NextLast modified: November 3, 2007