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The variant enzymes with uncharged side chains, W361G, W361A, and W361T displayed higher activity than that of the wild-type enzyme with the exception of W361L.
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Metal contamination significantly reduced the activities of these enzymes with the exception of LAP.
All of these enzymes with the exception of tryptophan 2,3-dioxygenase and aspartate beta-hydroxylase are NAD(P) + dependent.
Cognate cDNAs have been reported for all of the aforementioned enzymes with the exception of MSH, P6H and DBOX.
The only measurements that failed to correlate usefully with carcinogenicity were the induction of liver enzymes (with the exception of the enzymes associated with peroxisome proliferation).
Blood clotting enzymes, with the exception of factor IX and prothrombin, are activated following single proteolytic cleavage (1).
These data showed that the affinities for ATP and substrate were similar for each of the enzymes, with the exception of EphB2, which was lower for both.
Concurrently, we detected a significant increase in the activities of the same enzymes with the exception of α-mannosidase in the cell culture media.
Activities towards aromatic and/or aliphatic nitriles were displayed by the wild-type enzyme and all of the alanine-substituted mutant enzymes, with the exception of R129A.
All restriction enzymes with the exception of EcoRI gave rise to a single hybridizing band with size variation between the sterile and fertile lines.
As mentioned above, the histidine pathway biosynthesis is performed by the endosymbionts and all enzymes, with the exception of histidinol-phosphate phosphatase (HPP, EC:3.1.3.15), have been identified.
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