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a Related Biological Terms:

Cysteinyl aspartate-specific proteinase; a member of a group of cellular cysteine endopeptidases that cleave so as to leave an N-terminal aspartate residue. The group includes interleukin-converting enzymes and enzymes associated with activation of apoptosis either as initiators near the head of a cascade of events, or as executioners, which perform limited proteolyisis of cellular proteins at the bottom of the cascade.Nicholson, D.W. and Thornberry, N.A. (1997) Trends Biochem. Sci. 22, 299-306; Salvesen, G.S. and Dixit, V.M. (1997) Cell 91, 443-446; Villa, P., Kaufmann, S.H. and Earnshaw, W.C. (1997) Trends Biochem. Sci. 22, 388-393; Nicholson, D.W Learn more about restriction enzymes.

A mutation-containing restriction fragment that can replace the homologous fragment excised from the genome of an organism.

A method to determine the limits of tolerance of a protein to amino acid substitution. A cloned gene is mutated by synthesis of short segments of the gene with random base substitutions, insertion of these altered polynucleotide sequences into the gene and then transformation of cells with the mutated gene. Cells that contain a functional protein are selected and the protein (or gene) is examined to identify the successful mutation. Testing of many such short segments until the entire structural gene is examined maps the areas of tolerance and of sensitivity of the gene product to substitutions. Bowie, J.U., Reidhaar-Olsen, J.S., Lim, W.A. and Sauer, R.T. (1990) Science 247, 1306-1310 Related reading: mutagenesis

The action of energy-yielding metabolic pathways that degrade macromolecules and complex compounds or small molecules into CO2, H2O, etc. (see also amphibolic pathway; anabolism)

A degradation product derived from a more complex compound. (see also anabolite)

(see glucose effect)

(see glucose effect)

(see ribozyme)

An antibody with catalytic properties; often raised against a hapten that chemically resembles the transition state of the intended substrate so as to force a substrate into that transition state. Hilvert, D. (1994) Curr. Opin. Struct. Biol. 4, 612-617; Jacobsen, J.R. and Schultz, P.G. (1995) Curr. Opin. Struct. Biol. 5, 818-824

(see entropy effect)

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