3P073 Optimization of amino-acid substitutions in engineered phenylacetaldehyde dehydrogenase

Functional analysis in Saccharomyces cerevisiae of naturally occurring amino acid substitutions in human dihydrolipoamide dehydrogenase.

Dihydrolipoamide dehydrogenase is a common component of mammalian multienzyme complexes that decarboxylate alpha-ketoacids and catabolize glycine. The common function is to reoxidize a reduced lipoate component of each complex, thereby preparing that lipoate for another round of catalysis. Regions within dihydrolipoamide dehydrogenase involved in association with other proteins of the complexes...

Scoring Amino Acid Substitutions In Φhage Genomes

Substitution matrices are among the most widely used scoring techniques : BLAST, Muscle and other alignment packages, all use them. However these matrices are general; they ignore organism specific properties and do not provide customized scoring schemes. We present a Φhage-specific scoring matrix based on the abundances of aligned substitutions. These matrices use information from approximatel...

Amino Acid Properties and Consequences of Substitutions

Combinatorial codon-based amino acid substitutions.

Twenty Fmoc-protected trinucleotide phosphoramidites representing a complete set of codons for the natural amino acids were chemically synthesized for the first time. A pool of these reagents was incorporated into oligonucleotides at substoichiometric levels to generate two libraries of variants that randomly carry either few or many codon replacements on a region encoding nine amino acids of t...

Amino Acid Substitutions: Effects on Protein Stability

A living cell can be viewed as a biochemical factory, with as many as 100,000 distinct proteins providing the hardware to carry out cellular processes. The roles of these molecular machines include such diverse activities as pumping (e.g. voltage gated membrane channels), motor functions (e.g. flagella), amplification (e.g. cyclic AMP), and catalysis. The ability of a protein to function in one...