Abstract: A synthetic nucleic acid sequence is disclosed, comprising a non-naturally occurring polymer of nucleic acids, having a biological function encoded by the sequence and known from a starting nucleic acid sequence, and having a difference in sequence of at least about 5% between the nucleic acids of the synthetic sequence and the starting sequence. The difference between the nucleic acid sequences results in a different free energy of folding for the synthetic sequence as compared to the starting sequence, such that the synthetic sequence would be expressed better in a selected heterologous host cell than the starting sequence would be if expressed in the same heterologous host cell.

Abstract: Pro-dyes of direct dyes having an enzymatically-labile functionality, e.g.

Abstract: Mutants of leucine dehydrogenase sequences, formate dehydrogenase sequences and galactose oxidase sequences are provided. An amino acid sequence that is a mutant of a leucine dehydrogenase sequence as described in SEQ ID 2, or its substantial equivalent, contains at least one mutation selected from the group consisting of F102S, V33A, S351T, N145S and like mutations in subsantially equivalent sequences. An amino acid sequence that is a mutant of a formate dehydrogenase sequence as described in SEQ ID 1, or its substantial equivalent, contains at least one mutation selected from the group consisting of D195S, Y196H, K356T and like mutations in subsantially equivalent sequences.

Abstract: A methods for producing a hydroxy-amino acid or derivative thereof, such as statine, phenylstatine or isostatine, is provided. A substituted &bgr;-ketodiester having a ketone group and two ester functional groups is contacted with a ketoreductase under conditions permitting the reduction of the ketone group to an alcohol. Only one of the ester functional groups is regioselectively hydrolyzed to the corresponding carboxylic acid, whereby a non-hydrolyzed ester functional group remains. Either the carboxylic acid or the non-hydrolyzed ester functional group is converted to an amine or a derivative thereof to produce a hydroxy-amino acid or derivative thereof.

Abstract: Methods for producing single diastereomers of isoleucine in high stereochemical purity are provided. D-isoleucine is produced by converting (R)-2-methylbutyraldehyde to a diastereomeric mixture of D-isoleucine hydantoin and L-allo-isoleucine hydantoin (5S-[(R)-1-methylpropyl]hydantoin) under conditions whereby no significant racemization of the chiral center in (R)-2-methylbutyraldehyde occurs, followed by contacting said diastereomeric hydantoin mixture with a D-hydantoinase to stereoselectively hydrolyze any D-isoleucine hydantoin in the mixture to the corresponding N-carbamoyl-D-isoleucine, preferably under conditions permitting the simultaneous epimerization of the chiral center at C-5 of the hydantoin. The simultaneous epimerization permits the reaction to be carried out to substantial completion so that the diastereomeric hydantoin mixture is converted to N-carbamoyl-D-isoleucine in high yield. The N-carbamoyl-D-isoleucine is then decarbamoylated to produce D-isoleucine.

Abstract: A method for producing D-allo-isoleucine is provided. The method comprises converting L-isoleucine to the corresponding hydantoin. Amixture containing the hydantoin is contacted with a D-hydantoinase to stereoselectively hydrolyze any D-allo-isoleucine hydantoin in the mixture to the corresponding N-carbamoyl-D-allo-isoleucine. The N-carbamoyl-D-allo-isoleucine is decarbamoylated to produce D-allo-isoleucine. Preferably the contacting of the hydantoin with a D-hydantoinase is carried out under conditions permitting the simultaneous epimerization of the chiral center at C-5 of the hydantoin.

Abstract: The invention relates to a coupled enzymatic process for producing tryptamine derivatives from indole compounds. In the first enzyme-catalyzed reaction, indole derivatives are converted to tryptophan derivative intermediates, then the tryptophan intermediates are decarboxylated in a second enzymatic reaction in the same reaction system. In this way, tryptamine derivative products are formed from indole derivatives in a single process. The invention is also directed to novel tryptophan and tryptamine derivatives, which can be prepared by the inventive method.

Abstract: A synthetic nucleic acid sequence is disclosed, comprising a non-naturally occurring polymer of nucleic acids, having a biological function encoded by the sequence and known from a starting nucleic acid sequence, and having a difference in sequence of at least about 5% between the nucleic acids of the synthetic sequence and the starting sequence. The difference between the nucleic acid sequences results in a different free energy of folding for the synthetic sequence as compared to the starting sequence, such that the synthetic sequence would be expressed better in a selected heterologous host cell than the starting sequence would be if expressed in the same heterologous host cell.

Abstract: The present invention relates to an agent for dyeing keratin fibers, containing at least one compound with a nucleophilic reaction center, at least one alcohol from the group comprising aryl alcohol derivatives and benzyl alcohol derivatives and at least one suitable oxidizing enzyme, as well as to a method for dyeing keratin fibers using this agent.

Abstract: Methods for chemically transforming compounds using a mutated enzyme are provided, and more particularly a method for the production of an amino acid from a target 2-ketoacid, the production of an amine from a target ketone and the production of an alcohol from a target ketone. The methods comprise creating a mutated enzyme that catalyzes the reductive amination or transamination of the target 2-ketoacid or ketone or the reduction of the ketone and providing the mutated enzyme in a reaction mixture comprising the target 2-ketoacid or ketone under conditions sufficient to permit the formation of the desired amino acid, amine or alcohol to thereby produce the amino acid, amine or alcohol.

Abstract: A method of making a synthetic nucleic acid sequence comprises providing a starting nucleic acid sequence, which optionally encodes an amino acid sequence, and determining the predicted &Dgr;Gfolding of the sequence. The starting nucleic acid sequence can be a naturally occurring sequence or a non-naturally occurring sequence. The starting nucleic acid sequence is modified by replacing at least one codon from the starting nucleic acid sequence with a different corresponding codon to provide a modified nucleic acid sequence. As used herein, a “different corresponding codon” refers to a codon which does not have the identical nucleotide sequence, but which encodes the identical amino acid. The predicted &Dgr;Gfolding of the modified nucleic acid sequence is determined and compared with the &Dgr;Gfolding of the starting nucleic acid sequence.

Abstract: The disclosure describes novel precursors for the preparation of chiral 1,3-aminoalcohols. The precursors are chiral 4-hydroxycarboxamides, 4-hydroxyhydroxamic acids, or 4-hydroxyhydrazides produced from chiral gamma-lactones, which in turn are derived from 1,4-diols by stereoselective oxidation. The chiral 4-hydroxycarboxamides, 4-hydroxyhydroxamic acids, or 4-hydroxyhydrazides are converted into chiral 1,3-aminoalcohols by stereospecific rearrangement.

Abstract: The disclosure describes new compositions of matter useful for the preparation of optically-active vicinal aminoalcohols. The compositions are chiral .beta.-hydroxycarboxamides, .beta.-hydroxyhydraxides, and .beta.-hydroxyhydroxamic acids.

Abstract: The disclosure describes a method for the preparation of chiral 1,3-aminoalcohols in high optical purity. The method combines the stereoselective oxidation of a 1,4-diol to a gamma-lactone using an alcohol dehydrogenase, the conversion of the gamma-lactone to the corresponding 4-hydroxyamide, 4-hydroxyhydroxamic acid, or 4-hydroxyhydrazide, and stereospecific rearrangement of the 4-hydroxyamide, 4-hydroxyhydroxamic acid, or 4-hydroxyhydrazide to the corresponding chiral 1,3-aminoalcohol.

Abstract: A method for quantitating L-homocysteine and/or L-methionine in a solution involves contacting a solution containing L-homocysteine and/or L-methionine with a reagent comprising methionine gamma-lyase and a cofactor capable of forming a Schiff base with the L-methionine and/or L-homocysteine for a time sufficient to catalyze the conversion of L-homocysteine and/or L-methionine to 2-ketobutyrate. The amount of 2-ketobutyrate formed is determined, and the amount of L-homocysteine and/or L-methionine present in the original solution can be determined based on the amount of 2-ketobutyrate formed. A composition for measuring the amount of L-homocysteine and/or L-methionine in a solution comprises methionine gamma-lyase, a cofactor capable of forming a Schiff base with the L-methionine and/or L-homocysteine and at least one 2-ketobutyrate detecting agent, but is substantially free of L-methionine, L-homocysteine, 2-ketobutyrate, pyruvate and mercury.

Abstract: The disclosure describes a method for the preparation of chiral vicinal aminoalcohols in high optical purity. The method combines the stereoselective reduction of the keto group of a .beta.-ketoacid, .beta.-keotester, or derivative with the stereospecific rearrangement of the corresponding amide, hyroxamic acid, or hydrazide to produce chiral vicinal aminoalcohols with control of stereochemistry at both chiral centers.

Abstract: This invention provides genes encoding aspartate beta decarboxylase, vectors containing the genes, microbial host cells transformed with the vectors, and the use of such transformed host cells and compositions derived therefrom to produce L-alanine and certain derivatives thereof.

Abstract: This invention relates to a method for the production of a composition comprising the enzyme cyclodextrin glucosyltransferase bound by covalent means to a support material in the presence of a source of divalent calcium ion, said immobilized cyclodextrin glucosyltransferase having a higher activity and greater stability than heretofore reported. This invention further relates to the use of the immobilized cyclodextrin glucosyltransferase for the production of cyclodextrins.

Abstract: A biocatalytic method for producing a desired amino acid is disclosed. The method involves contacting a 2-ketoacid corresponding to the desired amino acid with lactic acid, aspartic acid and ammonia, or salts thereof, in the presence of:(a) one or more transaminase enzymes capable of catalyzing the conversion of the 2-ketoacid and L-aspartic acid to the desired amino acid and oxaloacetic acid;(b) a malate-lactate transhydrogenase enzyme capable of catalyzing the conversion of lactic acid and oxaloacetic acid to pyruvic acid and malic acid;(c) a fumarase enzyme capable of catalyzing the conversion of malic acid to fumaric acid; and(d) an aspartate-ammonia lyase enzyme capable of catalyzing the conversion of fumaric acid and ammonia to aspartic acid.

Abstract: This invention relates to a process for producing a desired alpha-amino acid, AA.sub.d, or a derivative thereof. The process comprises:(a) reacting a first alpha-amino acid, AA.sub.NH.sbsb.2 ; a first alpha-keto acid, KA.sub.t ; a second alpha-keto acid, KA.sub.pre ; a first transaminase enzyme and a second transaminase enzyme to produce (i) the desired alpha-amino acid, AA.sub.d and (ii) a third alpha-keto acid, KA.sub.prod ; and(b) removing KA.sub.prod from the other keto acids, amino acids and enzymes wherein AA.sub.d and KA.sub.pre, AA.sub.t and KA.sub.t, and AA.sub.NH.sbsb.2 and KA.sub.prod are interconvertible, respectively, by amino group transfer. The first transaminase efficiently catalyzes reaction (i), but not reaction (ii) and the second transaminase efficiently catalyzes reaction (ii) but not reaction (i):AA.sub.NH.sbsb.2 +KA.sub.t .revreaction.AA.sub.t +KA.sub.prod (i)AA.sub.t +KA.sub.pre .revreaction.AA.sub.d +KA.sub.t (ii)In one embodiment KA.sub.