Abstract: New genes containing a DNA sequence coding for hydroxynitrile lyase, which genes can be prepared via a primer combination based on the DNA sequence of the 5?-region of the mdl genes from Prunus serotina and from Prunus amygdalus and/or a primer 2 based on the 3?-region of the DNA sequences of one of the hydroxynitrile lyase isoenzymes from Prunus serotina or from Prunus amygdalus, subsequent amplification with a DNA polymerase using a DNA from organisms, containing genes coding for hydroxynitrile lyase, as templates and cloning, and also recombinant proteins which can be prepared in suitable host cells by heterologous expression of the DNA sequence of said HNL genes, and proteins and fusion proteins derived therefrom and use of said proteins for preparing (R)- or (S)-cyanohydrins.

Abstract: An enzyme that cleaves 1,3-dicarbonyl compounds by incorporating molecular oxygen into the substrate in amounts equimolar to the amount of substrate cleaved. The enzyme from Acinetobacter johnsonii is a multimer of about 67 kilodaltons made up of subunits of about 16.6 kilodaltons. Nucleotide and amino acid sequence analysis of a cloned A. johnsonii subunit indicates little homology with other proteins. Native or recombinant enzyme can be used to decontaminate or detoxify acetylacetone or related diketones.

Abstract: Screening method for detecting amidase or nitrohydratase activity, which comprises

Abstract: An enzyme that cleaves 1,3-dicarbonyl compounds by incorporating molecular oxygen into the substrate in amounts equimolar to the amount of substrate cleaved. The enzyme from Acinetobacter johnsonii is a multimer of about 67 kilodaltons made up of subunits of about 16.6 kilodaltons. Nucleotide and amino acid sequence analysis of a cloned A. johnsonii subunit indicates little homology with other proteins. Native or recombinant enzyme can be used to decontaminate or detoxify acetylacetone or related diketones.

Abstract: New genes containing a DNA sequence coding for hydroxynitrile lyase, which genes can be prepared via a primer combination based on the DNA sequence of of the 5′-region of the mdl genes from Prunus serotina and from Prunus amygdalus and/or a primer 2 based on the 3′-region of the DNA sequences of one of the hydroxynitrile lyase isoenzymes from Prunus serotina or from Prunus amygdalus, subsequent amplification with a DNA polymerase using a DNA from organisms, containing genes coding for hydroxynitrile lyase, as templates and cloning, and also recombinant proteins which can be prepared in suitable host cells by heterologous expression of the DNA sequence of said HNL genes, and proteins and fusion proteins derived therefrom and use of said proteins for preparing (R)- or (S)-cyanohydrins.

Abstract: Nucleic acids encoding cytochrome P450 variants are provided. The cytochrome P450 variants of have a higher alkane-oxidation capability, alkene-oxidation capability, and/or a higher organic-solvent resistance than the corresponding wild-type or parent cytochrome P450 enzyme. A preferred wild-type cytochrome P450 is cytochrome P450 BM-3. Preferred cytochrome P450 variants include those having an improved capability to hydroxylate alkanes and epoxidate alkenes comprising less than 8 carbons, and have amino acid substitutions corresponding to V78A, H236Q, and E252G of cytochrome P450 BM-3. Preferred cytochrome P450 variants also include those having an improved hydroxylation activity in solutions comprising co-solvents such as DMSO and THF, and have amino acid substitutions corresponding to T235A, R471A, E494K, and S1024E of cytochrome P450 BM-3.