Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Oxidoreductase
Patent
1997-11-24
1999-12-21
Wax, Robert A.
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Oxidoreductase
435132, 435147, 435148, 435155, 435156, 536 232, C12N 902, C12P 724, C12P 722, C07H 2104
Patent
active
060047895
ABSTRACT:
A process for obtaining a pyruvate decarboxylase by isolation from a producer organism. The pyruvate decarboxylase is capable of forming (R)-(-)-phenylacetylcarbinole (I) in .gtoreq.95% enantiomer unit with a product ratio of (I) to 2-hydoxypropiophenone of .gtoreq.95%. In addition, the pyruvate decarboxylase has a specific activity with regard to phenylacetylcarbinole formation of >1U/mg. It is the aim of the invention to obtain a pyruvate decarboxylase with improved synthesis capacity concerning the formation of (R)-(-)-phenylacetylcarbinole. The process of the invention developed for this purpose is characterized in that use is made of a producing organism with a gene coding for pyruvate decarboxylase from Zymomonas mobilis, in the DNA sequence of which the tryptophane radical coding codon TGG is replaced at position 1174-1176 by a codon which codes for an amino acid radical with a reduced volume ratio.
REFERENCES:
Eur J. Biochem, Dec. 1, 1995, 234(2) P650-5, Germany, XP000607025, Bruhn et al., "The Replacement of Trp392 By Alanine Infulences The Cecarboxylase/Carboligase From Zymomonas mobilis." p. 63.
Eur. J. Biochem, Sep. 1, 1994 224(2) P651-61, Germany, XP000607136, Pohl M. et al, "Reversible Dissociation and Unfolding of Pyruvate Decarboxylase From Zymomonas mobilis", p. 658.
Eur. J. Biochem, 1994, Germany, Candy et al., XP 000607055, Investigation of The Cofactor-Binding Site of Zymomonas mobilis, "Pyruvate Decarboxylase by Site-Directed Mutagenesis".
Crout et al., "Applications of Hydrolytic and Decarboxylating Enzymes in Biotransformations", 1994, vol. 9, pp. 1-30.
Bruhn Heike
Kula Maria-Regina
Mesch Karin
Pohl Martina
Bach Klaus J.
Forschungszentrum Julich GmbH
Stole Einar
Wax Robert A.
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