FIELD: medicine.
SUBSTANCE: claimed is novel mutant oxidase of D-amino acids with higher temperature stability. Amino acid sequence of enzyme corresponds to amino acid sequence of oxidase of D-amino acids from Trigonopsis variabilis of wild type, in which tryptophan residue in position 46 is substituted with phenylalanine residue and cysteine residue in position 298 is substituted with alanine residue, and 6 last amino acids on C-end are replaced by novel sequence of 28 residues.
EFFECT: invention makes it possible to increase temperature stability of obtained mutant oxidase of D-amino acids in comparison with thermal stability of wild type enzyme.
2 dwg, 2 tbl, 4 ex
| Title | Year | Author | Number |
|---|---|---|---|
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|
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| MUTANT OXIDASE OF D-AMINO ACIDS (VERSIONS) | 2012 |
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|
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|
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|
RU2310687C1 |
| MUTANT FORMATE DEHYDROGENASE (VERSIONS) | 2012 |
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RU2522819C2 |
| MUTANT PLANT FORMATE DEHYDROGENASE (VERSIONS) | 2014 |
|
RU2557299C1 |
| MUTANT FORMATE DEHYDROGENASE (VERSIONS) | 2013 |
|
RU2545966C1 |
| RECOMBINANT DNA ENCODING FUNCTIONALLY ACTIVE HYBRID PROTEIN OF D-AMINO ACID OXYDASE WITH CHITIN-COUPLING DOMAIN (DAOcbd), pVR1 RECOMBINANT PLASMID PROVIDING SYNTHESIS THEREOF IN Escherichia coli CELLS AND RECOMBINANT Escherichia coli STRAIN C 41 (DE3)/pVR1 AS PRODUCER OF DAOcbd | 2006 |
|
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|
RU2312897C1 |
