A novel amidase (half-amidase) for half-amide hydrolysis involved in the bacterial metabolism of cyclic imides

Article Abstract:

An amidase, named 'half-amidase,' that catalyzes the second step of cyclic imide transformation has been reported. It is involved in the half-amide hydrolysis that is part of the bacterial metabolism of cyclic imides, for which it is highly specific.

Bacteria, Protein engineering, Cyclic compounds, Histidine, Amides

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Construction of deoxyriboaldolase-overexpressing Escherichia coli and its application to 2-deoxyribose 5-phosphate synthesis from glucose and acetaldehyde for 2'-deoxyribonucleoside production

Article Abstract:

Results demonstrate that 2-deoxyribose 5-phosphate is produced by deoxyriboaldolase encoding gene of Klebsiella pneumoniae, which is overexpressed in Escherichia coli, in the presence of ATP using glucose and acetaldehyde. Data indicate that under the optimal conditions, 100 millimolar 2-deoxyribose 5-phosphate is produced, which is further transformed to 2'-deoxyribonucleoside.

Science & research, Analysis, Genetic aspects, Microbiological synthesis, Gene expression, Antisense drugs, Deoxyribonucleotides, Deoxynucleotides

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Cyclic-imide-hydrolyzing activity of D-hydantoinase from Blastobacter sp. strain A17p-4

Article Abstract:

A study of the cyclic-imide-hydrolyzing activity of a prokaryotic cyclic-ureide-hydrolyzing enzyme, D-hydantoinase, revealed that its structure, physico-chemical properties and NH2-terminal amino acid sequence similar to other reported bacterial D-hydantoinases. It showed the highest catalytic efficiency toard dihydropyrimidines and was induced by dihydropyrimidines. These imply that the cyclic-imide-hydrolyzing activity of D-hydantoinase might likewise be a general property of bacterial D-hydantoinases identical to dihydropyrimidinase.

Hydrolysis, Enzyme structure-activity relationships, Pyrimidines

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