Artificial Thermostable D-Amino Acid Dehydrogenase: Creation and Application
نویسندگان
چکیده
منابع مشابه
An amperometric D-amino acid biosensor prepared with a thermostable D-proline dehydrogenase and a carbon nanotube-ionic liquid gel.
Carbon nanotube (CNT) gel, which is composed of a mixture of single-wall CNT, an ionic liquid, and a thermostable D-proline dehydrogenase (D-Pro DH) immobilized electrode was utilized for the determination of D-amino acids (DAAs) in food samples. When a critical comparison with CNT, Ketjen Black (KB), and carbon powder (CP) was also carried out, the CNT/D-Pro DH immobilized electrode showed the...
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D-amino acid aminotransferases (D-AATs) from Geobacillus toebii SK1 and Geobacillus sp. strain KLS1 were cloned and characterized from a genetic, catalytic, and structural aspect. Although the enzymes were highly thermostable, their catalytic capability was approximately one-third of that of highly active Bacilli enzymes, with respective turnover rates of 47 and 55 s(-1) at 50 degrees C. The Ge...
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D-Arginine dehydrogenase (DADH) is a flavin-dependent enzyme that requires FAD as a cofactor for catalysis (1). It is found in Pseudomonas aeruginosa, a common opportunistic human pathogen (2). DADH catalyzes the oxidation of D-arginine to iminoarginine, which is subsequently converted to ketoarginine and ammonia in solution (1). Previous studies have established that the enzyme is active on al...
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The single amino acid replacement of Tyr52 with Leu drastically increased the activity of Lactobacillus pentosus NAD-dependent D-lactate dehydrogenase toward larger aliphatic or aromatic 2-ketoacid substrates by 3 or 4 orders of magnitude and decreased the activity toward pyruvate by about 30-fold, converting the enzyme into a highly active D-2-hydroxyisocaproate dehydrogenase.
متن کاملSpin label studies on the flavoproteins lipoamide dehydrogenase and D-amino acid oxidase.
Maleimide spin label was covalently bound to sulfhydryl residues of D-amino acid oxidase and lipoamide dehydrogenase. Labeling of native D-amino acid oxidase resulted in a non-homogeneous EPR-spectrum, which consisted of 4 moles of spin label bound immobile to the enzyme (mol.-weight 90.000). A detailed analysis of the spectrum, the kinetics of the reaction of the spin label with the protein an...
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ژورنال
عنوان ژورنال: Frontiers in Microbiology
سال: 2018
ISSN: 1664-302X
DOI: 10.3389/fmicb.2018.01760