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Enzymatic characterization of a thermostable 6-phosphogluconate dehydrogenase from and its application for NADH regeneration.
3 Biotech
January 2025
Yantai Key Laboratory of Characteristic Agricultural Bioresource Conservation and Germplasm Innovative Utilization, School of Life Sciences, Yantai University, Yantai, 264005 Shandong People's Republic of China.
Unlabelled: 6-Phosphogluconate dehydrogenases (6PGDHs) are widely existing as reduced cofactor (NADH/NADPH) regeneration biocatalysts. Herein, a thermostable 6PGDH from (Ht6PGDH) was overexpressed in and enzymologically characterized. Ht6PGDH exhibited exceptional stability and catalytic activity under high-temperature conditions, with an optimum temperature of 85 °C and the ability to maintain high activity for prolonged periods at 70 °C, which could be purified through a one-step heat treatment.
View Article and Find Full Text PDFRecent Advances of Oxalate Decarboxylase: Biochemical Characteristics, Catalysis Mechanisms, and Gene Expression and Regulation.
J Agric Food Chem
May 2024
School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, P. R. China.
Article Synopsis
- * The enzyme has potential applications in treating hyperoxaluria, processing low-oxalate foods, and as a diagnostic tool, yet there are unresolved questions about its interactions with substrates and how it acquires manganese ions.
- * The review discusses OXDC's biochemical characteristics, gene regulation, and catalytic mechanisms, while also analyzing data from the National Center for Biotechnology Information to discover new variants with different biochemical traits.
Thiolase: A Versatile Biocatalyst Employing Coenzyme A-Thioester Chemistry for Making and Breaking C-C Bonds.
Annu Rev Biochem
June 2023
Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland; email:
Thiolases are CoA-dependent enzymes that catalyze the thiolytic cleavage of 3-ketoacyl-CoA, as well as its reverse reaction, which is the thioester-dependent Claisen condensation reaction. Thiolases are dimers or tetramers (dimers of dimers). All thiolases have two reactive cysteines: () a nucleophilic cysteine, which forms a covalent intermediate, and () an acid/base cysteine.
View Article and Find Full Text PDFThe chemical modifications of starch granules have been adopted to improve the characteristics, viz., paste clarity, resistant starch content, thermal stability, and so forth. The modified starch has been applied as a biopolymer in developing various preparations of food, nutraceutical, and pharmaceutical importance.
View Article and Find Full Text PDFBetween Protein Fold and Nucleophile Identity: Multiscale Modeling of the TEV Protease Enzyme-Substrate Complex.
ACS Omega
November 2022
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia.
The cysteine protease from the tobacco etch virus (TEVp) is a well-known and widely utilized enzyme. TEVp's chymotrypsin-like fold is generally associated with serine catalytic triads that differ in terms of a reaction mechanism from the most well-studied papain-like cysteine proteases. The question of what dominates the TEVp mechanism, nucleophile identity, or structural composition has never been previously addressed.
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