Engineering the thermostability of d-lyxose isomerase from Caldanaerobius polysaccharolyticus via multiple computer-aided rational design for efficient synthesis of d-mannose

Rational engineering of homospermidine synthase for enhanced catalytic efficiency toward spermidine synthesis

“…In recent years, protein engineering has emerged as a powerful strategy for obtaining target catalysts. Several studies have utilized molecular modification to successfully alter enzyme properties such as catalytic activity, stability, and selectivity [ [14] , [15] , [16] ]. Bv HSS consists of 477 amino acids, and its crystal structure has been identified as a dimer (Protein Data Bank [PDB] ID: 4PLP), with each monomer containing its own catalytically active center and NAD + binding site [ 17 ].…”

Computer‐aided design to enhance the stability of aldo‐keto reductase KdAKR

“…incorporated PROSS into the rational design strategy, increasing the melting temperature of lipase from Pseudomonas alcaligenes by 14 • C. [23] PROSS has been widely used to enhance the stability of enzymes by using structure models predicted by SWISS-MODEL or AlphaFold 2, such as D-lyxose isomerase, alginate lyase and βglucosidase. [24][25][26] In our previous study, we constructed an AKR mutant KdAKR M6 (KdAKR-Y28A/L58I/I63L/G223P/Y296W/W297H) from Kluyveromyces dobzhanskii, which had strict stereoselectivity and enhanced activity toward t-butyl 6-chloro-(5S)-hydroxy-3-oxohexanoate ((5S)-CHOH) (Figure 1A). Herein, we employed PROSS to predict potentially stable mutants of KdAKR M6 .…”