Characterization and identification of three novel aldo-keto reductases from Lodderomyces elongisporus for reducing ethyl 4-chloroacetoacetate.
Lodderomyces elongisporus LH703 isolated from soil samples contained three novel aldo-keto reductases (AKRs) (LEAKR 48, LEAKR 49, and LEAKR 50). The three enzymes were cloned, expressed, and purified to homogeneity for characterization. These three AKRs shared <40% amino acid identity with each other. LEAKR 50 was identified as a member of AKR3 family, whereas the other two LEAKRs were identified as members of two novel AKR families, respectively. All the three AKRs required nicotinamide adenine dinucleotide phosphate as a cofactor. However, they showed diverse characteristics, including optimum catalyzing conditions, resistance to adverse reaction conditions, and substrate specificity. LEAKR 50 was estimated to be a promising biocatalyst that could reduce ethyl 4-chloroacetoacetate with high enantiomeric excess (98% e. e.) and high activity residue under adverse conditions.
['Ning|Chenxi|C|', 'Su|Erzheng|E|', 'Wei|Dongzhi|D|']
D000090:Acetoacetates D000449:Aldehyde Reductase D000074408:Aldo-Keto Reductases D000595:Amino Acid Sequence D003001:Cloning, Molecular D005656:Fungal Proteins D008969:Molecular Sequence Data D009243:NAD D012442:Saccharomycopsis
Characterization Identification Lodderomyces elongisporus Ethyl 4-chloroacetoacetate Aldo–keto reductase