title: YNL134C from Saccharomyces cerevisiae encodes a novel protein with aldehyde reductase activity for detoxification of furfural derived from lignocellulosic biomass.
abstract: Furfural and 5-hydroxymethylfurfural (HMF) are the two main aldehyde compounds derived from pentoses and hexoses, respectively, during lignocellulosic biomass pretreatment. These two compounds inhibit microbial growth and interfere with subsequent alcohol fermentation. Saccharomyces cerevisiae has the in situ ability to detoxify furfural and HMF to the less toxic 2-furanmethanol (FM) and furan-2,5-dimethanol (FDM), respectively. Herein, we report that an uncharacterized gene, YNL134C, was highly up-regulated under furfural or HMF stress and Yap1p and Msn2/4p transcription factors likely controlled its up-regulated expression. Enzyme activity assays showed that YNL134C is an NADH-dependent aldehyde reductase, which plays a role in detoxification of furfural to FM. However, no NADH- or NADPH-dependent enzyme activity was observed for detoxification of HMF to FDM. This enzyme did not catalyse the reverse reaction of FM to furfural or FDM to HMF. Further studies showed that YNL134C is a broad-substrate aldehyde reductase, which can reduce multiple aldehydes to their corresponding alcohols. Although YNL134C is grouped into the quinone oxidoreductase family, no quinone reductase activity was observed using 1,2-naphthoquinone or 9,10-phenanthrenequinone as a substrate, and phylogenetic analysis indicates that it is genetically distant to quinone reductases. Proteins similar to YNL134C in sequence from S. cerevisiae and other microorganisms were phylogenetically analysed.
authors: Institute of Ecological and Environmental Sciences, College of Resources and Environmental Sciences, Sichuan Agricultural University, Wenjiang, Sichuan, People's Republic of China.
authors: Xianxian
authors: X
authors: Zhao
authors: Juan
authors: J
authors: Tang
authors: Xu
authors: X
authors: Wang
authors: Ruoheng
authors: R
authors: Yang
authors: Xiaoping
authors: X
authors: Zhang
authors: Yunfu
authors: Y
authors: Gu
authors: Xi
authors: X
authors: Li
authors: Menggen
authors: M
authors: Ma
mesh_terms: D000438:Alcohols / Q000378:metabolism; D000449:Aldehyde Reductase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism; D000595:Amino Acid Sequence; D005662:Furaldehyde / Q000032:analysis / Q000378:metabolism / Q000633:toxicity*; D008031:Lignin / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010802:Phylogeny; D012441:Saccharomyces cerevisiae / Q000145:classification / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000438:Alcohols; D000447:Aldehydes; D029701:Saccharomyces cerevisiae Proteins; D009243:NAD; C036909:lignocellulose; D008031:Lignin; D005662:Furaldehyde; D010088:Oxidoreductases; C586417:YNL134C protein, S cerevisiae; D000449:Aldehyde Reductase
keywords: Aldehyde reductase; Saccharomyces cerevisiae; detoxification; ethanol; furfural; lignocellulosic biomass