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Publication Abstract from PubMed

Glucosidases play key roles in many diseases and are limiting enzymes during cellulose degradation, which is an important part of global carbon cycle. Here, we identified a novel beta-glucosidase, CmGH1, isolated from marine bacterium Croceicoccus marinus E4A9(T). In spite of its high sequence and structural similarity with beta-xylosidase family members, CmGH1 had enzymatic activity toward p-nitrophenyl-beta-D-glucopyranoside (p-NPG) and cellobiose. The K m and K cat values of CmGH1 toward p-NPG were 0.332 +/- 0.038 mM and 2.15 +/- 0.081 min(-1), respectively. CmGH1 was tolerant to high concentration salts, detergents, as well as many kinds of organic solvents. The crystal structure of CmGH1 was resolved with a 1.8 A resolution, which showed that CmGH1 was composed of a canonical (alpha/beta)8-barrel catalytic domain and an auxiliary beta-sandwich domain. Although no canonical catalytic triad residues were found in CmGH1, structural comparison and mutagenesis analysis suggested that residues Gln157 and Tyr264 of CmGH1 were the active sites. Mutant Q157E significantly increased its hydrolase activity up to 15-fold, whereas Y264E totally abolished its enzymatic activity. These results might provide new insights into understanding the different catalytic mechanism during evolution for beta-glucosidases and beta-xylosidases.

Structural and Functional Insights Into CmGH1, a Novel GH39 Family beta-Glucosidase From Deep-Sea Bacterium.,Shen Y, Li Z, Huo YY, Bao L, Gao B, Xiao P, Hu X, Xu XW, Li J Front Microbiol. 2019 Dec 20;10:2922. doi: 10.3389/fmicb.2019.02922. eCollection , 2019. PMID:31921083^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.