hymecromone and salicin

Thermostable enzymes derived from Thermotoga maritima have attracted worldwide interest for their potential industrial applications. Structural analysis and docking studies were preformed on T. maritima β-glucosidase enzyme with cellobiose and pNP-linked substrates. The 3D structure of the thermostable β-glucosidase was downloaded from the Protein Data Bank database. Substrates were downloaded from the PubCehm database and were minimized using MOE software. Docking of BglA and substrates was carried out using MOE software. After analyzing docked enzyme/substrate complexes, it was found that Glu residues were mainly involved in the reaction, and other important residues such as Asn, Ser, Tyr, Trp, and His were involved in hydrogen bonding with pNP-linked substrates. By determining the substrate recognition pattern, a more suitable β-glucosidase enzyme could be developed, enhancing its industrial potential.

Topics: Amino Acid Sequence; Benzyl Alcohols; beta-Glucosidase; Cellobiose; Glucosides; Hydrogen Bonding; Hymecromone; Kinetics; Molecular Conformation; Molecular Docking Simulation; Nitrophenylgalactosides; Software; Substrate Specificity; Thermotoga maritima

Four aryl-phospho-beta- d-glucosidases were identified in Bacillus subtilis by using 4-methylumbelliferyl-phospho-beta- d-glucopyranoside as a substrate. Two of these enzymes are the products of the bglA and bglH genes, previously suggested to encode aryl-phospho-beta- d-glucosidases, while the other enzymes are encoded by the yckE and ydhP genes. Together, these four genes account for >99.9% of the glucosidase activity in B. subtilis on aryl-phospho-beta- d-glucosides. yckE was expressed at a low and constant level during growth, sporulation, and spore germination, and was not induced by aryl-beta- d-glucosides. ydhP was also not induced by aryl-beta- d-glucosides. However, while ydhP was expressed at only a very low level in exponential-phase cells and germinating spores, this gene was expressed at a higher levels upon entry into the stationary phase of growth. Strains lacking yckE or ydhP exhibited no defects in growth, sporulation, or spore germination or in growth on aryl-beta- d-glucosides. However, a strain lacking bglA, bglH and yckE grew poorly if at all on aryl-beta- d-glucosides as the sole carbon source.

Topics: Arbutin; Bacillus subtilis; Benzyl Alcohols; Gene Expression Regulation, Bacterial; Genes, Bacterial; Glucose; Glucosidases; Glucosides; Hymecromone; Spores, Bacterial