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Publication Abstract from PubMed

The most extensively studied beta-d-galactosidases (EC3.2.1.23) belonging to four glycoside hydrolase (GH) families 1, 2, 35, and 42 are widely distributed among Bacteria, Archaea and Eukaryotes. Here, we report a novel GH35 family beta-galactosidase from the hyperthermophilic Thermoprotei archaeon Desulfurococcus amylolyticus (DabetaGal). Unlike fungal monomeric six-domain beta-galactosidases, the DabetaGal enzyme is a dimer; it has an extra jelly roll domain D7 and three composite domains (D4, D5, and D6) that are formed by the distantly located polypeptide chain regions. The enzyme possesses a high specificity for beta-d-galactopyranosides, and its distinguishing feature is the ability to cleave pNP-beta-d-fucopyranoside. DabetaGal efficiently catalyzes the hydrolysis of lactose at high temperatures, remains stable and active at 65 degrees capital ES, Cyrillic, and retains activity at 95 degrees capital ES, Cyrillic with a half-life time value equal to 73 min. These properties make archaeal DabetaGal a more attractive candidate for biotechnology than the widely used fungal beta-galactosidases.

The archaeal highly thermostable GH35 family beta-galactosidase DabetaGal has a unique seven domain protein fold.,Kil Y, Pichkur EB, Sergeev VR, Zabrodskaya Y, Myasnikov A, Konevega AL, Shtam T, Samygina VR, Rychkov GN FEBS J. 2024 Jun 2. doi: 10.1111/febs.17166. PMID:38825733^[1]

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