Structural highlights
FunctionPublication Abstract from PubMedCarbohydrates are complex macromolecules in biological metabolism. Enzymatic synthesis of carbohydrates is recognized as powerful tool to overcome the problems associated with large-scale synthesis of carbohydrates. Novel enzymes with significant transglycosylation ability are still in great demand in glycobiology studies. Here we report a novel glycoside hydrolase (GH) family 16 elongating beta-transglycosylase from Paecilomyces thermophila (PtBgt16A), which efficiently catalyzes the synthesis of higher polymeric oligosaccharides using beta-1,3/1,4 oligosaccharides as donor/acceptor substrates. Further structural information reveals that PtBgt16A own a binding pocket around the -1 subsite. The catalytic mechanism of PtBgt16A is partly similar to an exo- glycoside hydrolase, which cleaves the substrate from the non-reducing end one by one. However, PtBgt16A releases the reducing end product and uses remainder glucosyl as transglycosylation donor. This catalytic mechanism has similarity with the catalytic mode of amylosucrase, which leads the transglycosylation products gradually extend by one glucose unit. PtBgt16A thus has the potential to be a tool enzyme for the enzymatic synthesis of new beta-oligosaccharides and glycoconjugates. Catalytic mechanism of a novel glycoside hydrolase family 16 elongating beta - transglycosylase.,Qin Z, Yang S, Zhao L, You X, Yan Q, Jiang Z J Biol Chem. 2016 Dec 12. pii: jbc.M116.762419. PMID:27956553[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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