10 April 2017: A classic GH family:
The Glycoside Hydrolase Family 22
page was completed today by Spencer Williams
, with editorial input from Responsible Curator David Vocadlo
contains the classic bacterial peptidoglycan hydrolase, hen egg-white lysozyme (HEWL), the first enzyme for which the three-dimensional structure was solved (reported in 1965). Moreover, seminal enzyme-carbohydrate complex structures have made HEWL a paradigm for glycosidases that operate through the classical Koshland retaining mechanism
. Although the nature of the reaction intermediate remained contentious for many years since the original proposal of an oxacarbenium ion-carboxylate pair, a definitive study by Vocadlo
, Laine, and Withers
resolved the covalent nature of the glycosyl-enzyme HEWL in 2001, thus bringing mechanistic understanding of this classic enzyme in concordance with other retaining
GH families. The lysozyme fold of HEWL defines the archetype for other hexosaminidases (i.e. those of GH19
) and the non-catalytic alpha-lactalbumins, and this fold notably has also been observed in recently emergent families of cellulases (GH124
) and mannanases (GH134
). Find out more about this classic GH family here!
2 December 2016: A new CAZyme-specific journal: The journal Amylase has been recently launched under the editorial leadership of Stefan Janecek and a number of other CAZypedians, including Bernard Henrissat, Magali Remaud-Simeon, Birte Svensson, Pedro Coutinho, and Leila LoLeggio. Amylase is an open access journal that will focus on the biochemistry and biotechnology of starch hydrolases and related alpha-glucan-active enzymes, such as those from GH13, GH70, and GH77 (Clan GH-H), as well as GH57, GH119, GH14, GH15, and GH31. Visit the Amylase homepage for more information on the scope of the journal and details on how to submit manuscripts for publication.
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