@article { ISI:000315947400041,
	title = {alpha-Galacturonidase(s): A new class of Family 4 glycoside hydrolases with strict specificity and a unique CHEV active site motif},
	journal = {FEBS LETTERS},
	volume = {587},
	number = {6},
	year = {2013},
	month = {MAR 18},
	pages = {799-803},
	abstract = {The catalytic activity of the Family 4 glycosidase LplD protein, whose active site motif is CHEV, is unknown despite its crystal structure having been determined in 2008. Here we identify that activity as being an alpha-galacturonidase whose natural substrate is probably alpha-1,4-di-galacturonate (GalUA(2)). Phylogenetic analysis shows that LplD belongs to a monophyletic clade of CHEV Family 4 enzymes, of which four other members are also shown to be galacturonidases. Family GH 4 enzymes catalyze the cleavage of the glycosidic bond, via a non-canonical redox-assisted mechanism that contrasts with Koshland{\textquoteright}s double-displacement mechanism. Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.},
	issn = {0014-5793},
	doi = {10.1016/j.febslet.2013.02.004},
	author = {Thompson, John and Pikis, Andreas and Rich, Jamie and Hall, Barry G. and Withers, Stephen G.}
}
