title: Structural biology of glucan phosphatases from humans to plants.
abstract: Glucan phosphatases are functionally conserved at the enzymatic level, dephosphorylating glycogen in animals and starch in plants. The human glucan phosphatase laforin is the founding member of the family and it is comprised of a carbohydrate binding module (CBM) domain followed by a dual specificity phosphatase (DSP) domain. Plants encode two glucan phosphatases: Starch EXcess4 (SEX4) and Like Sex Four2 (LSF2). SEX4 contains a DSP domain followed by a CBM domain, while LSF2 contains a DSP domain and lacks a CBM. This review demonstrates how glucan phosphatase function is conserved and highlights how each family member employs a unique mechanism to bind and dephosphorylate glucan substrates.
authors: Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, United States. Electronic address: matthew.gentry@uky.edu.
authors: Matthew S
authors: MS
authors: Gentry
authors: Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, United States.
authors: M Kathryn
authors: MK
authors: Brewer
authors: Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, United States. Electronic address: craig.vanderkooi@uky.edu.
authors: Craig W
authors: CW
authors: Vander Kooi
mesh_terms: D000818:Animals; D005936:Glucans / Q000378:metabolism*; D006801:Humans; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D010766:Phosphorylation; D010944:Plants / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D005936:Glucans; D010744:Phosphoric Monoester Hydrolases