Glycosyltransferase family 47 (GT47) proteins in plants and animals

Zhang, Liang; Prabhakar, Pradeep Kumar; Bharadwaj, Vivek S; Bomble, Yannick J; Peña, Maria J; Urbanowicz, Breeanna R

doi:10.1042/ebc20220152

Title: Glycosyltransferase family 47 (GT47) proteins in plants and animals

Journal Article · Fri Apr 14 00:00:00 EDT 2023 · Essays in Biochemistry

DOI:https://doi.org/10.1042/ebc20220152· OSTI ID:1969274

Zhang, Liang ^[1]; Prabhakar, Pradeep Kumar ^[1];

^[2]; Bomble, Yannick J ^[3]; Peña, Maria J ^[1];

^[1]

University of Georgia, Athens, GA (United States)
National Renewable Energy Laboratory (NREL), Golden, CO (United States). Renewable Resources and Enabling Science Center
National Renewable Energy Laboratory (NREL), Golden, CO (United States)

Glycosyltransferases (GTs) are carbohydrate-active enzymes that are encoded by the genomes of organisms spanning all domains of life. GTs catalyze glycosidic bond formation, transferring a sugar monomer from an activated donor to an acceptor substrate, often another saccharide. GTs from family 47 (GT47, PF03016) are involved in the synthesis of complex glycoproteins in mammals and insects and play a major role in the synthesis of almost every class of polysaccharide in plants, with the exception of cellulose, callose, and mixed linkage β-1,3/1,4-glucan. GT47 enzymes adopt a GT-B fold and catalyze the formation of glycosidic bonds through an inverting mechanism. Unlike animal genomes, which encode few GT47 enzymes, plant genomes contain 30 or more diverse GT47 coding sequences. With our current knowledge of the GT47 family across plant species brings us an interesting view, showcasing how members exhibit a great diversity in both donor and acceptor substrate specificity, even for members that are classified in the same phylogenetic clade. Thus, we discuss how plant GT47 family members represent a great case to study the relationship between substrate specificity, protein structure, and protein evolution. Most of the plant GT47 enzymes that are identified to date are involved in biosynthesis of plant cell wall polysaccharides, including xyloglucan, xylan, mannan, and pectins. This indicates unique and crucial roles of plant GT47 enzymes in cell wall formation. The aim of this review is to summarize findings about GT47 enzymes and highlight new challenges and approaches on the horizon to study this family.

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Research Organization:: National Renewable Energy Laboratory (NREL), Golden, CO (United States); Univ. of Georgia, Athens, GA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC36-08GO28308; SC0023223; SC0015662

OSTI ID:: 1969274

Alternate ID(s):: OSTI ID: 1972478

Report Number(s):: NREL/JA-2800-85168; MainId:85941; UUID:8b496376-37c0-42a1-9030-32457b8ace44; MainAdminID:69265

Journal Information:: Essays in Biochemistry, Vol. 67, Issue 3; ISSN 0071-1365

Publisher:: Portland PressCopyright Statement

Country of Publication:: United States

Language:: English

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
CAZyme
duckweed
glycosyltransferases
GT-47
molecular modeling
carbohydrate-active enzyme
exostosin
glycosaminoglycan
Glycosyltransferase
GT47
PF03016

Title: Glycosyltransferase family 47 (GT47) proteins in plants and animals

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