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Physiological roles of plant glycoside hydrolases

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Abstract

The functions of plant glycoside hydrolases and transglycosidases have been studied using different biochemical and molecular genetic approaches. These enzymes are involved in the metabolism of various carbohydrates containing compounds present in the plant tissues. The structural and functional diversity of the carbohydrates implies a vast spectrum of enzymes involved in their metabolism. Complete genome sequence of Arabidopsis and rice has allowed the classification of glycoside hydrolases in different families based on amino acid sequence data. The genomes of these plants contain 29 families of glycoside hydrolases. This review summarizes the current research on plant glycoside hydrolases concerning their principal functional roles, which were attributed to different families. The majority of these plant glycoside hydrolases are involved in cell wall polysaccharide metabolism. Other functions include their participation in the biosynthesis and remodulation of glycans, mobilization of energy, defence, symbiosis, signalling, secondary plant metabolism and metabolism of glycolipids.

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Abbreviations

ABA:

Abscisic acid

AGP:

Arabinogalactan protein

DBE:

Starch-debranching enzyme

DIBOA:

2,4-Dihydroxy-1,4-benzoxazin-3-one

DIMBOA:

2,4-Dihydroxy-7-methoxy -1,4-benzoxazin-3-one

CAZY:

Carbohydrate-active enzymes

Endo H:

Endoglucosaminidase

ER:

Endoplasmatic reticulum

IAA:

Indole-3-acetic acid

GE:

β-Glucan elicitor

GEBP:

Glucan elicitor binding protein

GH:

Glycoside hydrolase

GT:

Glycosyltransferase

GUS:

β-d-Glucuronidase

NF:

Nod factor

PG:

Polygalacturonase

PR:

Pathogenesis-related

XET:

Xyloglucan endotransglucosylase

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Acknowledgments

I wish to thank Dr. Guy Hervé and Leanne Enns for the critical review of the manuscript. I thank two anonymous reviewers for their helpful comments and suggestions for improving the manuscript.

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    Zoran Minic

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Minic, Z. Physiological roles of plant glycoside hydrolases. Planta 227, 723–740 (2008). https://doi.org/10.1007/s00425-007-0668-y

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