Microbial Glucuronoyl Esterases: 10 Years after Discovery.
A carbohydrate esterase called glucuronoyl esterase (GE) was discovered 10 years ago in a cellulolytic system of the wood-rotting fungus Schizophyllum commune Genes coding for GEs were subsequently found in a number of microbial genomes, and a new family of carbohydrate esterases (CE15) has been established. The multidomain structures of GEs, together with their catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass, led to the view that the esterases evolved for hydrolysis of the ester linkages between 4-O-methyl-d-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. This idea of the function of GEs is further supported by the effects of cloning of fungal GEs in plants and by very recently reported evidence for changes in the size of isolated lignin-carbohydrate complexes due to uronic acid de-esterification. These facts make GEs interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants. This article is a brief summary of current knowledge of these relatively recent and unexplored esterases.
Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovakia chempbsa@savba.sk.
Peter
P
Biely
D004950:Esterases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020723:Glucuronic Acid / Q000378:metabolism; D008958:Models, Molecular; D012567:Schizophyllum / Q000737:chemistry / Q000145:classification / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
D005656:Fungal Proteins; D020723:Glucuronic Acid; D004950:Esterases
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