L-Rhamnose Dehydrogenase LraA of Aspergillus niger Shows High Substrate Specificity Matching Its Expression Profile
Agata Terebieniec, Li Xu, Mao Peng, Miia R. Mäkelä, Ronald P. de Vries

TL;DR
A fungal enzyme called LraA is highly specific to L-rhamnose, matching its expression and function in sugar metabolism.
Contribution
LraA shows unique high substrate specificity and expression profile, differing from other fungal sugar enzymes.
Findings
LraA is highly specific for L-rhamnose and inactive on other substrates.
LraA's expression is only significant on L-rhamnose.
LraA's specificity suggests a unique role in fungal sugar catabolism.
Abstract
L-rhamnose is one of the main monomeric sugars of rhamnogalacturonan I and II, which are polysaccharide components of pectin. In the ascomycete fungus Aspergillus niger it is metabolized through the non-phosphorylated L-rhamnose pathway, of which the first step is catalyzed by L-rhamnose dehydrogenase (LraA), converting L-rhamnose into L-rhamnono-γ-lactone. This enzyme belongs to PFAM PF00106, unlike most of other reductases/dehydrogenases involved in fungal sugar catabolism that are typically assigned to PF00248 and PF00107. The enzymes of those families have broad substrate specificity and in some cases have been shown to be involved in multiple pathways. In this study we heterologously produced and biochemically characterized A. niger LraA and studied its expression on a set of monosaccharides. This revealed that, in contrast to other metabolic redox enzymes, LraA is highly specific…
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Taxonomy
TopicsMicrobial Metabolites in Food Biotechnology · Polysaccharides and Plant Cell Walls · Plant nutrient uptake and metabolism
