ArticlePloS one2016
Biochemical Characterization of a Family 15 Carbohydrate Esterase from a Bacterial Marine Arctic Metagenome.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 34 citations in OpenAlex.
- Biochemical Characterization of Multimodular Xylanolytic Carbohydrate Esterases from the Marine Bacterium Flavimarina sp. Hel_I_48.Chembiochem : a European journal of chemical biology · 2025Article
- New insights to diversity and enzyme-substrate interactions of fungal glucuronoyl esterases.Applied microbiology and biotechnology · 2023Review
- Glucuronoyl esterases - enzymes to decouple lignin and carbohydrates and enable better utilization of renewable plant biomass.Essays in biochemistry · 2023Review
- Plastid Transformation: New Challenges in the Circular Economy Era.International journal of molecular sciences · 2022Review
- Mechanism and biomass association of glucuronoyl esterase: an α/β hydrolase with potential in biomass conversion.Nature communications · 2022Article
- A genomic view of the microbiome of coral reef demosponges.The ISME journal · 2021Article
- Bioprospecting of Novel Extremozymes From Prokaryotes-The Advent of Culture-Independent Methods.Frontiers in microbiology · 2021Review
- Comparative Genome Analysis of the Lignocellulose Degrading BacteriaFrontiers in microbiology · 2020Article
- Characterization of an acetyl xylan esterase from the marine bacterium Ochrovirga pacifica and its synergism with xylanase on beechwood xylan.Microbial cell factories · 2019Article
- Structure-function analyses reveal that a glucuronoyl esterase fromThe Journal of biological chemistry · 2019Article
- Characterisation of a Hydroxycinnamic Acid Esterase From theFrontiers in microbiology · 2018Article
- Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion.Biotechnology for biofuels · 2018Article
- Structural insight into a CE15 esterase from the marine bacterial metagenome.Scientific reports · 2017Article
- Optimization of a metatranscriptomic approach to study the lignocellulolytic potential of the higher termite gut microbiome.BMC genomics · 2017Article
- Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds.Applied microbiology and biotechnology · 2017Article
- Comparative Metagenomics of Cellulose- and Poplar Hydrolysate-Degrading Microcosms from Gut Microflora of the Canadian Beaver (Frontiers in microbiology · 2017Article
- A New Functional Classification of Glucuronoyl Esterases by Peptide Pattern Recognition.Frontiers in microbiology · 2017Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundThe glucuronoyl esterase enzymes of wood-degrading fungi (Carbohydrate Esterase family 15; CE15) form part of the hemicellulolytic and cellulolytic enzyme systems that break down plant biomass, and have possible applications in biotechnology. Homologous enzymes are predicted in the genomes of several bacteria, however these have been much less studied than their fungal counterparts. Here we describe the recombinant production and biochemical characterization of a bacterial CE15 enzyme denoted MZ0003, which was identified by in silico screening of a prokaryotic metagenome library derived from marine Arctic sediment. MZ0003 has high similarity to several uncharacterized gene products of polysaccharide-degrading bacterial species, and phylogenetic analysis indicates a deep evolutionary split between these CE15s and fungal homologs.
resultsMZ0003 appears to differ from previously-studied CE15s in some aspects. Some glucuronoyl esterase activity could be measured by qualitative thin-layer chromatography which confirms its assignment as a CE15, however MZ0003 can also hydrolyze a range of other esters, including p-nitrophenyl acetate, which is not acted upon by some fungal homologs. The structure of MZ0003 also appears to differ as it is predicted to have several large loop regions that are absent in previously studied CE15s, and a combination of homology-based modelling and site-directed mutagenesis indicate its catalytic residues deviate from the conserved Ser-His-Glu triad of many fungal CE15s. Taken together, these results indicate that potentially unexplored diversity exists among bacterial CE15s, and this may be accessed by investigation of the microbial metagenome. The combination of low activity on typical glucuronoyl esterase substrates, and the lack of glucuronic acid esters in the marine environment suggest that the physiological substrate of MZ0003 and its homologs is likely to be different from that of related fungal enzymes.
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