The Mobility of the Cap Domain Is Essential for the Substrate Promiscuity of a Family IV Esterase from Sorghum Rhizosphere Microbiome
Year: 2023
Type: article
Abstract: A better understanding of structure-function relationships of enzymes allows revelation of key structural motifs or elements. Here, we studied the structural basis of the substrate promiscuity of EH 0 , a family IV esterase, isolated from a sample of the Sorghum bicolor rhizosphere microbiome exposed to technical cashew nut shell liquid.
DOI: 10.1128/aem.01807-22
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Awards: G100543663, G1218642281, G1363966722, G1855990336, G2030845156, G2262748287, G2309174360, G2465836362, G2601397997, G2673512141, G300979063, Microbial hitch-hikers of marine plastics: the survival, persistence & ecology of microbial communities in the Plastisphere, G330101941, G3456137197, G3480869486, G3518538256, G35757357, G3681454997, G3683909761, G3690828678, G4042783231, G410571670, G425668148, G430777504, G434337789, G4415506788, G4416174655, G451917667, G5080475149, G5421974903, G5787276900, G5805502524, G5913267992, G5967599077, G6492710620, Technologies of the Future for Low-Cost Enzymes for Environment-Friendly Products, G7613257594, G8401454605, G8430294048, G8684520763, G8765352115, G8787740968
OpenAlex ID: W4313544600
