Identification and analysis of a unique group of glycoside hydrolase family 188 sequences with an altered sulfonate binding residue

Abstract

Sulfoquinovosyldiacylglycerol (SQDG) is a plant sulfolipid that plays a major role in the global sulfur cycle. Bacteria contain sulfoglycolytic pathways that are responsible for metabolizing SQDG which requires initial delipidation by a sulfolipase and sulfoquinovosidase (SQase). Recently, a new group of SQases was discovered and have been categorized in a separate glycoside hydrolase family (GH188). Here we have identified a subset of GH188s with an altered sulfonate binding residue. We found that these GH188s have a distinct dimer interface and are found in unique gene clusters that may represent new sulfoglycolytic pathways. Further investigation into these enzymes could broaden our understanding of this new glycoside hydrolase family and uncover diverse sulfoglycolytic pathways.