conserveddomain/PSSMID119335

Predicate	Object
abstract	Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
title	GH20_GcnA-like
isDiscussedBy	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11905448 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8527973 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1701917 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7223040
type	http://purl.obolibrary.org/obo/SO_0000417

Predicate	Subject
has component	http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ8WVB3 http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACC2EPN_A

Total number of triples: 9.