http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID176518
Outgoing Links
Predicate | Object |
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abstract | Glycerophosphodiester phosphodiesterase-like domain of spider venom sphingomyelinases D, bacterial phospholipase D, and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase-like domain (GDPD-like) present in sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.4) from spider venom, the Corynebacterium pseudotuberculosis Phospholipase D (PLD)-like protein from pathogenic bacteria, and the Ajellomyces capsulatus H143 PLD-like protein from ascomycetes. Spider SMases D and bacterial PLD proteins catalyze the Mg2+-dependent hydrolysis of sphingomyelin producing choline and ceramide 1-phosphate (C1P), which possess a number of biological functions, such as regulating cell proliferation and apoptosis, participating in inflammatory responses, and playing a key role in phagocytosis. In the presence of Mg2+, SMases D can function as lysophospholipase D and hydrolyze lysophosphatidylcholine (LPC) to choline and lysophosphatidic acid (LPA), which is a multifunctional phospholipid involved in platelet aggregation, endothelial hyperpermeability, and pro-inflammatory responses. Loxosceles spider venoms' SMases D are the principal toxins responsible for dermonecrosis and complement dependent haemolysis induced by spider venom. Due to amino acid substitutions at the entrance to the active-site pocket, some members lack activity. The typical GDPD domain consists of a TIM barrel and a small insertion domain named as the GDPD-insertion (GDPD-I) domain, which is specific for GDPD proteins. Although proteins in this family contain a non-typical GDPD domain which lacks the GDPD-I, their catalytic mechanisms are based on Mg2+-dependent acid-base reactions similar to GDPD proteins. They might be divergent members of the GDPD family. Moreover, this family does not belong to phospholipase D (PLD) superfamily, since it lacks the conserved HKD sequence motif that characterizes the catalytic center of the PLD superfamily. It belongs to the superfamily of PLC-like phosphodiesterases. |
title | GDPD_like_SMaseD_PLD |
isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7039350 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19211488 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22746753 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/31517346 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2358592 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19877882 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3695945 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9211514 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16631805 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32166037 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14491950 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26139427 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/983166 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21896207 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8277128 |
type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 224.