http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID438543
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | dimerization/docking (D/D) domain found in enolase 4 and similar proteins. Enolase (EC 4.2.1.11), also known as phosphopyruvate hydratase, is a metalloenzyme responsible for the catalyzing the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. ENO4, also called 2-phospho-D-glycerate hydro-lyase, may be required for sperm motility and function. It contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1. |
| title | DD_ENO4 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 8.