http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID319801
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase. Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. |
| title | HAD_PSP_eu |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9784554 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27419344 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13165778 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17317772 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6410543 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 14.