Dual-specificity phosphatase (DUSP; DSP) is a form of phosphatase that can act upon tyrosine or serine/threonine residues. There are several families of dual-specificity phosphatase enzymes in mammals. All share a similar catalytic mechanism, by which a conserved cysteine residue forms a covalent intermediate with the phosphate group to be eliminated. The residues surrounding their catalytic core obey a rather strict consensus: His-Cys-x-x-x-x-x-Arg-Ser. The serine side chain and an additional conserved aspartate play a central role in the elimination of the Cys-linked intermediate, thus completing their enzymatic cycle. The main difference between tyrosine-specific phosphatases and dual-specificity phosphatases lies in the width of the latter enzymes' catalytic pocket: thus they can accom
Attributes | Values |
---|---|
rdf:type |
|
rdfs:label |
|
rdfs:comment |
|
dcterms:subject | |
Wikipage page ID |
|
Wikipage revision ID |
|
Link from a Wikipage to another Wikipage | |
sameAs | |
dbp:wikiPageUsesTemplate | |
has abstract |
|
gold:hypernym | |
prov:wasDerivedFrom | |
page length (characters) of wiki page |
|
foaf:isPrimaryTopicOf | |
is Link from a Wikipage to another Wikipage of | |
is Wikipage redirect of | |
is Wikipage disambiguates of | |
is foaf:primaryTopic of |