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Enzyme From Wikipedia, the free encyclopedia
In biochemistry, a dual-specificity kinase (EC 2.7.12.1) is a kinase that can act as both tyrosine kinase and serine/threonine kinase.
Dual-specificity kinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.12.1 | ||||||||
CAS no. | 134549-83-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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MEKs, involved in MAP pathways, are principal examples of dual-specificity kinases. Other common examples include:
The systematic name of this enzyme class is ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating).
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