In this article we are going to address the topic of Dual-specificity kinase in a complete and detailed manner, with the aim of providing the reader with a deep and updated vision on this topic. From its origins to its evolution today, through its main characteristics, applications and possible impacts in different areas. Dual-specificity kinase is a topic of great relevance today, which not only arouses interest in experts and specialists, but also in a general public eager for knowledge. Therefore, in the following lines we will delve into its different aspects to offer an enriching and contextualized perspective on Dual-specificity kinase.
| Dual-specificity kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
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.
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).