Homoserine kinase
| Homoserine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Homoserine kinase tetramer, Methanocaldococcus jannaschii | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.1.39 | ||||||||
| CAS no. | 9026-58-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Homoserine kinase (EC 2.7.1.39) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from baker's yeast and Neurospora converts homoserine to O-phospho-L-homoserine by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). This is part of the biosynthetic pathway to the amino acid, threonine.[1][2]
This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-homoserine O-phosphotransferase. Other names in common use include homoserine kinase (phosphorylating), and HSK.[3]
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1FWK, PDB: 1FWL, PDB: 1H72, PDB: 1H73, PDB: 1H74, and PDB: 2PPQ.
References
- ↑ Watanabe, Yasushi; Konishi, Shimpachi; Shimura, Kensuke (1957). "Biosynthesis of Threonine from Homoserine". The Journal of Biochemistry. 44 (5): 299–307. doi:10.1093/oxfordjournals.jbchem.a126756.
- ↑ Flavin, Martin; Slaughter, Clarence (1960). "Purification and Properties of Threonine Synthetase of Neurospora". Journal of Biological Chemistry. 235 (4): 1103–1108. doi:10.1016/S0021-9258(18)69487-6. PMID 13823379.
- ↑ Enzyme 2.7.1.39 at KEGG Pathway Database.
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