Histidine—tRNA ligase
In enzymology, a histidine-tRNA ligase (EC 6.1.1.21) is an enzyme that catalyzes the chemical reaction
- ATP + L-histidine + tRNAHis AMP + diphosphate + L-histidyl-tRNAHis
| histidine-tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.1.1.21 | ||||||||
| CAS number | 9068-78-4 | ||||||||
| Alt. names | histidyl tRNA synthetase, Jo-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The 3 substrates of this enzyme are ATP, L-histidine, and tRNA(His), whereas its 3 products are AMP, diphosphate, and L-histidyl-tRNA(His).
This enzyme participates in histidine metabolism and aminoacyl-trna biosynthesis.
Nomenclature
Histidine—tRNA ligase belongs to the family of ligase enzymes, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-histidine:tRNAHis ligase (AMP-forming). Other names in common use include histidyl-tRNA synthetase, histidyl-transfer ribonucleate synthetase, and histidine translase.
gollark: Aren't they in Australia?
gollark: (But it would be totally possible to ban E2EE chat apps from stores)
gollark: (Obviously they can't entirely ban it)
gollark: It also seems to function as a plausibly deniable way to ban end to end encryption (it never mentions it explicitly but does have a mechanism to force technology companies to make their service amenable to centralised monitoring).
gollark: The UK government is also working on the incredibly ææææ "online safety bill", which obliges online things to ban "harmful content" (not illegal, "harmful").
See also
References
- von Tigerstrom M, Tener GM (1967). "Histidyl transfer ribonucleic acid synthetase from bakers' yeast". Can. J. Biochem. 45 (7): 1067–74. doi:10.1139/o67-123. PMID 6035970.
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