Biology:Histidine—tRNA ligase
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histidine-tRNA ligase | |||||||||
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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 | ||||||||
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In enzymology, a histidine-tRNA ligase (EC 6.1.1.21) is an enzyme that catalyzes the chemical reaction
- ATP + L-histidine + tRNAHis [math]\displaystyle{ \rightleftharpoons }[/math] AMP + diphosphate + L-histidyl-tRNAHis
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.
See also
- Anti-Jo1
References
- "Histidyl transfer ribonucleic acid synthetase from bakers' yeast". Can. J. Biochem. 45 (7): 1067–74. 1967. doi:10.1139/o67-123. PMID 6035970.
Original source: https://en.wikipedia.org/wiki/Histidine—tRNA ligase.
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