Rhea- Annotated reactions database

Enzymes

UniProtKB ^help_outline	2,955 proteins
Enzyme class ^help_outline	EC 2.3.2.8 arginyltransferase
GO Molecular Function ^help_outline	GO:0004057 arginyltransferase activity

Reaction participants Show >> << Hide

Name^help_outline an N-terminal L-α-aminoacyl-[protein] Identifier RHEA-COMP:10636 Reactive part ^help_outline
- Name ^help_outline N-terminal L-α-amino-acid residue Identifier CHEBI:78597 Charge +1 Formula C2H4NOR SMILES^help_outline [NH3+][C@@H]([*])C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 4 reaction(s) Find proteins in UniProtKB for this molecule
Name^help_outline L-arginyl-tRNA^Arg Identifier RHEA-COMP:9673 Reactive part ^help_outline
- Name ^help_outline 3'-(L-arginyl)adenylyl group Identifier CHEBI:78513 Charge +1 Formula C16H26N9O7P SMILES^help_outline NC(=[NH2+])NCCC[C@H]([NH3+])C(=O)O[C@H]1[C@@H](O)[C@@H](O[C@@H]1COP([O-])(-*)=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 2 reaction(s) Find proteins in UniProtKB for this molecule
Name ^help_outline H⁺ Identifier CHEBI:15378 Charge +1 Formula H InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 8,755 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline N-terminal L-arginyl-L-amino acid-[protein] Identifier RHEA-COMP:10638 Reactive part ^help_outline
- Name ^help_outline N-terminal L-arginyl-L-α-amino acid residue Identifier CHEBI:83562 Charge +2 Formula C8H17N5O2R SMILES^help_outline NC(=[NH2+])NCCC[C@H]([NH3+])C(=O)N[C@@H]([*])C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 1 reaction(s) Find proteins in UniProtKB for this molecule
Name^help_outline tRNA^Arg Identifier RHEA-COMP:9658 Reactive part ^help_outline
- Name ^help_outline AMP 3'-end residue Identifier CHEBI:78442 Charge -1 Formula C10H12N5O6P SMILES^help_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(-*)=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 64 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 2 reaction(s) Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:10208	RHEA:10209	RHEA:10210	RHEA:10211
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	2,955 proteins	1 proteins
EC numbers ^help_outline	2.3.2.8
Gene Ontology ^help_outline	GO:0004057
KEGG ^help_outline				R03862
MetaCyc ^help_outline				ARGINYLTRANSFERASE-RXN

Publications

Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm.

Soffer R.L., Horinishi H.

J Mol Biol 43:163-175(1969) [PubMed] [EuropePMC]
Peptide acceptors in the arginine transfer reaction.

Soffer R.L.

J Biol Chem 248:2918-2921(1973) [PubMed] [EuropePMC]
Enzymatic modification of proteins. II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm.

Soffer R.L.

J Biol Chem 245:731-737(1970) [PubMed] [EuropePMC]

RHEA:10208 an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-tRNA(Arg) = H(+) + N-terminal L-arginyl-L-amino acid-[protein] + tRNA(Arg)

Enzymes

Reaction participants Show >> << Hide

Cross-references

Publications

Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm.

Peptide acceptors in the arginine transfer reaction.

Enzymatic modification of proteins. II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm.