6.1.1.19: arginine-tRNA ligase

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For detailed information about arginine-tRNA ligase, go to the full flat file.

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Synonyms

Arg-tRNA synthetase, Arginine translase, Arginine--tRNA ligase, Arginine-tRNA synthetase, Arginyl transfer ribonucleic acid synthetase, Arginyl-transfer RNA synthetase, Arginyl-tRNA synthetase, arginyl�tRNA synthetase, ArgRS, ArgS2, MtArgRS, RARS, RARS2, RRS, Synthetase, arginyl-transfer ribonucleate

ECTree

     6 Ligases

         6.1 Forming carbon-oxygen bonds

             6.1.1 Ligases forming aminoacyl-tRNA and related compounds

                6.1.1.19 arginine-tRNA ligase

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Results	in table
7	Activating Compound
54070	AA Sequence
1	CAS Registry Number
28	Cloned(Commentary)
26	Cofactor
12	Crystallization (Commentary)
122	Disease/ Diagnostics
3	Expression
4	General Information
8	General Stability
2	IC50 Value
34	Inhibitors
12	kcat/KM [mM/s]
2	Ki Value [mM]
132	KM Value [mM]
9	Localization
15	Metals/Ions
30	Molecular Weight [Da]
24	Natural Substrates/ Products (Substrates)
291	Organism
4	Pathway
28	PDB ID
9	pH Optimum
1	pH Range
2	pI Value
2	Posttranslational Modification
33	Protein Variants
38	Purification (Commentary)
9	Reaction
8	Reaction Type
85	Reference
21	Source Tissue
21	Specific Activity [micromol/min/mg]
4	Storage Stability
103	Substrates and Products (Substrate)
26	Subunits
63	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
3	Temperature Range [°C]
8	Temperature Stability [°C]
42	Turnover Number [1/s]

Inhibitors

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Inhibitors on EC 6.1.1.19 - arginine-tRNA ligase

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2'-methoxyadenosine 5'-triphosphate

Escherichia coli

-

-

280

2-Aminopurine riboside 5'-triphosphate

Escherichia coli

-

-

280

3'-Deoxyadenosine 5'-triphosphate

Saccharomyces pastorianus

-

-

273, 279

6-N-Benzyladenosine 5'-triphosphate

2 entries

8-azido-ATP

Escherichia coli

-

-

276

8-azidoadenosine 5'-triphosphate

Escherichia coli

-

-

280

8-bromoadenosine 5'-triphosphate

2 entries

adenosine 5'-[alpha,beta-methylene]triphosphate

Saccharomyces pastorianus

-

-

257

ADP

Geobacillus stearothermophilus

-

-

278

AMP

Mycolicibacterium smegmatis

-

-

284

argininosuccinate

Escherichia coli

-

-

269

Arginyl hydroxamate

Saccharomyces pastorianus

-

-

257

citrulline

Escherichia coli

-

-

269

diphosphate

2 entries

hemin

2 entries

homoarginine

Escherichia coli

-

-

276

K2SO4

Escherichia coli

-

45 mM

672397

KCl

2 entries

NaCl

Canavalia ensiformis

B2G3G6

50% inhibition at 100 mM, recombinant HIS-/thioredoxin-tagged enzyme

694971

ornithine

Escherichia coli

-

-

269

p-hydroxymercuribenzoate

Escherichia coli

-

tRNA or DTT protects against heat inactivation

276

Periodate-oxidized tRNA

2 entries

-

purine riboside

Escherichia coli

-

-

280

purine-riboside 5'-triphosphate

Saccharomyces pastorianus

-

-

273

RNA minihelix

Cricetulus sp.

-

-

661183

-

RNAi

Caenorhabditis elegans

Q19825

-

706759

-

6-N-Benzyladenosine 5'-triphosphate

Escherichia coli

-

-

280

6-N-Benzyladenosine 5'-triphosphate

Saccharomyces pastorianus

-

-

279

8-bromoadenosine 5'-triphosphate

Escherichia coli

-

-

280

8-bromoadenosine 5'-triphosphate

Saccharomyces pastorianus

-

-

273, 279

diphosphate

Mycolicibacterium smegmatis

-

-

284

diphosphate

Rattus norvegicus

-

50% inhibition at 0.033 mM (free enzyme), at 0.040 (complexed enzyme)

283

hemin

Homo sapiens

-

hemin is a protoporphyrin containing a ferric iron in the center. ArgRS Cys115 acts as a specific axial ligand of hemin binding that is located in the Add1 domain, but hemin binding to Cys115 is not responsible for the inhibition of enzymatic activity. Hemin inhibits the catalytic activity of full-length and N-terminal 72-amino acid-truncated hcArgRSs by blocking amino acid activation. Hemin induces oligomerization of both the isolated Add1 domain and the wild type enzyme, which might account for the inhibition of catalytic activity. Km values for tRNAArg, arginine, and ATP in the presence of hemin are not altered, but kcat values dramatically decrease compared with those in the absence of hemin, kinetic analysis, overview

715565

hemin

Plasmodium falciparum

Q8I5M2

hemin induces a dimeric form of the enzyme that is thus rendered enzymatically dead as it is unable to recognize its cognate tRNAarg

746516

KCl

Escherichia coli

-

-

672397

KCl

Rattus norvegicus

-

50% inhibition: at 150 mM (free enzyme), at 180 mM (complexed enzyme)

283

Periodate-oxidized tRNA

Escherichia coli

-

mixed type non-competitive, irreversible

275

-

Periodate-oxidized tRNA

Geobacillus stearothermophilus

-

-

278

-