Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.2.48 extracted from

  • Kagawa, W.; Arai, T.; Ishikura, S.; Kino, K.; Kurumizaka, H.
    Structure of RizA, an L-amino-acid ligase from Bacillus subtilis (2015), Acta Crystallogr. Sect. F, 71, 1125-1130.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.2.48

Cloned(Commentary)

Cloned (Comment) Organism
gene rizA, overexpression of selenomethionine-substituted enzyme in Escherichia coli strain B834(DE3) Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified selenomethionine-substituted, substrate-free enzyme, X-ray diffraction structure determination and analysis Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-arginine + an L-amino acid Bacillus subtilis
-
 ADP + phosphate + an L-arginyl-L-amino acid
-
 ?
ATP + L-arginine + an L-amino acid Bacillus subtilis NBRC3134
-
 ADP + phosphate + an L-arginyl-L-amino acid
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis B5UAT8 gene rizA
-
Bacillus subtilis NBRC3134 B5UAT8 gene rizA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant selenomethionine-substituted enzyme from Escherichia coli strain B834(DE3) by anion exchange and hydrophobic interaction chromatography, ultrafiltration, gel filtration, another different step of anion exchange chromatography, and ultrafiltration Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-arginine + an L-amino acid
-
 Bacillus subtilis ADP + phosphate + an L-arginyl-L-amino acid
-
 ?
ATP + L-arginine + an L-amino acid RizA exhibits strict substrate specificity for arginine as the N-terminal amino acid of the synthesized dipeptide, substrate binding site structure analysis, overview Bacillus subtilis ADP + phosphate + an L-arginyl-L-amino acid
-
 ?
ATP + L-arginine + an L-amino acid
-
 Bacillus subtilis NBRC3134 ADP + phosphate + an L-arginyl-L-amino acid
-
 ?
ATP + L-arginine + an L-amino acid RizA exhibits strict substrate specificity for arginine as the N-terminal amino acid of the synthesized dipeptide, substrate binding site structure analysis, overview Bacillus subtilis NBRC3134 ADP + phosphate + an L-arginyl-L-amino acid
-
 ?

Synonyms

Synonyms Comment Organism
RizA
-
 Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
ATP ATP binding site structure analysis, overview Bacillus subtilis

General Information

General Information Comment Organism
evolution the enzyme is a member of the ATP-dependent carboxylate-amine/thiol ligase superfamily Bacillus subtilis
metabolism L-amino-acid ligase RizA from Bacillus subtilis participates in the biosynthesis of the oligopeptide antibiotic rhizocticin Bacillus subtilis
additional information L-amino acid ligases contain the ATP-grasp fold, which is composed of three conserved domains referred to as the A-domain (N-terminal domain), the B-domain (central domain) and the C-domain (C-terminal domain). These three domains commonly grasp the ATP molecule, and also provide binding sites for the Mg2+ ion and the amino-acid substrate Bacillus subtilis