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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.48 Mg2+ required Bacillus subtilis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.48 Bacillus subtilis B5UAT8 gene rizA
-
6.3.2.48 Bacillus subtilis NBRC3134 B5UAT8 gene rizA
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.48 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.48 ATP + L-arginine + an L-amino acid
-
Bacillus subtilis ADP + phosphate + an L-arginyl-L-amino acid
-
?
6.3.2.48 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
-
?
6.3.2.48 ATP + L-arginine + an L-amino acid
-
Bacillus subtilis NBRC3134 ADP + phosphate + an L-arginyl-L-amino acid
-
?
6.3.2.48 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

EC Number Synonyms Comment Organism
6.3.2.48 RizA
-
Bacillus subtilis

Cofactor

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

General Information

EC Number General Information Comment Organism
6.3.2.48 evolution the enzyme is a member of the ATP-dependent carboxylate-amine/thiol ligase superfamily Bacillus subtilis
6.3.2.48 metabolism L-amino-acid ligase RizA from Bacillus subtilis participates in the biosynthesis of the oligopeptide antibiotic rhizocticin Bacillus subtilis
6.3.2.48 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