EC Number | Cloned (Comment) | Organism |
---|---|---|
6.3.2.48 | gene rizA, overexpression of selenomethionine-substituted enzyme in Escherichia coli strain B834(DE3) | Bacillus subtilis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.3.2.48 | purified selenomethionine-substituted, substrate-free enzyme, X-ray diffraction structure determination and analysis | Bacillus subtilis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.48 | Mg2+ | required | Bacillus subtilis |
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 | - |
? |
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 | - |
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 |
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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.3.2.48 | RizA | - |
Bacillus subtilis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.48 | ATP | ATP binding site structure analysis, overview | Bacillus subtilis |
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 |