Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required. When Mg2+ is replaced by Mn2+ and Co2+, L-amino acid ligase activity is decreased | Bacillus subtilis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
45000 | - |
2 * 45000, SDS-PAGE | Bacillus subtilis |
46344 | - |
2 * 46344, calculated from sequence | Bacillus subtilis |
80000 | - |
gel filtration | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Bacillus subtilis | the enzyme is expected to be involved in the biosynthesis of rhizocticin (dipeptide or tripeptide antibiotics that commonly possess L-arginyl-L-2-amino-5-phosphono-3-cis-pentenoic acid) | ? | - |
? | |
additional information | Bacillus subtilis NBRC3134 | the enzyme is expected to be involved in the biosynthesis of rhizocticin (dipeptide or tripeptide antibiotics that commonly possess L-arginyl-L-2-amino-5-phosphono-3-cis-pentenoic acid) | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | B5UAT8 | - |
- |
Bacillus subtilis NBRC3134 | B5UAT8 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Bacillus subtilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-arginine + an L-amino acid = ADP + phosphate + an L-arginyl-L-amino acid | Xaa is an arbitrary amino acid except Pro (Arg, Lys, His, Gln, Asn, Glu, Asp, Ala, Ser, Thr, Gly, Val, Leu, Ile, Met, Cys, Phe, Trp, Tyr) | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 2 L-Arg | the enzyme synthesizes hetero-dipeptides. Arg is present at the N-terminus. The enzyme synthesizes Arg-Arg, when only Arg is used as substrate, but preferentially synthesizes Arg-Xaa when Arg and other amino acids are used as substrates. RizA has strict substrate specificity toward L-arginine as the N-terminal substrate. The substrate specificity at the C-terminus is very relaxed. Hetero-dipeptide consisting of Arg and Pro is not detected. The enzyme does not use D-form amino acids as substrates. No tripeptides and no longer peptides are detected. The substrate specificity at the C-terminus is relaxed | Bacillus subtilis | ADP + phosphate + L-Arg-L-Arg | - |
? | |
ATP + 2 L-Arg | the enzyme synthesizes hetero-dipeptides. Arg is present at the N-terminus. The enzyme synthesizes Arg-Arg, when only Arg is used as substrate, but preferentially synthesizes Arg-Xaa when Arg and other amino acids are used as substrates. RizA has strict substrate specificity toward L-arginine as the N-terminal substrate. The substrate specificity at the C-terminus is very relaxed. Hetero-dipeptide consisting of Arg and Pro is not detected. The enzyme does not use D-form amino acids as substrates. No tripeptides and no longer peptides are detected. The substrate specificity at the C-terminus is relaxed | Bacillus subtilis NBRC3134 | ADP + phosphate + L-Arg-L-Arg | - |
? | |
ATP + L-Arg + L-2-amino-5-phosphono-3-cis-pentenoate | - |
Bacillus subtilis | ADP + phosphate + L-Arg-L-2-amino-5-phosphono-3-cis-pentenoate | - |
? | |
ATP + L-Arg + L-2-amino-5-phosphono-3-cis-pentenoate | - |
Bacillus subtilis NBRC3134 | ADP + phosphate + L-Arg-L-2-amino-5-phosphono-3-cis-pentenoate | - |
? | |
ATP + L-Arg + L-Ala | - |
Bacillus subtilis | ADP + phosphate + L-Arg-L-Ala | - |
? | |
ATP + L-Arg + L-Ala | - |
Bacillus subtilis NBRC3134 | ADP + phosphate + L-Arg-L-Ala | - |
? | |
ATP + L-Arg + L-His | - |
Bacillus subtilis | ADP + phosphate + L-Arg-L-His | - |
? | |
ATP + L-Arg + L-His | - |
Bacillus subtilis NBRC3134 | ADP + phosphate + L-Arg-L-His | - |
? | |
ATP + L-Arg + L-Ser | - |
Bacillus subtilis | ADP + phosphate + L-Arg-L-Ser | - |
? | |
ATP + L-Arg + L-Xaa | the enzyme synthesizes hetero-dipeptides. Arg is present at the N-terminus. The enzyme synthesizes Arg-Arg, when only Arg is used as substrate, but preferentially synthesizes Arg-Xaa when Arg and other amino acids are used as substrates. RizA has strict substrate specificity toward L-arginine as the N-terminal substrate. Hetero-dipeptide consisting of Arg and Pro is not detected. The enzyme does not use D-form amino acids as substrates. No tripeptides and no longer peptides are detected. The substrate specificity at the C-terminus is relaxed | Bacillus subtilis | ADP + phosphate + L-Arg-L-Xaa | - |
? | |
additional information | the enzyme is expected to be involved in the biosynthesis of rhizocticin (dipeptide or tripeptide antibiotics that commonly possess L-arginyl-L-2-amino-5-phosphono-3-cis-pentenoic acid) | Bacillus subtilis | ? | - |
? | |
additional information | the enzyme is expected to be involved in the biosynthesis of rhizocticin (dipeptide or tripeptide antibiotics that commonly possess L-arginyl-L-2-amino-5-phosphono-3-cis-pentenoic acid) | Bacillus subtilis NBRC3134 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 45000, SDS-PAGE | Bacillus subtilis |
homodimer | 2 * 46344, calculated from sequence | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
RizA | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Bacillus subtilis |
37 | - |
- |
Bacillus subtilis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 50 | 30°C: about 50% of maximal activity, 50°C: about 55% of maximal activity. Significant decrease of activity above 50°C | Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Bacillus subtilis |
9.5 | - |
- |
Bacillus subtilis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
9 | 10 | pH 9.0: about 60% of maximal activity, pH 10.0: about 50% of maximal activity. Sharp decrease of activity below pH 9.0 and above pH 10.0 | Bacillus subtilis |