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Literature summary for 6.3.2.48 extracted from

  • Kino, K.; Kotanaka, Y.; Arai, T.; Yagasaki, M.
    A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptide-antibiotic rhizocticin (2009), Biosci. Biotechnol. Biochem., 73, 901-907.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

Metals/Ions

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 [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/ Products (Substrates)

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

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

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis

Reaction

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 and Products (Substrate)

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

Subunits Comment Organism
homodimer 2 * 45000, SDS-PAGE Bacillus subtilis
homodimer 2 * 46344, calculated from sequence Bacillus subtilis

Synonyms

Synonyms Comment Organism
RizA
-
Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Bacillus subtilis
37
-
-
Bacillus subtilis

Temperature Range [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Bacillus subtilis
9.5
-
-
Bacillus subtilis

pH Range

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