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Enzyme Nomenclature
Information on EC 6.3.2.48 - L-arginine-specific L-amino acid ligase
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The expected taxonomic range for this enzyme is: Bacillus subtilis
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EC NUMBER 
COMMENTARY 
6.3.2.48
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RECOMMENDED NAME
GeneOntology No.
L-arginine-specific L-amino acid ligase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-arginine + an L-amino acid = ADP + phosphate + an L-arginyl-L-amino acid
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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)
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)
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SYSTEMATIC NAME
IUBMB Comments
L-arginine:L-amino acid ligase (ADP-forming)
The enzyme, characterized from the bacterium Bacillus subtilis, requires Mn2+ for activity. It shows strict substrate specificity toward L-arginine as the first (N-terminal) amino acid of the product. The second amino acid could be any standard protein-building amino acid except for L-proline.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
the enzyme is a member of the ATP-dependent carboxylate-amine/thiol ligase superfamily
evolution
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the enzyme is a member of the ATP-dependent carboxylate-amine/thiol ligase superfamily
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metabolism
L-amino-acid ligase RizA from Bacillus subtilis participates in the biosynthesis of the oligopeptide antibiotic rhizocticin
metabolism
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L-amino-acid ligase RizA from Bacillus subtilis participates in the biosynthesis of the oligopeptide antibiotic rhizocticin
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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
additional information
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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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-Arg + L-2-amino-5-phosphono-3-cis-pentenoate
ADP + phosphate + L-Arg-L-2-amino-5-phosphono-3-cis-pentenoate
ATP + L-Arg + L-Xaa
ADP + phosphate + 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
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ATP + 2 L-Arg
ADP + phosphate + L-Arg-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 specifity 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
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ATP + 2 L-Arg
ADP + phosphate + L-Arg-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 specifity 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
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ATP + L-Arg + L-2-amino-5-phosphono-3-cis-pentenoate
ADP + phosphate + L-Arg-L-2-amino-5-phosphono-3-cis-pentenoate
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ATP + L-Arg + L-2-amino-5-phosphono-3-cis-pentenoate
ADP + phosphate + L-Arg-L-2-amino-5-phosphono-3-cis-pentenoate
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ATP + L-arginine + an L-amino acid
ADP + phosphate + an L-arginyl-L-amino acid
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ATP + L-arginine + an L-amino acid
ADP + phosphate + an L-arginyl-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
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ATP + L-arginine + an L-amino acid
ADP + phosphate + an L-arginyl-L-amino acid
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ATP + L-arginine + an L-amino acid
ADP + phosphate + an L-arginyl-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
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additional information
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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)
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additional information
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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)
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-arginine + an L-amino acid
ADP + phosphate + an L-arginyl-L-amino acid
B5UAT8
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ATP + L-arginine + an L-amino acid
ADP + phosphate + an L-arginyl-L-amino acid
B5UAT8
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additional information
?
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B5UAT8
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)
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additional information
?
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B5UAT8
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)
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
required. When Mg2+ is replaced by Mn2+ and Co2+, L-amino acid ligase activity is decreased
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
30°C: about 50% of maximal activity, 50°C: about 55% of maximal activity. Significant decrease of activity above 50°C
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified selenomethionine-substituted, substrate-free enzyme, X-ray diffraction structure determination and analysis
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene rizA, overexpression of selenomethionine-substituted enzyme in Escherichia coli strain B834(DE3)
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LINKS TO OTHER DATABASES (specific for EC-Number 6.3.2.48)
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