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

EC NUMBER
COMMENTARY hide
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 hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-arginine + an L-amino acid = ADP + phosphate + an L-arginyl-L-amino acid
show the reaction diagram
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2 L-Arg
ADP + phosphate + L-Arg-L-Arg
show the reaction diagram
ATP + L-Arg + L-2-amino-5-phosphono-3-cis-pentenoate
ADP + phosphate + L-Arg-L-2-amino-5-phosphono-3-cis-pentenoate
show the reaction diagram
ATP + L-Arg + L-Ala
ADP + phosphate + L-Arg-L-Ala
show the reaction diagram
ATP + L-Arg + L-His
ADP + phosphate + L-Arg-L-His
show the reaction diagram
ATP + L-Arg + L-Ser
ADP + phosphate + L-Arg-L-Ser
show the reaction diagram
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-
-
?
ATP + L-Arg + L-Xaa
ADP + phosphate + L-Arg-L-Xaa
show the reaction diagram
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 + L-arginine + an L-amino acid
ADP + phosphate + an L-arginyl-L-amino acid
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-arginine + an L-amino acid
ADP + phosphate + an L-arginyl-L-amino acid
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
ATP binding site structure analysis, overview
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
30°C: about 50% of maximal activity, 50°C: about 55% of maximal activity. Significant decrease of activity above 50°C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
2 * 45000, SDS-PAGE
46344
2 * 46344, calculated from sequence
80000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified selenomethionine-substituted, substrate-free enzyme, X-ray diffraction structure determination and analysis
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene rizA, overexpression of selenomethionine-substituted enzyme in Escherichia coli strain B834(DE3)