6.3.2.48: L-arginine-specific L-amino acid ligase
This is an abbreviated version!
For detailed information about L-arginine-specific L-amino acid ligase, go to the full flat file.
Reaction
Synonyms
RizA
ECTree
6.3.2.48 L-arginine-specific L-amino acid ligaseAdvanced search results
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Substrates Products on EC 6.3.2.48 - L-arginine-specific L-amino acid ligase
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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
-
-
?
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 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
-
-
?
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 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
-
-
?
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-2-amino-5-phosphono-3-cis-pentenoate
ADP + phosphate + L-Arg-L-2-amino-5-phosphono-3-cis-pentenoate
-
-
-
?
ATP + L-arginine + an L-amino acid
ADP + phosphate + an L-arginyl-L-amino acid
-
-
-
?
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
-
-
?
ATP + L-arginine + an L-amino acid
ADP + phosphate + an L-arginyl-L-amino acid
-
-
-
?
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
-
-
?
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)
-
-
?
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)
-
-
?
