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Information on EC 6.3.4.5 - argininosuccinate synthase and Organism(s) Thermus thermophilus and UniProt Accession P59846

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.5 argininosuccinate synthase
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This record set is specific for:
Thermus thermophilus
UNIPROT: P59846 not found.
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Word Map
The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
argininosuccinate synthetase, argininosuccinate synthase, elastin-binding protein, argininosuccinate synthase 1, argininosuccinic acid synthetase, arginine succinate synthetase, citrulline-aspartate ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Argininosuccinate synthetase
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Arginine succinate synthetase
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-
-
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Argininosuccinate synthetase
Argininosuccinic acid synthetase
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-
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Citrulline--aspartate ligase
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-
-
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Citrulline-aspartate ligase
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-
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Elastin-binding protein
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-
-
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Synthetase, argininosuccinate
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
show the reaction diagram
detailed catalytic mechanism, stereochemistry
ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
show the reaction diagram
catalytic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
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-
-
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SYSTEMATIC NAME
IUBMB Comments
L-citrulline:L-aspartate ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-58-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
show the reaction diagram
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
show the reaction diagram
seventh step of the arginine biosynthesis, second step of the urea cycle
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?
ATP + L-citrulline + L-aspartate
AMP + diphosphate + L-argininosuccinate
show the reaction diagram
-
second step of urea cycle
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required for maximal activity, in octahedral coordination with 3 oxygen atoms of the triphosphate group and 3 water molecules
Mg2+
-
essential for catalysis
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44815
4 * 44815, recombinant tAsS, subunit/domain structure, amino acid sequence
44815
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4 * 44815, recombinant tAsS, subunit/domain structure, amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 44815, recombinant tAsS, subunit/domain structure, amino acid sequence
tetramer
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4 * 44815, recombinant tAsS, subunit/domain structure, amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of enzyme complexed with intact ATP and substrates citrulline and aspartate, complexed with AMP and argininosuccinate, and complexed with AMP-PNP, arginine, aspartate and Mg2+, vapor diffusion method, X-ray analysis
3-dimensional structure of free enzyme and of complexes with intact ATP, adenylyl imidodiphosphate, arginine or succinate, hanging drop method
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)pLysE
overexpression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goto, M.; Nakajima, Y.; Hirotsu, K.
Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action
J. Biol. Chem.
277
15890-15896
2002
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team
Goto, M.; Omi, R.; Miyahara, I.; Sugahara, M.; Hirotsu, K.
Structures of argininosuccinate synthetase in enzyme-ATP substrates and enzyme-AMP product forms. Stereochemistry of the catalytic reaction
J. Biol. Chem.
278
22964-22971
2003
Thermus thermophilus (P59846), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (P59846)
Manually annotated by BRENDA team