Information on EC 6.3.4.4 - Adenylosuccinate synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
6.3.4.4
-
RECOMMENDED NAME
GeneOntology No.
Adenylosuccinate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
fully random mechanism
-
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
sequential rapid equilibrium fully random mechanism
-
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
fully random terter mechanism
-
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
random sequential binding mechanism
-
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
phosphate-binding region of adenylosuccinate synthetase is involved in a conformational change induced by GTP and IMP binding. GTP and IMP binding depend on the presence of the other substrate at the active site of the enzyme
-
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
sequential mechanism with a fully random order of substrate addition
-
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
rapid equilibrium random AB steady-state ordered C kinetic mechanism
Q57981
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenosine ribonucleotides de novo biosynthesis
-
-
Alanine, aspartate and glutamate metabolism
-
-
Metabolic pathways
-
-
Purine metabolism
-
-
purine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
IMP:L-aspartate ligase (GDP-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Adenylosuccinate synthase
-
-
-
-
Adenylosuccinate synthetase
-
-
-
-
AdSS
-
-
-
-
AMPSase
-
-
-
-
IMP--aspartate ligase
-
-
-
-
IMP-aspartate ligase
-
-
-
-
Succino-AMP synthetase
-
-
-
-
Succinoadenylic kinosynthetase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-57-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain pabaA1
-
-
Manually annotated by BRENDA team
Aspergillus nidulans pabaA1
strain pabaA1
-
-
Manually annotated by BRENDA team
Cryptococcus neoformans variant grubii
-
-
Manually annotated by BRENDA team
Cryptococcus neoformans H99
Cryptococcus neoformans variant grubii
-
-
Manually annotated by BRENDA team
cloned into the temperature-inducible, high-copy-number plasmid vector, pMOB45. Upon temperature induction, cells containing this plasmid produce adenylosuccinate synthetase at approximately 40times the wild-type level
-
-
Manually annotated by BRENDA team
strains BW25113 and MP101
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes D13A, E14A, H41N, and K16Q
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes D333N, D333E, and D333Q
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes L228A, S240A, and Q224E
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes R143L and D13A
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes R303L, R304L, and R305L
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes, R132K, R143L, and D231A
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes: G15V, K331L, and K331R
-
-
Manually annotated by BRENDA team
wild-type and mutant R143L
-
-
Manually annotated by BRENDA team
wild-type and mutant R147L
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
human
-
-
Manually annotated by BRENDA team
mouse
Uniprot
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
-
SwissProt
Manually annotated by BRENDA team
strain ST700
-
-
Manually annotated by BRENDA team
strain ST700
-
-
Manually annotated by BRENDA team
2 isozymic forms: acidic type L, and basic type M
-
-
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
ADSS1 inactivation as a somatic alteration causing lung carcinogenesis
physiological function
-
genetic variation of inosine triphosphatase causing an accumulation of inosine triphosphate protects patients against ribavirin-induced anemia during treatment for chronic hepatitis C infection. ITP can be used for ATP biosynthesis via adenylosuccinate synthase in place of guanosine triphosphate. With ribavirin challenge, erythrocyte ATP reduction is more severe in the wild-type inosine triphosphatase ITPA genotype than in the hemolysis protective ITPA genotype. The alleviation of ATP reduction by the hemolysis protective ITPA genotype is canceled by the adenylosuccinate synthase inhibitor 6-mercaptoethanol
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-dGTP + IMP + L-aspartate
2'-dGDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
P28650
-
-
-
?
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
ddGTP + IMP + L-aspartate
ddGDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
show the reaction diagram
P28650
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
show the reaction diagram
-
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
show the reaction diagram
-
-
-
-
-
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
show the reaction diagram
-
-
-
-
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
show the reaction diagram
-
-
-
-
-
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
show the reaction diagram
-
61% of the efficiency of IMP as substrate, V/Km
-
-
-
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
show the reaction diagram
-
-
-
-
-
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
show the reaction diagram
-
-
-
-
-
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
show the reaction diagram
-
i.e. allopurinol ribonucleotide
-
-
GTP + 8-azaIMP + L-Asp
GDP + phosphate + 8-azasuccinoAMP
show the reaction diagram
-
-
-
-
-
GTP + 8-azaIMP + L-Asp
GDP + phosphate + 8-azasuccinoAMP
show the reaction diagram
-
-
-
-
GTP + 8-azaIMP + L-Asp
GDP + phosphate + 8-azasuccinoAMP
show the reaction diagram
-
-
-
-
-
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
show the reaction diagram
-
-
-
-
-
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
show the reaction diagram
-
-
-
-
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
show the reaction diagram
-
-
-
-
-
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
show the reaction diagram
-
8.8% of the efficiency of IMP as substrate , V/Km
-
-
-
GTP + IMP + 6-methoxypurine nucleotide
?
show the reaction diagram
-
-
-
-
-
GTP + IMP + Ala-3-nitronate
GDP + phosphate + N6-(L-1-carboxy-2-nitroethyl)AMP
show the reaction diagram
-
-
-
-
GTP + IMP + cysteine sulfinate
?
show the reaction diagram
-
-
-
-
-
GTP + IMP + hydroxylamine
GDP + phosphate + ?
show the reaction diagram
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
P0A7D4
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
r
-
-
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
Aspergillus nidulans pabaA1
-
-
-
-
?
GTP + IMP + L-Asp
?
show the reaction diagram
-
plays an important role in the interconversion of purines
-
-
-
GTP + IMP + L-Asp
?
show the reaction diagram
-
plays an important role in the interconversion of purines
-
-
-
GTP + IMP + L-Asp
?
show the reaction diagram
-
first committed step towards the de novo biosynthesis of AMP
-
-
-
GTP + IMP + L-Asp
?
show the reaction diagram
-
first committed step towards the de novo biosynthesis of AMP
-
-
-
GTP + IMP + L-Asp
?
show the reaction diagram
-
penultimate step in pathway of AMP biosynthesis
-
-
-
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
P28650
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
O24396
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
Q96529
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
Q9U8D3
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
acidic and basic isozymes, which participates in the first committed step of de novo AMP biosynthesis and/or the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
catalyzes the first committed step in the de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
catalyzes the first step in the conversion of IMP to AMP in de novo purine nucleotide metabolism
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
catalyzing the first committed step in de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
catalyzing the first committed step in the biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
Q96529
catalyzing the first step in the de novo synthesis of adenylmonophosphate
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
O24396
catalyzing the first step in the de novo sythesis of adenylmonophosphate
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from L-aspartate and IMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
function in adenine nucleotide biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
P28650
governs the committed step of AMP biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
governs the first committed step in de novo biosynthesis of AMP plays a significant role in de novo purine nucleotide biosynthesis, the purine nucleotide cycle, and/or salvage pathway for nucleotides
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
key enzyme for the synthesis of adenosine de novo, first committed step in synythesis of adenosine, located at the branchpoint of AMP and GMP synthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
salvage pathway
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
Q9U8D3
salvage pathway, catalyzing the first committed step in the synthesis of AMP from IMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
Q8N142
first committed step in AMP synthesis. Isoenzyme AdSS1 has a potential role in muscle metabolism
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenosylsuccinate
show the reaction diagram
-
function in adenine nucleotide biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
Q57981
-
i.e. adenylosuccinate
-
?
GTP + ITP + L-aspartate
?
show the reaction diagram
-
-
-
?
ITP + IMP + L-Asp
IDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
ITP + IMP + L-Asp
IDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
ITP can be used for ATP biosynthesis via adenylosuccinate synthase in place of guanosine triphosphate
-
?
UTP + IMP + L-Asp
UDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
XTP + IMP + L-Asp
XDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
ITP + IMP + L-aspartate
IDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
additional information
?
-
-
ATP cannot be used as substrate instead of GTP
-
?
additional information
?
-
-
ATP is no substrate
-
?
additional information
?
-
-
vertebrates possess two isozymes, the acidic is similar to the synthetase from bacteria and plants, the basic isozyme participates in the purine nucleotide cycle
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-Asp
?
show the reaction diagram
-
plays an important role in the interconversion of purines
-
-
-
GTP + IMP + L-Asp
?
show the reaction diagram
-
plays an important role in the interconversion of purines
-
-
-
GTP + IMP + L-Asp
?
show the reaction diagram
-
first committed step towards the de novo biosynthesis of AMP
-
-
-
GTP + IMP + L-Asp
?
show the reaction diagram
-
first committed step towards the de novo biosynthesis of AMP
-
-
-
GTP + IMP + L-Asp
?
show the reaction diagram
-
penultimate step in pathway of AMP biosynthesis
-
-
-
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
acidic and basic isozymes, which participates in the first committed step of de novo AMP biosynthesis and/or the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
catalyzes the first committed step in the de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
catalyzes the first step in the conversion of IMP to AMP in de novo purine nucleotide metabolism
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
catalyzing the first committed step in de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
catalyzing the first committed step in the biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
Q96529
catalyzing the first step in the de novo synthesis of adenylmonophosphate
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
O24396
catalyzing the first step in the de novo sythesis of adenylmonophosphate
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from L-aspartate and IMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
function in adenine nucleotide biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
P28650
governs the committed step of AMP biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
governs the first committed step in de novo biosynthesis of AMP plays a significant role in de novo purine nucleotide biosynthesis, the purine nucleotide cycle, and/or salvage pathway for nucleotides
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
key enzyme for the synthesis of adenosine de novo, first committed step in synythesis of adenosine, located at the branchpoint of AMP and GMP synthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
salvage pathway
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
Q9U8D3
salvage pathway, catalyzing the first committed step in the synthesis of AMP from IMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
Q8N142
first committed step in AMP synthesis. Isoenzyme AdSS1 has a potential role in muscle metabolism
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenosylsuccinate
show the reaction diagram
-
function in adenine nucleotide biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
can replace Mg2+ with lower efficiency
Ba2+
-
absolute requirement for divalent metal ions
Ca2+
-
14.1% of the activation relative to Mg2+
Ca2+
-
16.2% of the activation relative to Mg2+
Ca2+
-
can replace Mg2+ with lower efficiency
Ca2+
-
can replace Mg2+ with lower efficiency
Ca2+
-
absolute requirement for divalent metal ions
Co2+
-
34.8% of the activation relative to Mg2+
Co2+
-
21.3% of the activation relative to Mg2+
Co2+
-
can replace Mg2+ with lower efficiency
Co2+
-
absolute requirement for divalent metal ions
Cu2+
-
10.9% of the activation relative to Mg2+
Cu2+
-
absolute requirement for divalent metal ions
Mg2+
-
required
Mg2+
-
full activity in presence of Mg2+
Mg2+
-
divalent cation required, maximal activity obtained with Mg2+
Mg2+
-
two Mg2+ ions are required. The first metal ion is coordinated with beta-phosphoryl groups and gamma-phosphoryl groups of GTP to provide an electron sink, and the second one seems to interact with Asp in the enzyme active site. Km for Mg2+: 0.114 mM
Mg2+
-
absolute requirement for divalent metal ions, best activator
Mg2+
-
active site Mg2+
Mg2+
-
required
Mg2+
-
AdSS2 requires 2.0 mM Mg(acetate)2, AdSS1 requires 8.0 mM Mg(acetate)2
Mg2+
Q57981
requires Mg2+ for catalysis with maximum activity obtained at 15 mM magnesium acetate
Mg2+
-
dependent on
Mn2+
-
37% of the activation relative to Mg2+
Mn2+
-
43.2% of the activation relative to Mg2+
Mn2+
-
can replace Mg2+ with lower efficiency
Mn2+
-
can replace Mg2+ with lower efficiency
Ni2+
-
can replace Mg2+ with lower efficiency
Mn2+
-
absolute requirement for divalent metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+)-Hydantocidin
-
-
(NH4)2SO4
-
25 mM
2-mercaptosuccinate
-
-
3',5'-cyclic GMP
-
-
3',5'-cyclic GMP
-
-
4-Oxo-2-aminopentanoic acid
-
i.e. 2-oxonorvaline, poor
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-amino-4-(N-succinocarboxamide)imidazole ribonucleotide
-
-
5-amino-4-carbamoyl-imidazole ribonucleotide
-
-
6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-monophosphate
-
-
6-mercaptopurine ribonucleotide
-
-
6-mercaptopurine riboside 5'-phosphate
-
-
6-Thio-GMP
-
-
6-Thio-GMP
-
-
6-thio-IMP
-
-
8-Aza-7-deaza-GMP
-
-
8-Aza-7-deaza-GMP
-
competitive with respect to GTP
8-aza-GMP
-
-
8-aza-GMP
-
competitive with respect to GTP
8-Aza-IMP
-
-
acyclo-GMP
-
-
adenosine 3',5'-AMP
-
-
adenylosuccinate
-
-
adenylosuccinate
-
-
adenylosuccinate
-
competitive with respect to IMP
adenylosuccinate
-
-
adenylosuccinate
-
-
adenylosuccinate
P28650
feedback inhibition
adenylosuccinate
-
-
adenylosuccinate
-
competitive versus IMP, non-competitive versus GTP and aspartate
adenylosuccinate
Q57981
competitive inhibitor of IMP, noncompetitive inhibitor of GTP and aspartate
ADP
-
-
allopurinol nucleotide
-
-
AMP
-
competitive with respect to IMP
AMP
P28650
feedback inhibition
AMP
-
inhibits the acidic isozyme competitively, weak inhibition of the basic isozyme noncompetitively
AMP
-
competitive versus IMP, non-competitive versus GTP and non-competitive versus aspartate
AMP
Q57981
competitive with respect to IMP and noncompetitive with GTP and aspartate
arabinosyl-GMP
-
-
arabinosyl-GMP
-
beta-D-arabinosyl-GMP, competitive with respect to GTP
argininosuccinate
-
-
argininosuccinate
-
-
aspartate analogs
-
-
beta,gamma-5'-Guanylylmethylene diphosphate
-
-
Ca2+
-
in presence of Mg2+
Carbamoylphosphate
-
-
Cd2+
-
in presence of Mg2+
CDP
-
-
Cl-
-
weak inhibitor
CMP
-
-
Cu2+
-
in presence of Mg2+
Cu2+
-
complete loss in activity within 4 h at 0.5 mM
cyanoalanine
-
poor
cyclic GMP
-
-
cysteine
-
poor
cysteine sulfonate
-
poor
D-fructose 1,6 bisphosphate
Q57981
competitive with IMP and noncompetitive against GTP
D-fructose 1,6-bisphosphate
-
inhibits both isozymes competitively
dAMP
-
-
dCMP
-
-
dGDP
-
-
dGMP
-
2'-dGMP
dGMP
-
2'-dGMP
dGMP
-
-
Formycin B monophosphate
-
-
fructose 1,6-diphosphate
-
basic type M isozym more strongly inhibited than acidic type L isozym
fructose 1,6-diphosphate
-
-
fumarate
-
-
GDP
-
-
GDP
-
competitive with respect to GTP
GDP
-
uncompetitive versus IMP, competitive versus GTP and non-competitive versus aspartate
GDP
Q57981
competitive inhibitor of GTP, noncompetitive inhibitor with IMP and aspartate
GMP
-
and analogs
GMP
-
competitive with respect to GTP
GMP
-
potent inhibitor, competitive inhibition towards IMP
GMP
-
uncompetitive versus IMP, competitive versus GTP and non-competitive versus aspartate
GMP
Q57981
competitive with respect to GTP and noncompetitive with IMP and aspartate
guanosine
-
-
guanosine 5'-(beta,gamma-imino)triphosphate
-
-
guanosine 5'-diphosphate
-
-
Guanosine 5'-diphosphate-3'-diphosphate
-
competitive with respect to GTP and noncompetitive with respect to L-Asp and IMP
Guanosine 5'-O-[S-(4-bromo-2,3-dioxobutyl)thio]phosphate
-
-
Hadacidin
-
5 mM, 100% inhibition
Hadacidin
-
-
Hadacidin
-
-
Hadacidin
-
uncompetitive versus IMP and GTP, competitive versus aspartate
Hadacidin
-
-
Hg2+
-
reversed by addition of DTT
homocysteine
-
poor
Hydantocidin 5'-phosphate
-
-
hydroxylamine
-
-
IDP
-
-
IMP
-
competitive inhibition of the acidic isozyme, noncompetitive of the basic isozyme
IMP
Q57981
inhibits the enzyme activity at subsaturating GTP concentrations
Maleate
-
-
methionine sulfone
-
poor
N-(Thiocarboxy)-L-aspartic anhydride
-
5 mM, 27.5% inhibition
N-Acetyl-5'-phosphohydantocidin
-
-
N-Acetyl-N-hydroxyglycine
-
5 mM, 72.9% inhibition
N-acetylglycine
-
5 mM, 51.2% inhibition
N-benzoylglycine
-
5 mM, 6% inhibition
N-formyl-N-hydroxyglycine
Q57981
i.e. hadacidin. competitive inhibitor of aspartate, showed uncompetitive inhibition with IMP and GTP
-
N-Formylglycine
-
5 mM, 61.1% inhibition
N-Hydroxyaspartate
-
poor
N-Hydroxyglycine
-
5 mM, 49.3% inhibition
N-methylaspartate
-
poor
Nucleotides
-
acidic type L isozyme more strongly inhibited than basic type M isozyme
-
oligonucleotides
-
inhibition by single-stranded autonomously replicating sequences, highly specific inhibition by a 44-base DNA oligonucleotide carrying the autonomously replicating sequences core consensus sequence
oxaloacetate
-
-
Pb2+
-
in presence of Mg2+
Phenylglyoxal
-
GTP or IMP partially protect
phosphate
-
-
phosphate
-
-
phosphate
-
competitive with aspartate
phosphate
Q57981
potent inhibitor, biphasic inhibition, competitive with IMP and noncompetitive with GTP
phosphoenolpyruvate
-
-
SCN-
-
i.e. thiocyanate
succinate
-
-
succinate
-
-
succinate
-
poor inhibitor
succinate
-
-
TDP
-
-
TMP
-
-
UDP
-
-
UMP
-
-
XMP
-
competitive with respect to IMP
Zn2+
-
in presence of Mg2+
Mn2+
-
in presence of Mg2+
additional information
-
hydantocidin 5'-phosphate, GDP, HPO42-, and Mg2+ may represent a set of synergistic inhibitors even more effective than the combination of IMP, GDP, NO3-, and Mg2+
-
additional information
-
negligible inhibition by adenine nucleotides
-
additional information
-
GMP is not a strong inhibitor of AMPsS at physiological concentrations
-
additional information
-
not inhibited Mn2+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP
-
ASS expression is induced by AMP
D-fructose 1,6 bisphosphate
-
binds to the Asp loop and induces a conformation that facilitates aspartate binding to the enzyme active site
D-fructose 1,6-diphosphate
-
activates
NH4+
-
ASS expression is induced rather than repressed by NH4
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.041
2'-dIMP
-
22C
0.058
2'-dIMP
P28650
22C
0.48
2'-dIMP
-
-
0.05
8-azaIMP
-
-
0.34
allopurinol ribonucleotide
-
-
0.34
allopurinol ribonucleotide
-
Asp, mutant R143L
0.26
arabinosylIMP
-
-
0.26
arabinosylIMP
-
2'-dIMP
0.03
Asp
-
-
0.03
Asp
-
muscle enzyme
0.03
Asp
-
IMP, wild-type
0.057
Asp
-
mutant R303L
0.0657
Asp
-
mutant R303L
0.115
Asp
-
mutant R147L
0.115
Asp
-
GTP, mutant S240A
0.191
Asp
-
wild-type
0.23
Asp
-
Asp, wild-type
0.25 - 0.36
Asp
-
muscle enzyme
0.25
Asp
-
skeletal muscle
0.25
Asp
-
L-Asp
0.28
Asp
-
wild-type
0.29 - 0.3
Asp
-
-
0.308
Asp
-
-
0.308
Asp
-
heart enzyme
0.308
Asp
-
Asp, mutant K16Q
0.33
Asp
-
liver basic type L isozyme
0.33
Asp
-
IMP
0.335
Asp
-
-
0.35
Asp
-
mutant G15V
0.35
Asp
-
Asp, wild-type, and mutant Q224M
0.36 - 1.47
Asp
-
acidic liver type L isozym
0.38
Asp
-
GTP
0.38
Asp
-
mutant S240A
0.44
Asp
-
GTP, mutant K331R
0.52
Asp
-
mutant Q34E
0.68
Asp
-
-
0.95 - 1.16
Asp
-
-
0.95
Asp
-
-
1.06
Asp
-
mutant L228A
1.4
Asp
-
mutant E14A
1.47
Asp
-
liver basic type M isozyme
1.95
Asp
-
mutant H41N
5.4
Asp
-
mutant K331L
0.17
aspartate
-
pH 7.7, 25C, mutant D21A
0.23
aspartate
-
pH 7.7, 25C, wild-type
0.24
aspartate
-
pH 7.7, 25C, mutant N38E
0.3
aspartate
-
pH 7.7, 25C, mutant N38A
0.34
aspartate
-
pH 7.7, 25C, mutant R419L
0.5
aspartate
-
pH 5.6, 25C, mutant N38D
0.9
aspartate
-
pH 5.6, 25C, wild-type
1.4
aspartate
-
pH 7.7, 25C, mutant T42A
1.4
aspartate
-
pH 7.5, 37C
2
aspartate
-
pH 7.7, 25C, mutant H41N
2.6
aspartate
-
pH 7.7, 25C, mutant N38D
0.85
beta-D-arabinosylIMP
-
-
0.004 - 0.38
GTP
-
muscle enzyme
0.0048
GTP
-
pH 7.5, 37C
0.009
GTP
-
pH 6.7, 22C, AdSS1-Tr
0.01 - 0.012
GTP
-
-
0.01 - 0.048
GTP
-
-
0.01
GTP
-
Asp, mutant R305L
0.01
GTP
-
-
0.011
GTP
-
-
0.011
GTP
-
pH 5.6, 25C, wild-type
0.012
GTP
-
muscle enzyme
0.012
GTP
-
IMP
0.012
GTP
-
pH 7.2, 22C
0.012
GTP
-
pH 6.7, 22C, AdSS1
0.013
GTP
-
pH 6.7, 22C, AdSS2-Tr
0.015 - 0.13
GTP
-
liver acidic type L isozyme
0.015
GTP
-
pH 6.7, 22C, AdSS2
0.015
GTP
P28650
22C, cosubstrate: 2'-dIMP
0.016
GTP
-
-
0.017
GTP
-
liver enzyme
0.0172
GTP
-
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.018
GTP
-
heart enzyme
0.0184
GTP
-
pH 7.5
0.02
GTP
-
Asp, liver enzyme; IMP, liver enzyme
0.0201
GTP
-
mutant R303L
0.0206
GTP
-
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.021
GTP
-
pH 7.7, 25C, mutant V273N
0.021
GTP
-
22C, cosubstrate: 2'-dIMP
0.022
GTP
-
wild-type
0.023
GTP
-
GTP, mutant K16Q
0.0248
GTP
-
wild-type, pH 7.0, 37C
0.0248
GTP
-
wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.025
GTP
-
mutant G15V
0.0251
GTP
-
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.026
GTP
-
wild-type
0.026
GTP
-
pH 7.7, 25C, wild-type
0.026
GTP
-
22C, cosubstrate: IMP
0.0265
GTP
-
mutant R304L
0.027
GTP
-
mutant N429V, pH 7.0, 37C; wild-type, pH 7.0, 25C
0.0278
GTP
-
mutant R155L, pH 7.0, 25C
0.0306
GTP
-
mutant R305L
0.031 - 0.072
GTP
-
-
0.031
GTP
-
-
0.031
GTP
-
GTP, mutant E14A
0.031
GTP
-
pH 7.7, 25C, mutant V273A
0.0347
GTP
-
mutant T307V, pH 7.0, 37C
0.035
GTP
-
IMP, mutant G15V
0.035
GTP
-
GTP, mutant R131L; IMP, mutant R131L
0.0358
GTP
-
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.038
GTP
-
-
0.0386
GTP
-
mutant R155K, pH 7.0, 25C
0.041
GTP
-
pH 7.7, 25C, mutant N38A
0.0426
GTP
Q57981
pH 6.0, 70C
0.044
GTP
-
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.045
GTP
-
pH 7.7, 25C, mutant V273T
0.0465
GTP
-
mutant K62L, pH 7.0, 37C
0.052
GTP
-
pH 7.7, 25C, mutant D21A
0.0535
GTP
-
wild-type
0.054
GTP
-
pH 7.7, 25C, mutant N38E
0.054
GTP
-
pH 7.7, 25C, mutant T128A
0.056
GTP
-
pH 7.7, 25C, mutant T300V
0.057
GTP
-
pH 7.7, 25C, mutant T301A, hydroxylamine as substrate
0.06
GTP
-
pH 8.0, 25C, native enzyme
0.0605
GTP
-
mutant Q224M
0.0689
GTP
-
mutant Q224E
0.07
GTP
-
-
0.074
GTP
-
pH 7.7, 25C, mutant V273T, hydroxylamine as substrate
0.081
GTP
-
pH 8.0, 25C, recombinant enzyme
0.0839
GTP
-
mutant L228A
0.09
GTP
-
IMP
0.09
GTP
-
liver basic type L isozyme
0.116
GTP
-
pH 5.6, 25C, mutant N38D
0.12
GTP
-
skeletal muscle
0.126
GTP
-
mutant H41N
0.13
GTP
-
liver basic type L isozyme
0.13
GTP
-
pH 7.7, 25C, mutant H41N
0.133
GTP
-
mutant R147L
0.14
GTP
-
mutant D333E
0.14
GTP
-
pH 7.7, 25C, mutant V273A, hydroxylamine as substrate
0.17
GTP
-
pH 7.7, 25C, mutant T300A
0.18
GTP
-
pH 7.7, 25C, mutant V273N, hydroxylamine as substrate
0.19
GTP
-
pH 7.7, 25C, wild-type, hydroxylamine as substrate
0.193
GTP
-
mutant D333N
0.25
GTP
-
pH 7.7, 25C, mutant R419L
0.269
GTP
-
mutant R143L
0.27
GTP
-
pH 7.7, 25C, mutant N38D
0.28
GTP
-
pH 7.7, 25C, mutant T42A
0.334
GTP
-
mutant D33Q
0.6
GTP
-
mutant K331L
1.7
GTP
-
pH 7.7, 25C, mutant T129A
91
hydroxylamine
-
pH 7.7, 25C, mutant T301A
110
hydroxylamine
-
pH 7.7, 25C, mutant V273N
140
hydroxylamine
-
pH 7.7, 25C, mutant V273T
230
hydroxylamine
-
pH 7.7, 25C, wild-type
255
hydroxylamine
-
pH 7.7, 25C, mutant V273A
0.009
IMP
-
pH 6.7, 22C, AdSS2-Tr
0.012
IMP
-
pH 6.7, 22C, AdSS2
0.0152
IMP
-
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.0167
IMP
-
wild-type, pH 7.0, 37C
0.0168
IMP
-
wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.017
IMP
-
pH 7.7, 25C, mutant V273A
0.019
IMP
-
pH 7.7, 25C, mutant T300A
0.0198
IMP
-
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.02 - 0.2
IMP
-
-
0.02
IMP
-
-
0.0205
IMP
-
wild-type, pH 7.0, 25C
0.021
IMP
-
wild-type
0.021
IMP
-
IMP
0.0216
IMP
-
mutant K62L, pH 7.0, 37C
0.0228
IMP
-
pH 7.5, 37C
0.023
IMP
-
pH 7.5
0.024
IMP
-
wild-type
0.024
IMP
-
pH 7.7, 25C, mutant V273N
0.0248
IMP
-
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.0276
IMP
-
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.0278
IMP
-
wild-type
0.028
IMP
-
pH 7.7, 25C, wild-type and mutant N38E
0.028
IMP
-
pH 7.7, 25C, wild-type
0.028
IMP
-
22C
0.0285
IMP
-
mutant T307V, pH 7.0, 37C
0.0292
IMP
-
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.0296
IMP
-
mutant R304L
0.03 - 0.32
IMP
-
liver acidic type L isozyme
0.0305
IMP
-
mutant R305L
0.033
IMP
-
pH 7.7, 25C, mutant T300V
0.0352
IMP
-
mutant R303L
0.037 - 0.07
IMP
-
-
0.037
IMP
-
-
0.04
IMP
-
mutant H41N
0.041
IMP
-
mutant K331L
0.043
IMP
-
pH 7.7, 25C, mutant V273T
0.043
IMP
-
pH 6.7, 22C, AdSS1-Tr
0.045
IMP
-
pH 7.2, 22C
0.045
IMP
-
pH 6.7, 22C, AdSS1
0.047
IMP
-
-
0.047
IMP
-
IMP, mutant K331R
0.048
IMP
-
pH 7.7, 25C, mutant D21A
0.049
IMP
-
pH 7.7, 25C, mutant N38A
0.0497
IMP
-
mutant N429V, pH 7.0, 37C
0.0505
IMP
-
mutant K16Q
0.0505
IMP
-
IMP, mutant Q224E
0.054
IMP
-
-
0.054
IMP
-
XTP, mutant D333Q
0.055
IMP
-
mutant E14A
0.0596
IMP
-
wild-type
0.066
IMP
-
pH 7.7, 25C, wild-type, hydroxylamine as substrate
0.07
IMP
-
pH 5.6, 25C, wild-type
0.0755
IMP
Q57981
pH 6.0, 70C
0.077
IMP
-
pH 7.7, 25C, mutant V273T, hydroxylamine as substrate
0.0798
IMP
-
mutant Q34E
0.0825
IMP
-
mutant S240A
0.107 - 0.2
IMP
-
-
0.113
IMP
-
pH 7.7, 25C, mutant V273N, hydroxylamine as substrate
0.118
IMP
-
mutant R147L
0.123
IMP
-
pH 7.7, 25C, mutant T42A
0.137
IMP
-
mutant L228A
0.14
IMP
-
pH 7.7, 25C, mutant V273A, hydroxylamine as substrate
0.167
IMP
-
heart enzyme
0.171
IMP
-
muscle enzyme
0.2 - 0.7
IMP
-
muscle enzyme
0.2
IMP
-
pH 8.0, 25C, recombinant enzyme
0.2
IMP
-
pH 7.7, 25C, mutant R419L
0.3
IMP
-
pH 8.0, 25C, native enzyme
0.31
IMP
-
pH 7.7, 25C, mutant T128A
0.316
IMP
-
mutant Q224M
0.32
IMP
-
liver basic type L isozyme
0.32
IMP
-
Asp, mutant Q224E
0.32
IMP
-
pH 7.7, 25C, mutant T301A, hydroxylamine as substrate
0.4
IMP
-
pH 7.7, 25C, mutant H41N
0.41
IMP
-
-
0.557
IMP
-
mutant R155K, pH 7.0, 25C
0.69
IMP
-
liver basic isozyme
0.7
IMP
-
skeletal muscle
0.89
IMP
-
pH 7.7, 25C, mutant T129A
1.6
IMP
-
pH 7.7, 25C, mutant N38D
1.73
IMP
-
mutant R143L
1.73
IMP
-
Asp, mutant K331R
2.554
IMP
-
mutant R155L, pH 7.0, 25C
3.8
IMP
-
pH 5.6, 25C, mutant N38D
1.07
ITP
-
mutant D333Q
2.87
ITP
-
mutant D333E
3.29
ITP
-
mutant D333N
17.3
ITP
-
wild-type
0.004
L-Asp
P28650
22C, cosubstrate: 2'-dIMP
0.013
L-Asp
-
22C, cosubstrate: 2'-dIMP
0.23
L-Asp
-
22C, cosubstrate: dIMP
0.31
L-Asp
-
wild-type, pH 7.0, 37C
0.37
L-Asp
-
wild-type, pH 7.0, 25C
0.48
L-Asp
-
mutant R155K, pH 7.0, 25C
0.49
L-Asp
-
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.57
L-Asp
-
mutant N429V, pH 7.0, 37C
0.78
L-Asp
-
mutant K62L, pH 7.0, 37C
0.98
L-Asp
-
-
0.98
L-Asp
-
-
1.1
L-Asp
-
mutant T307V, pH 7.0, 37C
1.32
L-Asp
-
mutant R155L, pH 7.0, 25C
1.4
L-Asp
-
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25C
1.73
L-Asp
-
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25C
1.9
L-Asp
-
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25C; wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25C
3.3
L-Asp
-
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.01
L-aspartate
-
-
0.14
L-aspartate
-
pH 7.2, 22C
0.14
L-aspartate
-
pH 6.7, 22C, AdSS1
0.15
L-aspartate
-
pH 6.7, 22C, AdSS1-Tr
0.17
L-aspartate
-
pH 7.7, 25C, mutant T128A
0.23
L-aspartate
-
pH 7.7, 25C, wild-type
0.24
L-aspartate
-
pH 7.7, 25C, mutant T129A
0.82
L-aspartate
-
pH 7.7, 25C, mutant T300V
0.95
L-aspartate
-
pH 6.7, 22C, AdSS2
1
L-aspartate
-
pH 8.0, 25C, native enzyme
1.03
L-aspartate
-
pH 6.7, 22C, AdSS2-Tr
1.079
L-aspartate
Q57981
pH 6.0, 70C
1.65
L-aspartate
-
pH 8.0, 25C, recombinant enzyme
1.8
L-aspartate
-
pH 7.5
3.4
L-aspartate
-
pH 7.7, 25C, mutant V273T
6.2
L-aspartate
-
pH 7.7, 25C, mutant T300A
6.7
L-aspartate
-
-
7
L-aspartate
-
pH 7.7, 25C, mutant V273A
1.27
UTP
-
mutant D333N
2.06
UTP
-
wild-type
3.41
UTP
-
mutant D333Q
4.38
UTP
-
mutant D333E
0.0286
XTP
-
mutant D333E
0.0331
XTP
-
mutant D333N
0.388
XTP
-
wild-type
9
L-aspartate
-
pH 7.7, 25C, mutant V273N
additional information
additional information
-
effect of metal ions on Km-values
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.96
2'-dIMP
-
22C
5.5
2'-dIMP
P28650
22C
0.0048
GTP
-
pH 7.7, 25C, mutant N38A
0.0095
GTP
-
pH 7.7, 25C, mutant H41N
0.0134
GTP
-
pH 7.7, 25C, mutant N38D
0.034
GTP
-
pH 7.7, 25C, mutant N38E
0.049
GTP
-
pH 7.7, 25C, mutant D21A
0.05
GTP
-
pH 7.7, 25C, mutant V273N
0.096
GTP
-
pH 5.6, 25C, wild-type
0.1
GTP
-
pH 7.7, 25C, mutant R419L
0.171
GTP
-
pH 5.6, 25C, mutant N38D
0.42
GTP
-
pH 7.7, 25C, mutant T129A
0.45
GTP
Q57981
pH 6.0, 70C
0.46
GTP
-
pH 7.7, 25C, mutant T128A
0.64
GTP
-
pH 7.7, 25C, mutant T300A
0.89
GTP
-
pH 7.7, 25C, mutant T42A
0.96
GTP
-
22C, cosubstrate: 2'-dIMP
1
GTP
-
pH 7.7, 25C, wild-type
1
GTP
-
pH 7.7, 25C, mutant V273A; pH 7.7, 25C, wild-type
1
GTP
-
22C, cosubstrate: IMP
1.1
GTP
-
pH 7.5
1.4
GTP
-
-
1.59
GTP
-
pH 7.8, 25C, wild-type
1.99
GTP
-
pH 7.7, 25C, mutant V273T
2.94
GTP
-
pH 7.8, 25C, wild-type
2.94
GTP
-
pH 7.7, 25C, mutant V273T
3.3
GTP
-
pH 7.7, 25C, mutant T300V
3.9
GTP
-
pH 6.7, 22C, AdSS1-Tr
4
GTP
-
pH 6.7, 22C, AdSS2-Tr
4.2
GTP
-
pH 6.7, 22C, AdSS2
4.2
GTP
Q57981
pH 6.0, 70C
5.4
GTP
-
pH 6.7, 22C, AdSS1
5.5
GTP
P28650
22C, cosubstrate: 2'-dIMP
6.08
GTP
-
pH 7.7, 25C, mutant T42A
6.08
GTP
-
pH 7.7, 25C, mutant T300A
0.08
hydroxylamine
-
pH 7.7, 25C, mutant V273T
0.21
hydroxylamine
-
pH 7.7, 25C, mutant V273A
0.24
hydroxylamine
-
pH 7.7, 25C, mutant T301A
0.29
hydroxylamine
-
pH 7.7, 25C, mutant V273N
0.5
hydroxylamine
-
pH 7.7, 25C, wild-type
0.0038
IMP
-
mutant R155A, pH 7.0, 25C
0.01
IMP
-
mutant R155L, pH 7.0, 25C
0.112
IMP
-
mutant R155K, pH 7.0, 25C
0.32
IMP
-
mutant N429V, pH 7.0, 37C
0.45
IMP
Q57981
pH 6.0, 70C
0.62
IMP
-
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.7
IMP
-
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25C
0.84
IMP
-
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25C
1
IMP
-
22C
1
IMP
-
wild-type, pH 7.0, 25C
1
IMP
-
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25C
1.09
IMP
-
mutant K62L, pH 7.0, 37C
1.1
IMP
-
pH 7.5
1.1
IMP
-
wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25C
1.44
IMP
-
wild-type, pH 7.0, 37C
1.7
IMP
-
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25C
1.72
IMP
-
mutant T307V, pH 7.0, 37C
4.2
IMP
Q57981
pH 6.0, 70C
0.96
L-Asp
-
22C, cosubstrate: 2'-dIMP
1
L-Asp
-
22C, cosubstrate: IMP
5.5
L-Asp
P28650
22C, cosubstrate: 2'-dIMP
0.45
L-aspartate
Q57981
pH 6.0, 70C
1.1
L-aspartate
-
pH 7.5
4.2
L-aspartate
Q57981
pH 6.0, 70C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0406
6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-monophosphate
-
pH 7.0, 25C
0.0094
adenylosuccinate
Q57981
pH 6.0, 70C, competitive inhibition of IMP
0.016
adenylosuccinate
-
pH 6.7, 22C, AdSS2
0.021
adenylosuccinate
-
pH 6.7, 22C, AdSS1
0.029
adenylosuccinate
-
pH 7.5
0.0426
adenylosuccinate
Q57981
pH 6.0, 70C, noncompetitive inhibition of aspartate
0.0429
adenylosuccinate
Q57981
pH 6.0, 70C, noncompetitive inhibition of GTP
2.7
adenylosuccinate
-
pH 8.0, 25C
0.0582
AMP
Q57981
pH 6.0, 70C, competitive inhibition of IMP
0.059
AMP
-
pH 6.7, 22C, AdSS2
0.066
AMP
-
pH 7.5
0.324
AMP
Q57981
pH 6.0, 70C, noncompetitive inhibition of aspartate
0.402
AMP
Q57981
pH 6.0, 70C, noncompetitive inhibition of GTP
0.7
AMP
-
pH 6.7, 22C, AdSS1
6
AMP
-
pH 8.0, 25C
4
ATP
-
pH 8.0, 25C
8
Cl-
-
pH 8.0, 25C
1.5
D-fructose 1,6 bisphosphate
Q57981
pH 6.0, 70C, competitive inhibition of IMP
4.8
D-fructose 1,6 bisphosphate
Q57981
pH 6.0, 70C, competitive inhibition of GTP
0.016
D-fructose 1,6-bisphosphate
-
pH 6.7, 22C, AdSS1, noncompetitive inhibition relative to IMP
0.019
D-fructose 1,6-bisphosphate
-
pH 6.7, 22C, AdSS2, noncompetitive inhibition relative to IMP
0.046
D-fructose 1,6-bisphosphate
-
pH 6.7, 22C, AdSS1
0.063
D-fructose 1,6-bisphosphate
-
pH 6.7, 22C, AdSS1, noncompetitive inhibition relative to GTP
0.081
D-fructose 1,6-bisphosphate
-
pH 6.7, 22C, AdSS1, noncompetitive inhibition relative to L-aspartate
0.128
D-fructose 1,6-bisphosphate
-
pH 6.7, 22C, AdSS2
0.4
D-fructose 1,6-bisphosphate
-
pH 6.7, 22C, AdSS2, noncompetitive inhibition relative to GTP
0.67
D-fructose 1,6-bisphosphate
-
pH 6.7, 22C, AdSS2, noncompetitive inhibition relative to L-aspartate
0.04
fumarate
-
pH 7.7, 25C, mutant V273N
0.18
fumarate
-
pH 7.7, 25C, mutant V273A
0.64
fumarate
-
pH 7.7, 25C, mutant V273T
0.0053
GDP
-
pH 7.5
0.007
GDP
Q57981
pH 6.0, 70C, competitive inhibition of GTP
0.019
GDP
-
pH 6.7, 22C, AdSS1
0.03
GDP
-
pH 6.7, 22C, AdSS2
0.0821
GDP
Q57981
pH 6.0, 70C, noncompetitive inhibition of aspartate
0.0822
GDP
Q57981
pH 6.0, 70C, noncompetitive inhibition of IMP
0.012
GMP
-
pH 6.7, 22C, AdSS1
0.0137
GMP
Q57981
pH 6.0, 70C, noncompetitive inhibition of GTP
0.014
GMP
-
pH 6.7, 22C, AdSS2
0.019
GMP
-
pH 7.5
0.057
GMP
-
pH 8.0, 25C
0.11
GMP
Q57981
pH 6.0, 70C, noncompetitive inhibition of IMP
0.12
GMP
Q57981
pH 6.0, 70C, noncompetitive inhibition of asparate
0.00032
Hadacidin
P28650
reaction with IMP
0.00049
Hadacidin
-
22C, reaction with IMP
0.01
Hadacidin
-
-
0.014
Hadacidin
P28650
reaction with 2'-dIMP
0.017
Hadacidin
-
22C, reaction with 2'-dIMP
0.078
Maleate
-
pH 7.7, 25C, mutant V273T
0.21
Maleate
-
pH 7.7, 25C, mutant V273N
1
Maleate
-
pH 7.7, 25C, mutant V273A
3.1
Maleate
-
pH 7.7, 25C, wild-type
0.0105
N-formyl-N-hydroxyglycine
Q57981
pH 6.0, 70C, competitive inhibition of asparate
-
0.0264
N-formyl-N-hydroxyglycine
Q57981
pH 6.0, 70C, uncompetitive inhibition of IMP
-
0.0269
N-formyl-N-hydroxyglycine
Q57981
pH 6.0, 70C, uncompetitive inhibition of GTP
-
1.9
phosphate
Q57981
pH 6.0, 70C, competitive inhibition of IMP
8.3
phosphate
Q57981
pH 6.0, 70C, competitive inhibition of GTP
28
phosphate
-
pH 7.0, 37C
0.08
succinate
-
pH 7.7, 25C, mutant V273T
0.89
succinate
-
pH 7.7, 25C, wild-type
1
succinate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00207
-
enzyme from guaBDELTACBS mutant crude extract
0.00493
-
enzyme from wild type crude extract
0.00641
-
-
3.84
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
-
mutant Q224E
6.3 - 6.8
-
-
6.5 - 7.4
-
-
6.8 - 7
-
-
7.7 - 8.7
-
-
7.7
-
wild-type
7.8
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2 - 8
-
-
5.5 - 8.5
-
50% of maximal activity at pH 5.5 and 8.5
6 - 8
-
50% of maximal activity at pH 6.0 and 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.9
-
acidic isoenzyme
7
-
calculated from amino acid sequence
8.7
A4Z6H0, A4Z6H1
calculated from sequence
8.9
-
most abundant isozyme
8.9
-
basic isoenzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q8N142
stromal cell, isoenzyme AdSS1
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
low level
Manually annotated by BRENDA team
Q8N142
isoenzyme AdSS1
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
-
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
weak expression level of ADSS2 mRNA
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
high expression level of ADSS2 mRNA
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
high expression level of ADSS2 mRNA
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
high expression level of ADSS2 mRNA
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
ADSS1 is predominantly expressed in the striated muscle tissue, ADSS1 is up-regulated significantly along with muscle growth
Manually annotated by BRENDA team
Q8N142
isoenzyme AdSS1
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
weak expression level of ADSS2 mRNA
Manually annotated by BRENDA team
-
adenylosuccinate synthetase expression is downregulated in SM-5 cells
Manually annotated by BRENDA team
-
adenylosuccinate synthetase expression is downregulated in SM-7 cells
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
high expression level of ADSS2 mRNA
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
high expression level of ADSS2 mRNA
Manually annotated by BRENDA team
-
adenylosuccinate synthetase expression is downregulated in thymic lymphoma cells
Manually annotated by BRENDA team
A4Z6H0, A4Z6H1
high expression level of ADSS2 mRNA
Manually annotated by BRENDA team
additional information
-
tissue distribution of L-isozyme and M-isozyme
Manually annotated by BRENDA team
additional information
A4Z6H0, A4Z6H1
ADSS1 is undetectable in lung, liver, spleen, stomach, fat, lymph, kidney, and intestine
Manually annotated by BRENDA team
additional information
A4Z6H0, A4Z6H1
expression of ADSS2 gene is relatively constant in the prenatal period and remains constant at a relatively higher expression level in postnatal period
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q8N142
expression in COS-7 cells
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45190
-
calculated from amino acid sequence
695062
47000
-
SDS-PAGE
649670
48000
-
theoretical molecular mass
649670
48000
-
SDS-PAGE
651884
48000
-
gel filtration, mutant R155A/G146R, plus small peak of dimeric enzyme
714324
50000
-
gel filtration
1572
55000 - 60000
-
liver and Novikoff ascites cells
1537
77000
-
gel filtration
649670
86000
-
equilibrium sedimentation ultracentrifugation, AdSS1
652500
89000
-
gel filtration
727078
90000 - 105000
-
skeletal muscle, heart, liver, gel filtration
1543
90700
-
equilibrium sedimentation ultracentrifugation, AdSS2
652500
92000
-
gel filtration, wild-type and mutants N429V, K62L, T307V, R155V, R155K, R155A
714324
96000
-
-
1533
100000
-
calculated from amino acid sequence
727078
100700
-
predicted from amino acid sequence, AdSS2
652500
101100
-
predicted from amino acid sequence, AdSS1
652500
102000
-
Yoshida sarcoma ascites tumor cells, sedimentation equilibrium analysis
1539
104000
-
sedimentation equilibrium analysis
1546
105000
-
gel filtration
653751
109000
-
gel filtration, in the absence of denaturant AdSS elutes as a single peak corresponding to a molecular mass of 109000 Da, which is indicative of dimer-tetramer equilibrium
691098
110000
-
gel filtration
1544
141000
-
HPLC gel filtration
1534
160000
-
gel filtration, in 20 mM Tris-HCl, pH 7.4
691098
250000
-
gel filtration
1541
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 47000, sedimentation equilibrium analysis in presence of 6 M guanidine-HCl
dimer
-
2 * 48000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 44000-46000, SDS-PAGE, liver, 2 * 53000-54000, heart, skeletal muscle, SDS-PAGE
dimer
-
2 * 50000, recombinant protein, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE, recombinant enzyme
dimer
-
2 * 79000, gel filtration, AdSS exhibits dimer-tetramer equilibrium with the equilibrium shifting towards the dimer in the presence of 100 mM NaCl
dimer
-
2 * 50000, calculated, wild-type
dimer
-
1 * 80000, the enzyme mainly exists as dimer in solution, SDS-PAGE
dimer
Q57981
2 * 37855, MALDI mass spectrometric analysis, equilibrium mixture of dimers and tetramers with the tetramer being the catalytically active form. The tetramer dissociates into dimers with a minor increase in ionic strength of the buffer, while the dimer is extremely stable and does not dissociate even at 1.2 M NaCl
dimer
Pyrococcus horikoshii OT-3
-
1 * 80000, the enzyme mainly exists as dimer in solution, SDS-PAGE
-
homodimer
-
-
homodimer
-
2 * 50000, SDS-PAGE
homodimer
-
2 * 46000, SDS-PAGE
homodimer
O24396
2 * 55000
homodimer
Q96529
2 * 55000
homodimer
-
2 * 46600
homodimer
Cryptococcus neoformans H99
-
2 * 46000, SDS-PAGE
-
tetramer
-
4 * 38000, gel filtration and dynamic light scattering, AdSS exhibits dimer-tetramer equilibrium with the equilibrium shifting towards the dimer in the presence of 100 mM NaCl
tetramer
Q57981
4 * 37855, MALDI mass spectrometric analysis, equilibrium mixture of dimers and tetramers with the tetramer being the catalytically active form. The tetramer dissociates into dimers with a minor increase in ionic strength of the buffer, while the dimer is extremely stable and does not dissociate even at 1.2 M NaCl
monomer
-
1 * 47933, calculation from amino acid sequence, 1 * 48000, SDS-PAGE
additional information
-
conserved arginine residue R155 is involved in dimer crosstalk and interacts with IMP in the active site of the symmetry related subunit
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
space group I23, cell constants a = b = c = 212.76 A
Q96529
hanging drop vapor diffusion method, using 0.1 M bis-Tris propane pH 8, 0.2 M sodium bromide, 17% (w/v) polyethylene glycol 3350
-
crystal structure of guanine nucleotide complexes of adenylosuccinate synthetase
-
crystal structure of the enzyme complexed with GDP, IMP hadacidin, NO3-, and Mg2+
-
crystal structure of unligated enzyme
-
crystals grown by the method of hanging drops
-
entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli
-
hanging drop method, GDP-2'-deoxy-6-phosphoryl-IMP-hadacidin complex
-
crystals grown by the method of hanging drops, space group P4(#)2(1)2, a = b = 69.93, c = 198.49
-
crystals grown by the method of hanging drops, space group P4(3)2(1)2, unit cell parameters a = b = 70.24 A, c = 199.14 A
P28650
hanging drop method, GDP-2'-deoxy-6-phosphoryl-IMP complex
P28650
enzyme-hydantocidin complex at 2.6 A resolution
-
space group C222(1), cell parameters a = 91.58 A, b = 117.12 A, c = 80.42A
-
sitting-drop vapour-diffusion method. Crystal belong to the trigonal space group P3(2)12, with unit-cell parameters a = b = 57.2, c = 107.9 A. There is a single molecule in the asymmetric unit
-
space group P4(1)2(1)2, cell constants a = b = 151.44 A, c = 91.94A
O24396
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
most stable at pH 7.0 in phosphate buffer
1539
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 90
-
thermal unfolding of AdSS exhibits a melting temperature of 85C with the process being only partially reversible, the half life of inactivation is 340 min, 150 min, 110 min, 60 min, 30 min and 15 min at 65, 70, 75, 80, 85 and 90C, respectively
691098
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
GTP and IMP stabilize the dimeric structure
-
completely destroyed by freezing
-
at 1.5 M urea the enzyme dissociates to form monomers and further increase in urea concentration causes unfolding of this species
-
requires presence of dithiothreitol during the entire course of purification for activity
-
purified enzyme is not stable, loses its activity within weeks
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
-
dramatic loss in secondary structure above 4 M guanidine-HCl with complete loss in secondary structure at 5 M guanidine-HCl
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, stable for more than 2 years
-
-20C, stable without any decrease in activity for at least 6 months
Q57981
4C, glycerol and EDTA stabilizes enzyme activity during storage, stable for at least 3 weeks
-
-20C, or 0C, rapid loss of enzyme activity in dilute solution
-
-20C, remains stable for months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
-
mutant enzymes R303L, R304L, and R305L
-
wild-type and mutant enzymes
-
partial
-
recombinant enzyme
Q8N142
recombinant enzyme
-
ammonium sulfate precipitation, anion exchange chromatography, and gel filtration
-
recombinant protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA expressed in Escherichia coli
Q96529
expressed in Escherichia coli BL21(DE3)pLysS cells
-
cloned into the temperature-inducible, high-copy-number plasmid vector, pMOB45. Upon temperature induction, cells containing this plasmid produce adenylosuccinate synthetase at approximately 40times the wild-type level
-
purA gene
-
purA gene overexpressed in strain H1238
-
overexpression in COS-7 cells
Q8N142
expressed in Escherichia coli BL21 (DE3) cells
-
expression in Escherichia coli BL21
Q57981
-
P28650
Adss1 gene, transient transfection into Rattus norvegicus primary cardiomyocytes, cotransfection into CV1 fibroblasts
-
expressed in Escherichia coli BL21 (DE3)
-
gene Adss1, quantitative RT-PCR analysis
-
mouse muscle gene AdSS1 and mouse nonmuscle gene AdSS2
-
overexpressed in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
hyperexpressed in Escherichia coli BL21 (DE3), complementation of purA mutant strain H1238
-
expression in Escherichia coli
-
expression in Escherichia coli. The archaeal adenylosuccinate synthetase has a significant number of substitutions in residues that are conserved in all other homologous enzymes from bacteria to man. Despite theses differences the purA-like archaeal gene seems to be normally expressed and its product functions in vivo in bacteria, since it complements an Escherichia coli purA auxotroph; the archaeal adenylosuccinate synthase has a significant number of substitutions in residues that are conserved in all other homologous enzymes from bacteria to human. In Escherichia coli, the conserved residues are essential for catalytic activity and/or for the folded structure of the homodimer. Despite these drastic differences, the purA-like archaeal gene is normally expressed and its product functions in vivo in bacteria, since it complements an Escherichia coli purA auxotroph
Q59726
gene Adss1, quantitative RT-PCR analysis
-
;
A4Z6H0, A4Z6H1
cDNA expressed in Escherichia coli
O24396
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D13A
-
mutant enzyme D13A shows no measurable activity, mutant enzymes E14A and H41N exhibit 1% of the activity of the wild-type enzyme and 2-7fold increases in Km of substrates. The mutant enzyme K16Q has 34% of the activity of wild-type enzyme and Km values for substrates are virtually unchanged from those of the wild-type enzyme
D21A
-
directed mutagenesis
D231A
-
wild-type and mutant enzymes, R132K, R143L, and D231A exist as a mixture of monomers and dimers, with a majority of the enzyme in the monomeric state. In the presence of active site ligands, the wild-type enzyme exists almost exclusively as a dimer, whereas the mutant enzymes show only slightly decreased dissociation constants for the dimerization
D333E
-
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme
D333N
-
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme
D333Q
-
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme
E14A
-
mutant enzyme D13A shows no measurable activity, mutant enzymes E14A and H41N exhibit 1% of the activity of the wild-type enzyme and 2-7fold increases in Km of substrates. The mutant enzyme K16Q has 34% of the activity of wild-type enzyme and Km values for substrates are virtually unchanged from those of the wild-type enzyme
G12V
-
replacement of Gly12, Gly15, or Gly17 with Val, or replacement of Lys18 with Arg, results in significant decrease in the kcat/Km values of the enzyme
G15V
-
the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP
G17V
-
replacement of Gly12, Gly15, or Gly17 with Val, or replacement of Lys18 with Arg, results in significant decrease in the kcat/Km values of the enzyme
H41N
-
mutant enzyme D13A shows no measurable activity, mutant enzymes E14A and H41N exhibit 1% of the activity of the wild-type enzyme and 2-7fold increases in Km of substrates. The mutant enzyme K16Q has 34% of the activity of wild-type enzyme and Km values for substrates are virtually unchanged from those of the wild-type enzyme
H41N
-
site-directed mutagenesis
K16Q
-
site-directed mutagenesis
K331l
-
the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP
K331R
-
the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP
L18R
-
replacement of Gly12, Gly15, or Gly17 with Val, or replacement of Lys18 with Arg, results in significant decrease in the kcat/Km values of the enzyme
N38A
-
site-directed mutagenesis
N38A
-
directed mutagenesis
N38D
-
directed mutagenesis
N38E
-
directed mutagenesis
Q224M
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
Q34E
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
R132L
-
wild-type and mutant enzymes, R132K, R143L, and D231A exist as a mixture of monomers and dimers, with a majority of the enzyme in the monomeric state. In the presence of active site ligands, the wild-type enzyme exists almost exclusively as a dimer, whereas the mutant enzymes show only slightly decreased dissociation constants for the dimerization
R143K
-
site-directed mutagenesis
R143L
-
mutant enzyme R143L with no change in catalytic constant or Km for Asp, but significantly impaired nucleotide binding, 60fold increased Km for IMP and 10fold increased Km for GTP
R143L
-
although the mutants R143L and D13A have low or no activity independently, when they are mixed, a significant amount of activity is obtained. These results indicate that the subunits exchange with each other to form heterodimers with a single viable active site
R143L
-
site-directed mutagenesis
R147L
-
mutant R147L shows increased Km for IMP and GTP relative to the wild-type enzyme, Km for Asp exhibits a modest decrease
R303L
-
mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable
R303L
-
site-directed mutagenesis
R304L
-
mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable
R304L
-
site-directed mutagenesis
R305L
-
mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable
R305L
-
site-directed mutagenesis
R419L
-
directed mutagenesis
S240A
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
S240E
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
T128A
-
site-directed mutagenesis
T129A
-
site-directed mutagenesis
T300A
-
site-directed mutagenesis
T301A
-
site-directed mutagenesis
T42A
-
directed mutagenesis
V273A
-
site-directed mutagenesis
V273N
-
site-directed mutagenesis
V273T
-
site-directed mutagenesis
C328D
-
the mutant shows reduced Km and increased turnover number for L-aspartate compared to the wild type protein
C328D/C368D
-
the mutant shows reduced Km and turnover number for L-aspartate compared to the wild type protein
C328S
-
the mutant exhibits no change in the aspartate Km value but reduced turnover number compared to the wild type protein
C328S/C368S
-
the mutant shows a 4fold reduced Km for aspartate and reduced turnover number compared to the wild type protein
C368S
-
the mutant exhibits a 1.7fold increase in the aspartate Km value compared to the wild type protein
K62L
-
increase in Km values for IMP, GTP and aspartate, respectively
N429V
-
increase in Km values for IMP, GTP and aspartate, respectively, along with a 5 fold drop in the kcat value
R155A
-
residue influences both ligand binding and catalysis
R155A/G146R
-
unlike dimeric wild-type, mainly monomeric. Inactive
R155K
-
residue influences both ligand binding and catalysis
R155L
-
residue influences both ligand binding and catalysis
T307V
-
increase in Km values for IMP, GTP and aspartate, respectively
L228A
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
additional information
-
the activity of AMPsS in crude dialyzed cell extracts is 2times lower in the guaBDELTACBS mutant compared with the wild type strain
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
the adenylosuccinate synthase gene is not associated with susceptibility for schizophrenia
medicine
-
genetic variation of inosine triphosphatase causing an accumulation of inosine triphosphate protects patients against ribavirin-induced anemia during treatment for chronic hepatitis C infection. ITP can be used for ATP biosynthesis via adenylosuccinate synthase in place of guanosine triphosphate. With ribavirin challenge, erythrocyte ATP reduction is more severe in the wild-type inosine triphosphatase ITPA genotype than in the hemolysis protective ITPA genotype. The alleviation of ATP reduction by the hemolysis protective ITPA genotype is canceled by the adenylosuccinate synthase inhibitor 6-mercaptoethanol
medicine
-
enzymes of the salvage pathway are good targets for anti-parasitic drugs
medicine
-
most parasitic protozoa lack the de novo purine biosynthetic pathway and rely exclusively on the salvage pathway for their purine biosynthetic pathway, enzymes of the salvage pathway are candidate drug targets
agriculture
-
target of herbicides
medicine
-
target of drugs