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Information on EC 6.3.4.4 - adenylosuccinate synthase
for references in articles please use BRENDA:EC6.3.4.4
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.4 Other carbon-nitrogen ligases
6.3.4.4 adenylosuccinate synthase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 6.3.4.4
- purine
- gtp
- inosine
- hadacidin
- hypoxanthine
- formycin
- adenylosuccinase
-
alanosine
- medicine
-
saicar
- synthesis
- agriculture
showSynonyms
adenylosuccinate synthetase, adssl1, adss1, adenylosuccinate synthase, pfadss, adss2, ampss, succino-amp synthetase, adenylosuccinate synthetase 1, as-synthetase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADE12
adenosylsuccinate synthetase
adenylo-succinate synthetase
Adenylosuccinate synthase
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-
-
-
Adenylosuccinate synthetase
AdSS
AdSS1
AdSS2
AMPSase
ASS
IMP--aspartate ligase
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-
-
-
IMP-aspartate ligase
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-
-
-
MGG_17000
PfAdSS
purA
Succino-AMP synthetase
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-
-
-
Succinoadenylic kinosynthetase
-
-
-
-
Adenylosuccinate synthetase
-
-
-
-
AdSS
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-
-
-
AMPSase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
fully random mechanism
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
sequential rapid equilibrium fully random mechanism
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
fully random terter mechanism
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
random sequential binding mechanism
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
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
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
sequential mechanism with a fully random order of substrate addition
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
rapid equilibrium random AB steady-state ordered C kinetic mechanism
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
rapid equilibrium random AB steady-state ordered C kinetic mechanism
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
adenosine ribonucleotides de novo biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
IMP:L-aspartate ligase (GDP-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9023-57-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-dGTP + IMP + L-aspartate
2'-dGDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
ddGTP + IMP + L-aspartate
ddGDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
GTP + IMP + Ala-3-nitronate
GDP + phosphate + N6-(L-1-carboxy-2-nitroethyl)AMP
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + hydroxylamine
GDP + phosphate + ?
Substrates: -
Products: -
Products: -
?
ITP + IMP + L-aspartate
IDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
UTP + IMP + L-Asp
UDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
XTP + IMP + L-Asp
XDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
Substrates: -
Products: -
Products: -
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
Substrates: -
Products: -
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?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
Substrates: -
Products: -
Products: -
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
Substrates: -
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?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
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Substrates: 61% of the efficiency of IMP as substrate, V/Km
Products: -
Products: -
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
Substrates: -
Products: -
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?
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
-
Substrates: -
Products: -
Products: -
?
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
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Substrates: i.e. allopurinol ribonucleotide
Products: -
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?
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
-
Substrates: -
Products: -
Products: -
?
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
-
Substrates: -
Products: -
Products: -
?
GTP + 8-azaIMP + L-Asp
GDP + phosphate + 8-azasuccinoAMP
-
Substrates: -
Products: -
Products: -
?
GTP + 8-azaIMP + L-Asp
GDP + phosphate + 8-azasuccinoAMP
-
Substrates: -
Products: -
Products: -
?
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
-
Substrates: -
Products: -
Products: -
?
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
-
Substrates: -
Products: -
Products: -
?
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
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Substrates: 8.8% of the efficiency of IMP as substrate , V/Km
Products: -
Products: -
?
GTP + beta-D-arabinosylIMP + L-Asp
GDP + phosphate + arabinosylsuccinoAMP
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
?
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Substrates: penultimate step in pathway of AMP biosynthesis
Products: -
Products: -
?
GTP + IMP + L-Asp
?
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Substrates: plays an important role in the interconversion of purines
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Products: -
?
GTP + IMP + L-Asp
?
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Substrates: plays an important role in the interconversion of purines
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Products: -
?
GTP + IMP + L-Asp
?
-
Substrates: first committed step towards the de novo biosynthesis of AMP
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Products: -
?
GTP + IMP + L-Asp
?
-
Substrates: first committed step towards the de novo biosynthesis of AMP
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: r
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
Escherichia coli B / ATCC 11303
-
Substrates: -
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Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: catalyzing the first step in the de novo synthesis of adenylmonophosphate
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: catalyzes the first step in the conversion of IMP to AMP in de novo purine nucleotide metabolism
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: catalyzing the first committed step in de novo biosynthesis of AMP
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: catalyzing the first committed step in the biosynthesis of AMP
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: 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
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: 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
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: first committed step in AMP synthesis. Isoenzyme AdSS1 has a potential role in muscle metabolism
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: catalyzes the first committed step in the de novo biosynthesis of AMP
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: governs the committed step of AMP biosynthesis
Products: -
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GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: acidic and basic isozymes, which participates in the first committed step of de novo AMP biosynthesis and/or the purine nucleotide cycle
Products: -
Products: -
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GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: salvage pathway
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GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: salvage pathway, catalyzing the first committed step in the synthesis of AMP from IMP
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GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
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Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: function in adenine nucleotide biosynthesis
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GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
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GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: 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
Products: -
Products: -
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GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
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GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: catalyzing the first step in the de novo sythesis of adenylmonophosphate
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
Substrates: -
Products: i.e. adenylosuccinate
Products: i.e. adenylosuccinate
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
Substrates: -
Products: i.e. adenylosuccinate
Products: i.e. adenylosuccinate
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
Substrates: function in adenine nucleotide biosynthesis
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
Substrates: -
Products: -
Products: -
?
ITP + IMP + L-Asp
IDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
ITP + IMP + L-Asp
IDP + phosphate + adenylosuccinate
-
Substrates: -
Products: ITP can be used for ATP biosynthesis via adenylosuccinate synthase in place of guanosine triphosphate
Products: ITP can be used for ATP biosynthesis via adenylosuccinate synthase in place of guanosine triphosphate
?
additional information
?
-
-
Substrates: vertebrates possess two isozymes, the acidic is similar to the synthetase from bacteria and plants, the basic isozyme participates in the purine nucleotide cycle
Products: -
Products: -
?
additional information
?
-
-
Substrates: ATP cannot be used as substrate instead of GTP
Products: -
Products: -
?
additional information
?
-
-
Substrates: ATP is no substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
Substrates: function in adenine nucleotide biosynthesis
Products: -
Products: -
?
GTP + IMP + L-Asp
?
-
Substrates: penultimate step in pathway of AMP biosynthesis
Products: -
Products: -
?
GTP + IMP + L-Asp
?
-
Substrates: plays an important role in the interconversion of purines
Products: -
Products: -
?
GTP + IMP + L-Asp
?
-
Substrates: plays an important role in the interconversion of purines
Products: -
Products: -
?
GTP + IMP + L-Asp
?
-
Substrates: first committed step towards the de novo biosynthesis of AMP
Products: -
Products: -
?
GTP + IMP + L-Asp
?
-
Substrates: first committed step towards the de novo biosynthesis of AMP
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: catalyzing the first step in the de novo synthesis of adenylmonophosphate
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: catalyzes the first step in the conversion of IMP to AMP in de novo purine nucleotide metabolism
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: catalyzing the first committed step in de novo biosynthesis of AMP
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: catalyzing the first committed step in the biosynthesis of AMP
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: 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
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: 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
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: first committed step in AMP synthesis. Isoenzyme AdSS1 has a potential role in muscle metabolism
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: catalyzes the first committed step in the de novo biosynthesis of AMP
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: governs the committed step of AMP biosynthesis
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: acidic and basic isozymes, which participates in the first committed step of de novo AMP biosynthesis and/or the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: salvage pathway
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: salvage pathway, catalyzing the first committed step in the synthesis of AMP from IMP
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: function in adenine nucleotide biosynthesis
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: 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
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: -
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
Substrates: catalyzing the first step in the de novo sythesis of adenylmonophosphate
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
Substrates: first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Cu2+
Mg2+
Mn2+
additional information
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+
requires Mg2+ for catalysis with maximum activity obtained at 15 mM magnesium acetate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-fructose 1,6 bisphosphate
competitive with IMP and noncompetitive against GTP
Guanosine 5'-diphosphate-3'-diphosphate
-
competitive with respect to GTP and noncompetitive with respect to L-Asp and IMP
N-formyl-N-hydroxyglycine
i.e. hadacidin. competitive inhibitor of aspartate, showed uncompetitive inhibition with IMP and GTP
N-[4-([9-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]-9H-purin-6-yl]amino)butyl]-N-hydroxyformamide
-
40% inhibition at 10 mM
-
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
adenylosuccinate
competitive inhibitor of IMP, noncompetitive inhibitor of GTP and aspartate
adenylosuccinate
-
competitive versus IMP, non-competitive versus GTP and aspartate
AMP
competitive with respect to IMP and noncompetitive with GTP and aspartate
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
fructose 1,6-diphosphate
-
basic type M isozym more strongly inhibited than acidic type L isozym
GDP
competitive inhibitor of GTP, noncompetitive inhibitor with IMP and aspartate
GDP
-
uncompetitive versus IMP, competitive versus GTP and non-competitive versus aspartate
GMP
competitive with respect to GTP and noncompetitive with IMP and aspartate
GMP
-
uncompetitive versus IMP, competitive versus GTP and non-competitive versus aspartate
Hadacidin
-
uncompetitive versus IMP and GTP, competitive versus aspartate
IMP
inhibits the enzyme activity at subsaturating GTP concentrations
IMP
-
competitive inhibition of the acidic isozyme, noncompetitive of the basic isozyme
phosphate
potent inhibitor, biphasic inhibition, competitive with IMP and noncompetitive with GTP
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
-
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
-
GMP is not a strong inhibitor of AMPsS at physiological concentrations
-
additional information
cellular uptake by Helicobacter pylori of formycins and hadacidin inhibitors is very poor. A cell penetration assessment method is developed for validating the cellular uptake of other drug candidates
-
additional information
-
negligible inhibition by adenine nucleotides
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-fructose 1,6 bisphosphate
binds to the Asp loop and induces a conformation that facilitates aspartate binding to the enzyme active site
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis
Effect of acidosis and uninephrectomy on isozymes of adenylosuccinate synthetase in rat kidney.
Adenocarcinoma of Lung
Adenylosuccinate synthetase 1 gene is a novel target of deletion in lung adenocarcinoma.
adenylosuccinate lyase deficiency
Adenylosuccinate Synthetase and Adenylosuccinate Lyase Deficiencies Trigger Growth and Infectivity Deficits in Leishmania donovani.
Ataxia Telangiectasia
Association analyses of the interaction between the ADSS and ATM genes with schizophrenia in a Chinese population.
Carcinogenesis
Adenylosuccinate synthetase 1 gene is a novel target of deletion in lung adenocarcinoma.
Carcinoma
Regulation of purine metabolism: a comparative study of the kinetic properties of adenylosuccinate synthetases from various sources.
Carcinoma 256, Walker
Regulation of purine metabolism: a comparative study of the kinetic properties of adenylosuccinate synthetases from various sources.
Cardiomegaly
The adenylosuccinate synthetase-1 gene is activated in the hypertrophied heart.
Distal Myopathies
ADSSL1 mutation relevant to autosomal recessive adolescent onset distal myopathy.
Distal Myopathies
Comparative transcriptome analysis of skeletal muscle in ADSSL1 myopathy.
Distal Myopathies
Expanding the disease phenotype of ADSSL1-associated myopathy in non-Korean patients.
Gout
Purine oversecretion in cultured murine lymphoma cells deficient in adenylosuccinate synthetase: genetic model for inherited hyperuricemia and gout.
Infections
Genome-wide identification of Streptococcus pneumoniae genes essential for bacterial replication during experimental meningitis.
Insulinoma
Adenylosuccinate Is an Insulin Secretagogue Derived from Glucose-Induced Purine Metabolism.
Leukemia
Identification of the antimetabolite of L-alanosine, L-alanosyl-5-amino-4-imidazolecarboxylic acid ribonucleotide, in tumors and assessment of its inhibition of adenylosuccinate synthetase.
Leukemia
Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells.
Leukemia, Experimental
Synthesis and in vitro biological evaluation of N-[(5-amino-1-beta-D-ribofuranosyl-1H-imidazol-4-yl)carbonyl]-3- (hydroxynitrosamino)-L-alanine (L-alanosine AICO ribonucleoside).
Lung Neoplasms
Adenylosuccinate synthetase 1 gene is a novel target of deletion in lung adenocarcinoma.
Lymphoma
Purine oversecretion in cultured murine lymphoma cells deficient in adenylosuccinate synthetase: genetic model for inherited hyperuricemia and gout.
Lymphoma, T-Cell
Abnormal regulation of de novo purine synthesis and purine salvage in a cultured mouse T-cell lymphoma mutant partially deficient in adenylosuccinate synthetase.
Lymphoma, T-Cell
Abnormal regulation of purine metabolism in a cultured mouse T-cell lymphoma mutant partially deficient in adenylosuccinate synthetase.
Malaria
Crystal structure of fully ligated adenylosuccinate synthetase from Plasmodium falciparum.
Malaria
Enrichment of reticulocytes from whole blood using aqueous multiphase systems of polymers.
Meningitis, Pneumococcal
Genome-wide identification of Streptococcus pneumoniae genes essential for bacterial replication during experimental meningitis.
Muscle Cramp
Enzymes of the purine nucleotide cycle in muscle of patients with exercise intolerance.
Muscle Weakness
Expanding the disease phenotype of ADSSL1-associated myopathy in non-Korean patients.
Muscular Diseases
ADSSL1 mutation relevant to autosomal recessive adolescent onset distal myopathy.
Muscular Diseases
ADSSL1 myopathy is the most common nemaline myopathy in Japan with variable clinical features.
Muscular Diseases
Anti-apoptotic Effects of Human Wharton's Jelly-derived Mesenchymal Stem Cells on Skeletal Muscle Cells Mediated via Secretion of XCL1.
Muscular Diseases
Comparative transcriptome analysis of skeletal muscle in ADSSL1 myopathy.
Muscular Diseases
Enzymes of the purine nucleotide cycle in muscle of patients with exercise intolerance.
Muscular Dystrophy, Duchenne
Identifying and circumventing the defect in Duchenne muscular dystrophy: clinical and biochemical restoration after practical intervention.
Myopathies, Nemaline
ADSSL1 myopathy is the most common nemaline myopathy in Japan with variable clinical features.
Neoplasms
Adenylosuccinate synthetase 1 gene is a novel target of deletion in lung adenocarcinoma.
Neoplasms
Identification of differentially expressed proteins in spontaneous thymic lymphomas from knockout mice with deletion of p53.
Neoplasms
Identification of the antimetabolite of L-alanosine, L-alanosyl-5-amino-4-imidazolecarboxylic acid ribonucleotide, in tumors and assessment of its inhibition of adenylosuccinate synthetase.
Neoplasms
Molecular transformation of tumor adenylosuccinate synthetase and characteristics of its converting factor.
Neoplasms
Oxidation of glutamine in cancer cells and regeneration of adenylates via adenylosuccinate synthetase.
Neoplasms
Purification and properties of adenylosuccinate synthetase from Yoshida sarcoma ascites tumor cells.
Neoplasms
Regulation of purine metabolism. Adenylosuccinate synthetase from Novikoff ascites tumor cells.
Neoplasms
Regulation of purine metabolism: a comparative study of the kinetic properties of adenylosuccinate synthetases from various sources.
Neoplasms
Synthesis and in vitro biological evaluation of N-[(5-amino-1-beta-D-ribofuranosyl-1H-imidazol-4-yl)carbonyl]-3- (hydroxynitrosamino)-L-alanine (L-alanosine AICO ribonucleoside).
Sarcoma, Yoshida
Molecular transformation of tumor adenylosuccinate synthetase and characteristics of its converting factor.
Sarcoma, Yoshida
Purification and properties of adenylosuccinate synthetase from Yoshida sarcoma ascites tumor cells.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0172
GTP
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0206
GTP
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0248
GTP
wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0251
GTP
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0358
GTP
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.044
GTP
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0152
IMP
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0168
IMP
wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0198
IMP
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0248
IMP
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0276
IMP
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.0292
IMP
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.49
L-Asp
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
1.4
L-Asp
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
1.73
L-Asp
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
1.9
L-Asp
wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25°C
1.9
L-Asp
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
3.3
L-Asp
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
additional information
additional information
-
effect of metal ions on Km-values
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.62
IMP
mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.7
IMP
mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
0.84
IMP
mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
1
IMP
mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C
1.1
IMP
wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25°C
1.7
IMP
mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0406
6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-monophosphate
-
pH 7.0, 25°C
0.0094
adenylosuccinate
pH 6.0, 70°C, competitive inhibition of IMP
0.0426
adenylosuccinate
pH 6.0, 70°C, noncompetitive inhibition of aspartate
0.0429
adenylosuccinate
pH 6.0, 70°C, noncompetitive inhibition of GTP
0.324
AMP
pH 6.0, 70°C, noncompetitive inhibition of aspartate
0.402
AMP
pH 6.0, 70°C, noncompetitive inhibition of GTP
1.5
D-fructose 1,6 bisphosphate
pH 6.0, 70°C, competitive inhibition of IMP
4.8
D-fructose 1,6 bisphosphate
pH 6.0, 70°C, competitive inhibition of GTP
0.016
D-fructose 1,6-bisphosphate
-
pH 6.7, 22°C, AdSS1, noncompetitive inhibition relative to IMP
0.019
D-fructose 1,6-bisphosphate
-
pH 6.7, 22°C, AdSS2, noncompetitive inhibition relative to IMP
0.063
D-fructose 1,6-bisphosphate
-
pH 6.7, 22°C, AdSS1, noncompetitive inhibition relative to GTP
0.081
D-fructose 1,6-bisphosphate
-
pH 6.7, 22°C, AdSS1, noncompetitive inhibition relative to L-aspartate
0.4
D-fructose 1,6-bisphosphate
-
pH 6.7, 22°C, AdSS2, noncompetitive inhibition relative to GTP
0.67
D-fructose 1,6-bisphosphate
-
pH 6.7, 22°C, AdSS2, noncompetitive inhibition relative to L-aspartate
0.0821
GDP
pH 6.0, 70°C, noncompetitive inhibition of aspartate
0.0822
GDP
pH 6.0, 70°C, noncompetitive inhibition of IMP
0.0137
GMP
pH 6.0, 70°C, noncompetitive inhibition of GTP
0.12
GMP
pH 6.0, 70°C, noncompetitive inhibition of asparate
0.0105
N-formyl-N-hydroxyglycine
pH 6.0, 70°C, competitive inhibition of asparate
0.0264
N-formyl-N-hydroxyglycine
pH 6.0, 70°C, uncompetitive inhibition of IMP
0.0269
N-formyl-N-hydroxyglycine
pH 6.0, 70°C, uncompetitive inhibition of GTP
1.9
phosphate
pH 6.0, 70°C, competitive inhibition of IMP
8.3
phosphate
pH 6.0, 70°C, competitive inhibition of GTP
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
560
-
crude cell extract, presence of 1 M KCl, pH 7.5, temperature not specified in the publication
720
-
crude cell extract, presence of 1 M KCl, pH 7.5, temperature not specified in the publication
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.4
7.7
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
adenylosuccinate synthetase expression is downregulated in SM-5 cells
brenda
-
adenylosuccinate synthetase expression is downregulated in SM-7 cells
brenda
-
adenylosuccinate synthetase expression is downregulated in thymic lymphoma cells
brenda
additional information
ADSS1 is predominantly expressed in the striated muscle tissue, ADSS1 is up-regulated significantly along with muscle growth
brenda
additional information
-
tissue distribution of L-isozyme and M-isozyme
brenda
additional information
ADSS1 is undetectable in lung, liver, spleen, stomach, fat, lymph, kidney, and intestine
brenda
additional information
ADSS1 is undetectable in lung, liver, spleen, stomach, fat, lymph, kidney, and intestine
brenda
additional information
expression of ADSS2 gene is relatively constant in the prenatal period and remains constant at a relatively higher expression level in postnatal period
brenda
additional information
expression of ADSS2 gene is relatively constant in the prenatal period and remains constant at a relatively higher expression level in postnatal period
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
ADSS1 inactivation as a somatic alteration causing lung carcinogenesis
metabolism
physiological function
metabolism
-
comparison of growth characteristics including intracellular protein levels, RNA content, and nucleotide pool sizes between the extreme halophile Halobacterium halobium and the moderate halophile Haloferax volcanii. The differences in the metabolism of purine bases and nucleosides and the sensitivity to purine analogs between the two halobacteria are reflected in differences in purine enzyme levels
metabolism
-
comparison of growth characteristics including intracellular protein levels, RNA content, and nucleotide pool sizes between the extreme halophile Halobacterium halobium and the moderate halophile Haloferax volcanii. The differences in the metabolism of purine bases and nucleosides and the sensitivity to purine analogs between the two halobacteria are reflected in differences in purine enzyme levels
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
physiological function
ADE12 is required for cell wall integrity and oxidative stress resistance. ADE12 deletion mutants are adenine auxotrophs, fail to produce conidia, and show reduced perithecia formation and pathogenicity. The mutant strain is hypersensitive to Congo red and oxidants
physiological function
Pyricularia oryzae ATCC MYA-4617
-
ADE12 is required for cell wall integrity and oxidative stress resistance. ADE12 deletion mutants are adenine auxotrophs, fail to produce conidia, and show reduced perithecia formation and pathogenicity. The mutant strain is hypersensitive to Congo red and oxidants
-
Show AA Sequence and Transmembrane Helices (27567 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus anthracis str. \'Ames Ancestor
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
102000
-
Yoshida sarcoma ascites tumor cells, sedimentation equilibrium analysis
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
37855
38000
-
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
47000
48000
50000
55000
79000
-
2 * 79000, gel filtration, AdSS exhibits dimer-tetramer equilibrium with the equilibrium shifting towards the dimer in the presence of 100 mM NaCl
80000
1 * 80000, the enzyme mainly exists as dimer in solution, SDS-PAGE
92000
gel filtration, wild-type and mutants N429V, K62L, T307V, R155V, R155K, R155A
37855
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
37855
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
47000
-
2 * 47000, sedimentation equilibrium analysis in presence of 6 M guanidine-HCl
48000
gel filtration, mutant R155A/G146R, plus small peak of dimeric enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
tetramer
additional information
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 * 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
-
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
1 * 80000, the enzyme mainly exists as dimer in solution, SDS-PAGE
dimer
-
1 * 80000, the enzyme mainly exists as dimer in solution, SDS-PAGE
-
dimer
-
2 * 47000, sedimentation equilibrium analysis in presence of 6 M guanidine-HCl
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
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
tetramer
-
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
-
additional information
in contrast to the Escherichia coli enzyme, monomer and dimer may not be in a dynamic equilibrium and binding of ligands may not push the equilibrium towards the dimer
additional information
-
in contrast to the Escherichia coli enzyme, monomer and dimer may not be in a dynamic equilibrium and binding of ligands may not push the equilibrium towards the dimer
-
additional information
conserved arginine residue R155 is involved in dimer crosstalk and interacts with IMP in the active site of the symmetry related subunit
additional information
-
conserved arginine residue R155 is involved in dimer crosstalk and interacts with IMP in the active site of the symmetry related subunit
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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+
entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli
-
analysis of high-resolution vibrational spectral fingerprints of each substrate and intermediate. The bound IMP is distorted toward its N1-deprotonated form even in the absence of any other ligands. Specific interactions between GTP and active-site amino acid residues result in large Raman shifts and contribute substantially to intrinsic binding energy. When both IMP and GTP are simultaneously bound, IMP is converted into an intermediate 6-phosphoryl inosine 5'-monophosphate. The intermediate complex is stable upon binding of the third ligand, L-aspartae analogue hadaicin. In the absence of hadaicin, 6-phosphoryl inosine 5'-monophosphate is quickly released from ADSS, is unstable in solution, and converts back into IMP. Hadaicin allosterically stabilizes ADSS through local conformational rearrangements
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
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
crystal structure of the enzyme complexed with GDP, IMP hadacidin, NO3-, and Mg2+
-
crystal structure of the enzyme complexed with GDP, IMP hadacidin, NO3-, and Mg2+
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P242N
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
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
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
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
N38A
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
R143L
R147L
-
mutant R147L shows increased Km for IMP and GTP relative to the wild-type enzyme, Km for Asp exhibits a modest decrease
R303L
R304L
R305L
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
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/G146R
unlike dimeric wild-type, mainly monomeric. Inactive
T307V
increase in Km values for IMP, GTP and aspartate, respectively
additional information
-
the activity of AMPsS in crude dialyzed cell extracts is 2times lower in the guaBDELTACBS mutant compared with the wild type strain
P242N
about 50% of wild-type activity. Mutant partially reduces the flux towards AMP derived from IMP and increases the riboflavin synthesis precursor GTP
P242N
-
about 50% of wild-type activity. Mutant partially reduces the flux towards AMP derived from IMP and increases the riboflavin synthesis precursor GTP
-
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
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
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
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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 90
-
thermal unfolding of AdSS exhibits a melting temperature of 85°C 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 90°C, respectively
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
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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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable without any decrease in activity for at least 6 months
4°C, glycerol and EDTA stabilizes enzyme activity during storage, stable for at least 3 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, anion exchange chromatography, and gel filtration
partial
purification by cation exchange, size exclusion, and anion exchange chromatography
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Adss1 gene, transient transfection into Rattus norvegicus primary cardiomyocytes, cotransfection into CV1 fibroblasts
-
cDNA expressed in Escherichia coli
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
-
expressed in Escherichia coli BL21 (DE3)
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
gene Adss1, quantitative RT-PCR analysis
hyperexpressed in Escherichia coli BL21 (DE3), complementation of purA mutant strain H1238
-
purA gene
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
synthesis
analysis
cellular uptake by Helicobacter pylori of formycins and hadacidin inhibitors is very poor. A cell penetration assessment method is developed for validating the cellular uptake of other drug candidates
analysis
-
cellular uptake by Helicobacter pylori of formycins and hadacidin inhibitors is very poor. A cell penetration assessment method is developed for validating the cellular uptake of other drug candidates
-
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
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
synthesis
expression of mutant P242N in an inosine-producing strain results in an approximately 4.66fold increase in inosine production, to 0.41 g/L, in minimal medium without hypoxanthine accumulation
synthesis
-
expression of mutant P242N in an inosine-producing strain results in an approximately 4.66fold increase in inosine production, to 0.41 g/L, in minimal medium without hypoxanthine accumulation
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Serra, M.A.; Bass, M.B.; Fromm, H.J.; Honzatko, R.B.
Preliminary X-ray crystallographic study of adenylosuccinate synthetase from Escherichia coli
J. Mol. Biol.
200
753-754
1988
Escherichia coli
brenda
Bass, M.B.; Fromm, H.J.; Stayton, M.M.
Overproduction, purification, and characterization of adenylosuccinate synthetase from Escherichia coli
Arch. Biochem. Biophys.
256
335-342
1987
Escherichia coli
brenda
Cooper, B.F.; Fromm, H.J.; Rudolph, F.B.
Isotope exchange at equilibrium studies with rat muscle adenylosauccinate synthetase
Biochemistry
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1986
Rattus norvegicus
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Jahngen, E.G.E.; Rossomando, E.F.
Adenylosuccinate synthetase from Dictyostelium discoideum: effects of hadacidin analogs and binding of [14C]hadacidin
Arch. Biochem. Biophys.
229
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1984
Dictyostelium discoideum
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Stayton, M.M.; Rudolph, F.B.; Fromm, H.J.
Regulation, genetics, and properties of adenylosuccinate synthetase
Curr. Top. Cell. Regul.
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1983
Escherichia coli, Rattus norvegicus, Oryctolagus cuniculus, Leishmania donovani, Azotobacter vinelandii, Trypanosoma cruzi, Bacillus subtilis, Schizosaccharomyces pombe, Homo sapiens, Sus scrofa, Gallus gallus, Triticum aestivum
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Porter, D.J.T.; Rudie, N.G.; Bright, H.J.
Nitro analogs of substrates for adenylosuccinate synthetase and adenylosuccinate lyase
Arch. Biochem. Biophys.
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1983
Azotobacter vinelandii
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Matsuda, Y.; Shimura, K.; Shiraki, H.; Nakagawa, H.
Purification and properties of adenylosuccinate synthetase from Yoshida sarcoma ascites tumor cells
Biochim. Biophys. Acta
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1980
Rattus norvegicus
brenda
Harada, S.; Matsuura, Y.; Tanaka, N.; Kakudo, M.; Matsuda, Y.; Ogawa, H.; Shiraki, H.; Nakagawa, H.
Preliminary crystallographic data for adenylosuccinate synthetase from rabbit skeletal muscle
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Oryctolagus cuniculus
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Specificity of adenylosuccinate synthetase and adenylosuccinate lyase from Leishmania donovani. Selective amination of an antiprotozoal agent
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Leishmania donovani
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Guanosine 5'-diphosphate-3'-diphosphate inhibition of adenylosuccinate synthetase
J. Biol. Chem.
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Escherichia coli, Escherichia coli B / ATCC 11303
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Fischer, H.E.; Muirhead, K.M.; Bishop, S.H.
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Methods Enzymol.
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Oryctolagus cuniculus
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Adenylosuccinate synthetase from Azotobacter vinelandii: purification, properties and steady-state kinetics
Arch. Biochem. Biophys.
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Azotobacter vinelandii
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Matsuda, Y.; Ogawa, H.; Fukutome, S.; Shiraki, H.; Nakagawa, H.
Adenylosuccinate synthetase in rat liver: the existence of two types and their regulatory roles
Biochem. Biophys. Res. Commun.
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1977
Rattus norvegicus
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Biochim. Biophys. Acta
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1976
Oryctolagus cuniculus
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Human adenylosuccinate synthetase. Partial purification, kinetic and regulatory properties of the enzyme from placenta
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Homo sapiens
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Purification of adenylosuccinate synthetase from rabbit skeletal muscle
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1974
Oryctolagus cuniculus
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Nagy, M.; Djembo-Taty, M.; Heslot, H.
Regulation of the biosynthesis of purine nucleotides in Schizosaccharomyces pombe. II. Kinetic studies of adenylosuccinate synthetase
Biochim. Biophys. Acta
309
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Schizosaccharomyces pombe
brenda
Fonne-Pfister, R.; Chemla, P.; Ward, E.; Girardet, M.; Kreuz, K.E.; Honzatko, R.B.; Fromm, H.J.; Schr, H.P.; Grutter, M.G.; Cowan-Jacob, S.W.
The mode of action and the structure of a herbicide in the complex with its target: binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase
Proc. Natl. Acad. Sci. USA
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1996
Ocimum basilicum
brenda
Wiesmuller, L.; Wittbrodt, J.; Noegel, A.A.; Schleicher, M.
Purification and cDNA-derived sequence of adenylosuccinate synthetase from Dictyostelium discoideum
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Dictyostelium discoideum
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Silva, M.M.; Poland, B.W.; Hoffman, C.R.; Fromm, H.J.; Honzatko, R.B.
Refined crystal structure of unligated adenylosuccinate synthetase from Escherichia coli
J. Mol. Biol.
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1995
Escherichia coli
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Poland, B.W.; Fromm, H.J.; Honzatko, R.B.
Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with GDP, IMP hadacidin, NO3-, and Mg2+
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Escherichia coli
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Moe, O.A.; Baker-Malcolm, J.F.; Wang, W.; Kang, C.; Fromm, H.J.; Colman, R.F.
Involvement of arginine 143 in nucleotide substrate binding at the active site of adenylosuccinate synthetase from Escherichia coli
Biochemistry
35
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1996
Escherichia coli
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Kang, C.; Fromm, H.J.
Characterization of the putative GTP-binding site residues of Escherichia coli adenylosuccinate synthetase by site-directed mutagenesis
Arch. Biochem. Biophys.
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1994
Escherichia coli
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Poland, B.W.; Lee, S.F.; Subramanian, M.V.; Siehl, D.L.; Anderson, R.J.; Fromm, H.J.; Honzatko, R.B.
Refined crystal structure of adenylsuccinate synthetase from Escherichia coli complexed with hydantocidin 5'-phosphate, GDP, HPO42-, Mg2+, and hadacidin
Biochemistry
35
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1996
Escherichia coli (P0A7D4), Escherichia coli
brenda
Poland, B.W.; Bruns, C.; Fromm, H.J.; Honzatko, R.B.
Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli
J. Biol. Chem.
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Escherichia coli
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Residues essential for catalysis and stability of the active site of Escherichia coli adenylosuccinate synthetase as revealed by directed mutation and kinetics
J. Biol. Chem.
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Escherichia coli
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Evidence for an arginine residue as the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis
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Escherichia coli
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Kang, C.; Sun, N.; Honzatko, R.B.; Fromm, H.J.
Replacement of Asp333 with Asn by site-directed mutagenesis changes the substrate specificity of Escherichia coli adenylosuccinate synthetase from guanosine 5'-triphosphate to xanthosine 5'-triphosphate
J. Biol. Chem.
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Escherichia coli
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Escherichia coli
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Identification of arginine residues in the putative L-aspartate binding site of Escherichia coli adenylosuccinate synthetase
J. Biol. Chem.
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Escherichia coli
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Poland, B.W.; Hou, Z.; Bruns, C.; Fromm, H.J.; Honzatko, R.B.
Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli
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Escherichia coli
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Kang, C.; Fromm, H.J.
Identification of a essential second metal ion in the reaction mechanism of Escherichia coli adenylosuccinate synthetase
J. Biol. Chem.
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1995
Escherichia coli
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Wang, W.; Gorrell, A.; Honzatko, R.B.; Fromm, H.J.
A study of Escherichia coli adenylosuccinate synthetase association states and the interface residues of the homodimer
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Escherichia coli
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Wang, W.; Hou, Z.; Honzatko, R.B.; Fromm, H.J.
Relationship of the conserved residues in the IMP binding site to substrate recognition and catalysis in Escherichia coli adenylosuccinate synthetase
J. Biol. Chem.
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Escherichia coli
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Liu, F.; Dong, Q.; Fromm, H.J.
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J. Biol. Chem.
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Escherichia coli
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Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase
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Homo sapiens
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Gallert, K.C.; Ohanjan, T.; Daignan-Fornier, B.; Lottspeich, F.; Krauss, G.
Enzymatic properties and inhibition by single-stranded autonomously replicating sequences of adenylosuccinate synthase from Saccharomyces cerevisiae
Eur. J. Biochem.
239
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1996
Saccharomyces cerevisiae
brenda
Siehl, D.L.; Subramanian, M.V.; Walters, E.W.; Lee, S.F.; Anderson, R.J.; Toschi, A.G.
Adenylosuccinate synthetase: site of action of hydantocidin, a microbial phytotoxin
Plant Physiol.
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1996
Arabidopsis thaliana, Zea mays
brenda
Walters, E.W.; Lee, S.F.; Niderman, T.; Bernasconi, P.; Subramanian, M.V.; Siehl, D.L.
Adenylosuccinate synthetase from maize. Purification, properties, and mechanism of inhibition by 5'-phosphohydantocidin
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Zea mays
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Honzatko, R.B.; Stayton, M.M.; Fromm, H.J.
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Adv. Enzymol. Relat. Areas Mol. Biol.
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Escherichia coli, Rattus norvegicus, Azotobacter vinelandii, Oryctolagus cuniculus, Leishmania donovani, Trypanosoma cruzi, Homo sapiens, Bacillus subtilis, Haemophilus influenzae, Acidithiobacillus ferrooxidans, Methanocaldococcus jannaschii, Pyrococcus sp., Dictyostelium discoideum, Zea mays, Triticum aestivum, Mus musculus, Schizosaccharomyces pombe, Arabidopsis thaliana, Pyrococcus sp. ST700
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Honzatko, R.B.; Stayton, M.M.; Fromm, H.J.
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Adv. Enzymol. Relat. Areas Mol. Biol.
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Saccharomyces cerevisiae
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Honzatko, R.B.; Fromm, H.J.
Structure-function studies of adenylosuccinate synthetase from Escherichia coli
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Escherichia coli
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Lipps, G.; Krauss, G.
Adenylosuccinate synthase from Saccharomyces cerevisiae: homologous overexpression, purification and characterization of the recombinant protein
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Saccharomyces cerevisiae
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Lee, P.; Gorrell, A.; Fromm, H.J.; Colman, R.F.
Implication of arginine-131 and arginine-303 in the substrate site of adenylosuccinate synthetase of Escherichia coli by affinity labeling with 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-monophosphate
Biochemistry
38
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1999
Escherichia coli
brenda
Ryzhova, T.A.; Andreichuk, Y.V.; Domkin, V.D.
Adenylosuccinate synthetase of the yeast Saccharomyces cerevisiae: purification and properties
Biochemistry
63
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1998
Saccharomyces cerevisiae
brenda
Wang, W.; Gorrell, A.; Hou, Z.; Honzatko, R.B.; Fromm, H.J.
Ambiguities in mapping the active site of a conformationally dynamic enzyme by directed mutation. Role of dynamics in structure-function correlations in Escherichia coli adenylosuccinate synthetase
J. Biol. Chem.
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1998
Escherichia coli
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Lewis, A.L.; Xia, Y.; Datta, S.K.; McMillin, J.; Kellems, R.E.
Combinatorial interactions regulate cardiac expression of the murine adenylosuccinate synthetase 1 gene
J. Biol. Chem.
274
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1999
Mus musculus
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Hou, Z.; Cashel, M.; Fromm, H.J.; Honzatko, R.B.
Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase
J. Biol. Chem.
274
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1999
Escherichia coli (P0A7D4), Escherichia coli
brenda
Iancu, C.V.; Borza, T.; Choe, J.Y.; Fromm, H.J.; Honzatko, R.B.
Recombinant mouse muscle adenylosuccinate synthetase: overexpression, kinetics, and crystal structure
J. Biol. Chem.
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2001
Mus musculus
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Iancu, C.V.; Borza, T.; Fromm, H.J.; Honzatko, R.B.
Feedback inhibition and product complexes of recombinant mouse muscle adenylosuccinate synthetase
J. Biol. Chem.
277
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2002
Mus musculus (P28650), Mus musculus
brenda
Hou, Z.; Wang, W.; Fromm, H.J.; Honzatko, R.B.
IMP alone organizes the active site of adenylosuccinate synthetase from Escherichia coli
J. Biol. Chem.
277
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2002
Escherichia coli (P0A7D4), Escherichia coli
brenda
Gorrell, A.; Wang, W.; Underbakke, E.; Hou, Z.; Honzatko, R.B.; Fromm, H.J.
Determinants of L-L-aspartate and IMP recognition in Escherichia coli adenylosuccinate synthetase
J. Biol. Chem.
277
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2002
Escherichia coli (P0A7D4), Escherichia coli
brenda
Borza, T.; Iancu, C.V.; Pike, E.; Honzatko, R.B.; Fromm, H.J.
Variations in the response of mouse isozymes of adenylosuccinate synthetase to inhibitors of physiological relevance
J. Biol. Chem.
278
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2003
Mus musculus
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Wen, H.Y.; Xia, Y.; Young, M.E.; Taegtmeyer, H.; Kellems, R.E.
The adenylosuccinate synthetase-1 gene is activated in the hypertrophied heart
J. Cell. Mol. Med.
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2002
Rattus norvegicus, Mus musculus
brenda
Prade, L.; Cowan-Jacob, S.W.; Chemla, P.; Potter, S.; Ward, E.; Fonne-Pfister, R.
Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana
J. Mol. Biol.
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Arabidopsis thaliana (Q96529), Arabidopsis thaliana, Triticum aestivum (O24396), Triticum aestivum
brenda
Eaazhisai, K.; Jayalakshmi, R.; Gayathri, P.; Anand, R.P.; Sumathy, K.; Balaram, H.; Murthy, M.R.
Crystal structure of fully ligated adenylosuccinate synthetase from Plasmodium falciparum
J. Mol. Biol.
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2004
Plasmodium falciparum (Q9U8D3), Plasmodium falciparum
brenda
Schmitzer, P.R.; Graupner, P.R.; Chapin, E.L.; Fields, S.C.; Gilbert, J.R.; Gray, J.A.; Peacock, C.L.; Gerwick, B.C.
Ribofuranosyl triazolone: A natural product herbicide with activity on adenylosuccinate synthetase following phosphorylation
J. Nat. Prod.
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2000
Arabidopsis thaliana, Helianthus annuus, Ipomoea hederacea, Echinochloa crus-galli, Avena fatua, Abutilon theophrasti, Amaranthus retroflexus, Setaria faberi, Alopecurus myosuroides
brenda
Jayalakshmi, R.; Sumathy, K.; Balaram, H.
Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli
Protein Expr. Purif.
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2002
Plasmodium falciparum
brenda
Raman, J.; Mehrotra, S.; Anand, R.P.; Balaram, H.
Unique kinetic mechanism of Plasmodium falciparum adenylosuccinate synthetase
Mol. Biochem. Parasitol.
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Plasmodium falciparum
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Sun, H.; Li, N.; Wang, X.; Chen, T.; Shi, L.; Zhang, L.; Wang, J.; Wan, T.; Cao, X.
Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells
Mol. Cell. Biochem.
269
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2005
Homo sapiens (Q8N142), Homo sapiens
brenda
Iancu, C.V.; Zhou, Y.; Borza, T.; Fromm, H.J.; Honzatko, R.B.
Cavitation as a mechanism of substrate discrimination by adenylosuccinate synthetases
Biochemistry
45
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2006
Mus musculus (P28650), Escherichia coli (P0A7D4)
brenda
Li, X.; Zhu, Z.; Mo, D.; Wang, H.; Yang, S.; Zhao, S.; Li, K.
Comparative molecular characterization of ADSS1 and ADSS2 genes in pig (Sus scrofa)
Comp. Biochem. Physiol. B
147B
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2007
Sus scrofa (A4Z6H0), Sus scrofa (A4Z6H1)
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Pimkin, M.; Markham, G.D.
The CBS subdomain of inosine 5-monophosphate dehydrogenase regulates purine nucleotide turnover
Mol. Microbiol.
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Escherichia coli
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Zhang, F.; Sham, P.C.; Fan, H.; Xu, Y.; Huang, X.; So, H.; Song, Y.; Liu, P.
An association study of ADSS gene polymorphisms with schizophrenia
Behav. Brain Funct.
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2008
Homo sapiens
brenda
Mehrotra, S.; Balaram, H.
Methanocaldococcus jannaschii adenylosuccinate synthetase: Studies on temperature dependence of catalytic activity and structural stability
Biochim. Biophys. Acta
1784
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2008
Methanocaldococcus jannaschii
brenda
Oestreicher, N.; Ribard, C.; Scazzocchio, C.
The nadA gene of Aspergillus nidulans, encoding adenine deaminase, is subject to a unique regulatory pattern
Fungal Genet. Biol.
45
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2008
Aspergillus nidulans, Aspergillus nidulans pabaA1
brenda
Honore, B.; Buus, S.; Claesson, M.H.
Identification of differentially expressed proteins in spontaneous thymic lymphomas from knockout mice with deletion of p53
Proteome Sci.
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Mus musculus
brenda
Miller, J.C.; Blake, D.C.; Herzog, C.R.
Adenylosuccinate synthetase 1 gene is a novel target of deletion in lung adenocarcinoma
Mol. Carcinog.
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2009
Mus musculus
brenda
Mehrotra, S.; Mylarappa, B.N.; Iyengar, P.; Balaram, H.
Studies on active site mutants of P. falciparum adenylosuccinate synthetase: insights into enzyme catalysis and activation
Biochim. Biophys. Acta
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Plasmodium falciparum (Q9U8D3), Plasmodium falciparum
brenda
Hitomi, Y.; Cirulli, E.T.; Fellay, J.; McHutchison, J.G.; Thompson, A.J.; Gumbs, C.E.; Shianna, K.V.; Urban, T.J.; Goldstein, D.B.
Inosine triphosphate protects against ribavirin-induced adenosine triphosphate loss by adenylosuccinate synthase function
Gastroenterology
140
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2011
Homo sapiens
brenda
Wang, X.; Akasaka, R.; Takemoto, C.; Morita, S.; Yamaguchi, M.; Terada, T.; Shirozu, M.; Yokoyama, S.; Chen, S.; Si, S.; Xie, Y.
Overexpression, purification, crystallization and preliminary crystallographic studies of a hyperthermophilic adenylosuccinate synthetase from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. F
67
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2011
Pyrococcus horikoshii (O58187), Pyrococcus horikoshii OT-3 (O58187)
brenda
Bouyoub, A.; Barbier, G.; Forterre, P.; Labedan, B.
The adenylosuccinate synthetase from the hyperthermophilic archaeon Pyrococcus species displays unusual structural features
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Pyrococcus sp. (Q59726), Pyrococcus sp. ST700 (Q59726)
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Blundell, R.D.; Williams, S.J.; Morrow, C.A.; Ericsson, D.J.; Kobe, B.; Fraser, J.A.
Purification, crystallization and preliminary X-ray analysis of adenylosuccinate synthetase from the fungal pathogen Cryptococcus neoformans
Acta Crystallogr. Sect. F
69
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2013
Cryptococcus neoformans
brenda
Mehrotra, S.; Balaram, H.
Kinetic characterization of adenylosuccinate synthetase from the thermophilic archaea Methanocaldococcus jannaschii
Biochemistry
46
12821-12832
2007
Methanocaldococcus jannaschii (Q57981), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57981)
brenda
Vemparala, S.; Mehrotra, S.; Balaram, H.
Role of loop dynamics in thermal stability of mesophilic and thermophilic adenylosuccinate synthetase: a molecular dynamics and normal mode analysis study
Biochim. Biophys. Acta
1814
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2011
Pyrococcus horikoshii (O58187), Pyrococcus horikoshii, Escherichia coli (P0A7D4), Escherichia coli
brenda
Mehrotra, S.; B Ningappa, M.; Raman, J.; Anand, R.P.; Balaram, H.
Mutational analysis of cysteine 328 and cysteine 368 at the interface of Plasmodium falciparum adenylosuccinate synthetase
Biochim. Biophys. Acta
1824
589-597
2012
Plasmodium falciparum (Q9U8D3), Plasmodium falciparum
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Stuer-Lauridsen, B.; Nygaard, P.
Purine salvage in two halophilic archaea: characterization of salvage pathways and isolation of mutants resistant to purine analogs
J. Bacteriol.
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Halobacterium salinarum, Haloferax volcanii
brenda
Karnawat, V.; Mehrotra, S.; Balaram, H.; Puranik, M.
Exquisite modulation of the active site of Methanocaldococcus jannaschii adenylosuccinate synthetase in forward reaction complexes
Biochemistry
55
2491-2499
2016
Methanocaldococcus jannaschii (Q57981), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57981)
brenda
Nomura, Y.; Nozawa, A.; Tozawa, Y.
Biochemical analyses of ppGpp effect on adenylosuccinate synthetases, key enzymes in purine biosynthesis in rice
Biosci. Biotechnol. Biochem.
78
1022-1025
2014
Oryza sativa, Escherichia coli, Bacillus subtilis, Bacillus subtilis 168
brenda
Wang, X.; Wang, G.; Li, X.; Fu, J.; Chen, T.; Wang, Z.; Zhao, X.
Directed evolution of adenylosuccinate synthetase from Bacillus subtilis and its application in metabolic engineering
J. Biotechnol.
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2016
Bacillus subtilis (P29726), Bacillus subtilis, Bacillus subtilis 168 (P29726)
brenda
Wojtys, M.I.; Jazwiec, R.; Kazazic, S.; Lescic Asler, I.; Knezevic, P.; Aleksic Sabo, V.; Luic, M.; Jagusztyn-Krynicka, E.K.; Bzowska, A.
A comprehensive method for determining cellular uptake of purine nucleoside phosphorylase and adenylosuccinate synthetase inhibitors by H. pylori
Appl. Microbiol. Biotechnol.
105
7949-7967
2021
Helicobacter pylori (P56137), Helicobacter pylori 26695 (P56137)
brenda
Tibrewal, N.; Elliott, G.I.
Design, synthesis and evaluation of AdSS bisubstrate inhibitors
ChemMedChem
15
2269-2272
2020
Homo sapiens
brenda
Bubic, A.; Mrnjavac, N.; Stuparevic, I.; Lyczek, M.; Wielgus-Kutrowska, B.; Bzowska, A.; Luic, M.; Lescic Asler, I.
In the quest for new targets for pathogen eradication the adenylosuccinate synthetase from the bacterium Helicobacter pylori
J. Enzyme Inhib. Med. Chem.
33
1405-1414
2018
Helicobacter pylori (P56137), Helicobacter pylori ATCC 700392 (P56137)
brenda
Zhang, Z.; Hao, Z.; Chai, R.; Qiu, H.; Wang, Y.; Wang, J.; Sun, G.
Adenylsuccinate synthetase MoADE12 plays important roles in the development and pathogenicity of the rice blast fungus
J. Fungi (Basel)
8
780
2022
Pyricularia oryzae (A4QXV8), Pyricularia oryzae ATCC MYA-4617 (A4QXV8)
brenda
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