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Information on EC 6.3.4.4 - adenylosuccinate synthase and Organism(s) Mus musculus and UniProt Accession P28650
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6.3.4.4 adenylosuccinate synthaseSpecify your search results
Word Map
- 6.3.4.4
- purine
- gtp
- inosine
- hadacidin
- hypoxanthine
- formycin
- adenylosuccinase
-
alanosine
- medicine
-
saicar
- synthesis
- agriculture
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
adenylosuccinate synthetase, adssl1, adss1, adenylosuccinate synthase, pfadss, adss2, ampss, succino-amp synthetase, adenylosuccinate synthetase 1, mouse muscle synthetase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Adenylosuccinate synthase
-
-
-
-
Adenylosuccinate synthetase
AdSS
-
-
-
-
AdSS1
AMPSase
IMP--aspartate ligase
-
-
-
-
IMP-aspartate ligase
-
-
-
-
Succino-AMP synthetase
-
-
-
-
Succinoadenylic kinosynthetase
-
-
-
-
Adenylosuccinate synthetase
-
-
-
-
AMPSase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
IMP:L-aspartate ligase (GDP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9023-57-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
vertebrates possess two isozymes, the acidic is similar to the synthetase from bacteria and plants, the basic isozyme participates in the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
governs the committed step of AMP biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
acidic and basic isozymes, which participates in the first committed step of de novo AMP biosynthesis and/or the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
catalyzes the first committed step in the de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
function in adenine nucleotide biosynthesis
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
governs the committed step of AMP biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
function in adenine nucleotide biosynthesis
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
acidic and basic isozymes, which participates in the first committed step of de novo AMP biosynthesis and/or the purine nucleotide cycle
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
catalyzes the first committed step in the de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP
-
inhibits the acidic isozyme competitively, weak inhibition of the basic isozyme noncompetitively
IMP
-
competitive inhibition of the acidic isozyme, noncompetitive of the basic isozyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
adenylosuccinate synthetase expression is downregulated in SM-5 cells
-
adenylosuccinate synthetase expression is downregulated in SM-7 cells
-
adenylosuccinate synthetase expression is downregulated in thymic lymphoma cells
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
ADSS1 inactivation as a somatic alteration causing lung carcinogenesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PURA1_MOUSE
457
0
50254
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
crystals grown by the method of hanging drops, space group P4(#)2(1)2, a = b = 69.93, c = 198.49
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Adss1 gene, transient transfection into Rattus norvegicus primary cardiomyocytes, cotransfection into CV1 fibroblasts
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Honzatko, R.B.; Stayton, M.M.; Fromm, H.J.
Adenylosuccinate synthetase: Recent developments
Adv. Enzymol. Relat. Areas Mol. Biol.
73
57-102
1999
Azotobacter vinelandii, Acidithiobacillus ferrooxidans, Arabidopsis thaliana, Bacillus subtilis, Oryctolagus cuniculus, Dictyostelium discoideum, Escherichia coli, Haemophilus influenzae, Homo sapiens, Leishmania donovani, Methanocaldococcus jannaschii, Mus musculus, Pyrococcus sp., Rattus norvegicus, Schizosaccharomyces pombe, Triticum aestivum, Trypanosoma cruzi, Zea mays, Pyrococcus sp. ST700
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
14188-14197
1999
Mus musculus
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.
276
42146-42152
2001
Mus musculus
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
40536-40543
2002
Mus musculus (P28650), Mus musculus
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
6673-6679
2003
Mus musculus
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.
6
235-243
2002
Mus musculus, Rattus norvegicus
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
11703-11711
2006
Escherichia coli (P0A7D4), Mus musculus (P28650)
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.
6
18
2008
Mus musculus
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