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Information on EC 6.3.4.4 - adenylosuccinate synthase and Organism(s) Rattus norvegicus

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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
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Rattus norvegicus
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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, as-synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosylsuccinate synthetase
-
-
Adenylosuccinate synthase
-
-
-
-
Adenylosuccinate synthetase
AdSS
-
-
-
-
AMPSase
IMP--aspartate ligase
-
-
-
-
IMP-aspartate ligase
-
-
-
-
Succino-AMP synthetase
-
-
-
-
Succinoadenylic kinosynthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
random sequential binding mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
IMP:L-aspartate ligase (GDP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-57-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
10.9% of the activation relative to Mg2+
additional information
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenylosuccinate
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-
argininosuccinate
-
-
Ca2+
-
in presence of Mg2+
Carbamoylphosphate
-
-
Cd2+
-
in presence of Mg2+
Cu2+
-
in presence of Mg2+
fructose 1,6-diphosphate
-
basic type M isozym more strongly inhibited than acidic type L isozym
guanosine
-
-
Hadacidin
-
-
Hg2+
-
reversed by addition of DTT
Mn2+
-
in presence of Mg2+
nucleotides
-
acidic type L isozyme more strongly inhibited than basic type M isozyme
-
Pb2+
-
in presence of Mg2+
phosphate
-
-
succinate
-
-
Zn2+
-
in presence of Mg2+
additional information
-
overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25 - 1.47
Asp
0.004 - 0.38
GTP
0.03 - 0.7
IMP
0.98
L-Asp
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
-
50% of maximal activity at pH 5.5 and 8.5
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
-
acidic isoenzyme
8.9
-
basic isoenzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
tissue distribution of L-isozyme and M-isozyme
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8I6A7H6_RAT
431
0
47763
TrEMBL
Mitochondrion (Reliability: 4)
A0A8I6GA01_RAT
362
0
40029
TrEMBL
other Location (Reliability: 3)
A0A8I6AT75_RAT
452
0
49558
TrEMBL
other Location (Reliability: 3)
A0A8I6G9X7_RAT
460
0
50261
TrEMBL
other Location (Reliability: 4)
D4AEP0_RAT
456
0
50085
TrEMBL
other Location (Reliability: 3)
A0A8I6G7N1_RAT
226
0
24461
TrEMBL
other Location (Reliability: 3)
M0R629_RAT
457
0
50250
TrEMBL
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
102000
-
Yoshida sarcoma ascites tumor cells, sedimentation equilibrium analysis
104000
-
sedimentation equilibrium analysis
47000
-
2 * 47000, sedimentation equilibrium analysis in presence of 6 M guanidine-HCl
52000
-
2 * 52000, SDS-PAGE
55000 - 60000
-
liver and Novikoff ascites cells
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
most stable at pH 7.0 in phosphate buffer
1539
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, or 0°C, rapid loss of enzyme activity in dilute solution
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Adss1, quantitative RT-PCR analysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cooper, B.F.; Fromm, H.J.; Rudolph, F.B.
Isotope exchange at equilibrium studies with rat muscle adenylosauccinate synthetase
Biochemistry
25
7323-7327
1986
Rattus norvegicus
Manually annotated by BRENDA team
Stayton, M.M.; Rudolph, F.B.; Fromm, H.J.
Regulation, genetics, and properties of adenylosuccinate synthetase
Curr. Top. Cell. Regul.
22
103-141
1983
Azotobacter vinelandii, Bacillus subtilis, Gallus gallus, Oryctolagus cuniculus, Escherichia coli, Homo sapiens, Leishmania donovani, Rattus norvegicus, Schizosaccharomyces pombe, Sus scrofa, Triticum aestivum, Trypanosoma cruzi
Manually annotated by BRENDA team
Matsuda, Y.; Shimura, K.; Shiraki, H.; Nakagawa, H.
Purification and properties of adenylosuccinate synthetase from Yoshida sarcoma ascites tumor cells
Biochim. Biophys. Acta
616
340-350
1980
Rattus norvegicus
Manually annotated by BRENDA team
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.
78
766-771
1977
Rattus norvegicus
Manually annotated by BRENDA team
Ogawa, H.; Shiraki, H.; Matsuda, Y.; Kakiuchi, K.; Nakagawa, H.
Purification, crystallization, and properties of adenylosuccinate synthetase from rat skeletal muscle
J. Biochem.
81
859-869
1977
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team