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Information on EC 6.3.4.4 - adenylosuccinate synthase and Organism(s) Escherichia coli and UniProt Accession P0A7D4

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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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This record set is specific for:
Escherichia coli
UNIPROT: P0A7D4 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Adenylosuccinate synthetase
-
adenosylsuccinate synthetase
-
-
Adenylosuccinate synthase
-
-
-
-
Adenylosuccinate synthetase
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
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
IMP:L-aspartate ligase (GDP-forming)
-
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
ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
show the reaction diagram
-
-
-
?
GTP + IMP + hydroxylamine
GDP + phosphate + ?
show the reaction diagram
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
show the reaction diagram
-
-
-
-
?
GTP + IMP + L-Asp
?
show the reaction diagram
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
-
-
-
-
?
ITP + IMP + L-Asp
IDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
UTP + IMP + L-Asp
UDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
XTP + IMP + L-Asp
XDP + 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-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
GTP + IMP + L-Asp
?
show the reaction diagram
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
absolute requirement for divalent metal ions
Co2+
-
absolute requirement for divalent metal ions
Cu2+
-
absolute requirement for divalent metal ions
additional information
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
guanosine 5'-diphosphate
-
Hadacidin
6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-monophosphate
-
-
6-mercaptopurine riboside 5'-phosphate
-
-
adenylosuccinate
-
-
beta,gamma-5'-Guanylylmethylene diphosphate
-
-
Guanosine 5'-diphosphate-3'-diphosphate
-
competitive with respect to GTP and noncompetitive with respect to L-Asp and IMP
Guanosine 5'-O-[S-(4-bromo-2,3-dioxobutyl)thio]phosphate
-
-
Phenylglyoxal
-
GTP or IMP partially protect
succinate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041
2'-dIMP
22°C
0.021 - 1.7
GTP
91 - 255
hydroxylamine
0.017 - 0.89
IMP
0.013 - 0.23
L-Asp
0.17 - 9
L-aspartate
0.34
allopurinol ribonucleotide
-
Asp, mutant R143L
0.03 - 5.4
Asp
0.17 - 2.6
aspartate
0.01 - 0.6
GTP
0.02 - 3.8
IMP
1.07 - 17.3
ITP
0.98
L-Asp
-
-
0.01
L-aspartate
-
-
1.27 - 4.38
UTP
0.0286 - 0.388
XTP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.96
2'-dIMP
22°C
0.05 - 6.08
GTP
0.08 - 0.5
hydroxylamine
0.96 - 1
L-Asp
0.0048 - 6.08
GTP
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21
GTP
-
pH 7.7, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 0.64
fumarate
0.00049 - 0.017
Hadacidin
0.078 - 3.1
Maleate
0.08 - 0.89
succinate
0.0406
6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-monophosphate
-
pH 7.0, 25°C
0.012
GDP
-
pH 7.7, 30°C
0.01
Hadacidin
-
-
0.05
ppGpp
-
pH 7.7, 30°C
1
succinate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00207
-
enzyme from guaBDELTACBS mutant crude extract
0.00493
-
enzyme from wild type crude extract
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
-
mutant Q224E
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 8
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
141000
-
HPLC gel filtration
46600
-
2 * 46600
48000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
-
2 * 46600
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme complexed with GDP, IMP hadacidin, NO3-, and Mg2+
crystals grown by the method of hanging drops
hanging drop method, GDP-2'-deoxy-6-phosphoryl-IMP-hadacidin complex
crystal structure of guanine nucleotide complexes of adenylosuccinate synthetase
-
crystal structure of the enzyme complexed with GDP, IMP hadacidin, NO3-, and Mg2+
-
crystal structure of unligated enzyme
-
entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T128A
site-directed mutagenesis
T129A
site-directed mutagenesis
T300A
site-directed mutagenesis
T301A
site-directed mutagenesis
V273A
site-directed mutagenesis
V273N
site-directed mutagenesis
V273T
site-directed mutagenesis
D13A
-
mutant enzyme D13A shows no measurable activity, mutant enzymes E14A and H41N exhibit 1% of the activity of the wild-type enzyme and 2-7fold increases in Km of substrates. The mutant enzyme K16Q has 34% of the activity of wild-type enzyme and Km values for substrates are virtually unchanged from those of the wild-type enzyme
D21A
-
directed mutagenesis
D231A
-
wild-type and mutant enzymes, R132K, R143L, and D231A exist as a mixture of monomers and dimers, with a majority of the enzyme in the monomeric state. In the presence of active site ligands, the wild-type enzyme exists almost exclusively as a dimer, whereas the mutant enzymes show only slightly decreased dissociation constants for the dimerization
D333E
-
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme
D333N
-
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme
D333Q
-
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme
E14A
-
mutant enzyme D13A shows no measurable activity, mutant enzymes E14A and H41N exhibit 1% of the activity of the wild-type enzyme and 2-7fold increases in Km of substrates. The mutant enzyme K16Q has 34% of the activity of wild-type enzyme and Km values for substrates are virtually unchanged from those of the wild-type enzyme
G12V
-
replacement of Gly12, Gly15, or Gly17 with Val, or replacement of Lys18 with Arg, results in significant decrease in the kcat/Km values of the enzyme
G15V
-
the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP
G17V
-
replacement of Gly12, Gly15, or Gly17 with Val, or replacement of Lys18 with Arg, results in significant decrease in the kcat/Km values of the enzyme
K16Q
-
site-directed mutagenesis
K331l
-
the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP
K331R
-
the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP
L18R
-
replacement of Gly12, Gly15, or Gly17 with Val, or replacement of Lys18 with Arg, results in significant decrease in the kcat/Km values of the enzyme
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
N38D
-
directed mutagenesis
N38E
-
directed mutagenesis
Q224M
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
Q34E
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
R132L
-
wild-type and mutant enzymes, R132K, R143L, and D231A exist as a mixture of monomers and dimers, with a majority of the enzyme in the monomeric state. In the presence of active site ligands, the wild-type enzyme exists almost exclusively as a dimer, whereas the mutant enzymes show only slightly decreased dissociation constants for the dimerization
R143K
-
site-directed mutagenesis
R143L
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
R419L
-
directed mutagenesis
S240A
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
S240E
-
mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme
T42A
-
directed mutagenesis
additional information
-
the activity of AMPsS in crude dialyzed cell extracts is 2times lower in the guaBDELTACBS mutant compared with the wild type strain
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
GTP and IMP stabilize the dimeric structure
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes
mutant enzymes R303L, R304L, and R305L
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the temperature-inducible, high-copy-number plasmid vector, pMOB45. Upon temperature induction, cells containing this plasmid produce adenylosuccinate synthetase at approximately 40times the wild-type level
-
purA gene
-
purA gene overexpressed in strain H1238
-
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
Manually annotated by BRENDA team
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
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
Stayton, M.M.; Fromm, H.J.
Guanosine 5'-diphosphate-3'-diphosphate inhibition of adenylosuccinate synthetase
J. Biol. Chem.
254
2579-2581
1979
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
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.
254
431-446
1995
Escherichia coli
Manually annotated by BRENDA team
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+
J. Mol. Biol.
264
1013-1027
1996
Escherichia coli
Manually annotated by BRENDA team
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
9024-9033
1996
Escherichia coli
Manually annotated by BRENDA team
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.
310
475-480
1994
Escherichia coli
Manually annotated by BRENDA team
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
15753-15759
1996
Escherichia coli (P0A7D4), Escherichia coli
Manually annotated by BRENDA team
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.
272
15200-15205
1997
Escherichia coli
Manually annotated by BRENDA team
Kang, C.; Sun, N.; Poland, B.W.; Gorrell, A.; Honzatko, R.B.; Fromm, H.J.
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.
272
11881-11885
1997
Escherichia coli
Manually annotated by BRENDA team
Dong, Q.; Liu, F.; Myers, A.M.; Fromm, H.J.
Evidence for an arginine residue as the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis
J. Biol. Chem.
266
12228-12233
1991
Escherichia coli
Manually annotated by BRENDA team
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.
269
24046-24049
1994
Escherichia coli
Manually annotated by BRENDA team
Kang, C.; Kim, S.; Fromm, H.J.
Subunit complementation of Escherichia coli adenylosuccinate synthetase
J. Biol. Chem.
271
29722-29728
1996
Escherichia coli
Manually annotated by BRENDA team
Wang, W.; Poland, B.W.; Honzatko, R.B.; Fromm, H.J.
Identification of arginine residues in the putative L-aspartate binding site of Escherichia coli adenylosuccinate synthetase
J. Biol. Chem.
270
13160-13168
1995
Escherichia coli
Manually annotated by BRENDA team
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
J. Biol. Chem.
271
15407-15413
1996
Escherichia coli
Manually annotated by BRENDA team
Kang, C.; Fromm, H.J.
Identification of a essential second metal ion in the reaction mechanism of Escherichia coli adenylosuccinate synthetase
J. Biol. Chem.
270
15539-15544
1995
Escherichia coli
Manually annotated by BRENDA team
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
J. Biol. Chem.
272
7078-7084
1997
Escherichia coli
Manually annotated by BRENDA team
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.
272
16911-16916
1997
Escherichia coli
Manually annotated by BRENDA team
Liu, F.; Dong, Q.; Fromm, H.J.
Site-directed mutagenesis of the phosphate-binding consensus sequence in Escherichia coli adenylosuccinate synthetase
J. Biol. Chem.
267
2388-2392
1992
Escherichia coli
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
Honzatko, R.B.; Fromm, H.J.
Structure-function studies of adenylosuccinate synthetase from Escherichia coli
Arch. Biochem. Biophys.
370
1-8
1999
Escherichia coli
Manually annotated by BRENDA team
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
5754-5763
1999
Escherichia coli
Manually annotated by BRENDA team
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.
273
16000-16004
1998
Escherichia coli
Manually annotated by BRENDA team
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
17505-17510
1999
Escherichia coli (P0A7D4), Escherichia coli
Manually annotated by BRENDA team
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
5970-5976
2002
Escherichia coli (P0A7D4), Escherichia coli
Manually annotated by BRENDA team
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
8817-8821
2002
Escherichia coli (P0A7D4), Escherichia coli
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Pimkin, M.; Markham, G.D.
The CBS subdomain of inosine 5-monophosphate dehydrogenase regulates purine nucleotide turnover
Mol. Microbiol.
68
342-359
2008
Escherichia coli
Manually annotated by BRENDA team
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
630-637
2011
Pyrococcus horikoshii (O58187), Pyrococcus horikoshii, Escherichia coli (P0A7D4), Escherichia coli
Manually annotated by BRENDA team
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
Bacillus subtilis, Bacillus subtilis 168, Escherichia coli, Oryza sativa
Manually annotated by BRENDA team