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ATP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + 2'-dIMP + L-Asp
GDP + phosphate + 2'-deoxysuccinoAMP
-
-
-
?
GTP + IMP + hydroxylamine
GDP + phosphate + ?
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
-
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
-
-
-
-
?
ITP + IMP + L-Asp
IDP + phosphate + adenylosuccinate
-
-
-
?
UTP + IMP + L-Asp
UDP + phosphate + adenylosuccinate
-
-
-
?
XTP + IMP + L-Asp
XDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
catalyzing the first committed step in de novo biosynthesis of AMP
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
governs the first committed step in de novo biosynthesis of AMP plays a significant role in de novo purine nucleotide biosynthesis, the purine nucleotide cycle, and/or salvage pathway for nucleotides
-
?
GTP + IMP + L-Asp
?
-
plays an important role in the interconversion of purines
-
-
?
GTP + IMP + L-Asp
?
-
first committed step towards the de novo biosynthesis of AMP
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
-
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
-
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
catalyzes the first step in the conversion of IMP to AMP in de novo purine nucleotide metabolism
-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
-
catalyzing the first committed step in the 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 + adenylosuccinate
-
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
-
?
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0.34
allopurinol ribonucleotide
-
Asp, mutant R143L
additional information
additional information
-
0.021
GTP
pH 7.7, 25°C, mutant V273N
0.021
GTP
22°C, cosubstrate: 2'-dIMP
0.026
GTP
pH 7.7, 25°C, wild-type
0.026
GTP
22°C, cosubstrate: IMP
0.031
GTP
pH 7.7, 25°C, mutant V273A
0.045
GTP
pH 7.7, 25°C, mutant V273T
0.054
GTP
pH 7.7, 25°C, mutant T128A
0.056
GTP
pH 7.7, 25°C, mutant T300V
0.057
GTP
pH 7.7, 25°C, mutant T301A, hydroxylamine as substrate
0.074
GTP
pH 7.7, 25°C, mutant V273T, hydroxylamine as substrate
0.14
GTP
pH 7.7, 25°C, mutant V273A, hydroxylamine as substrate
0.17
GTP
pH 7.7, 25°C, mutant T300A
0.18
GTP
pH 7.7, 25°C, mutant V273N, hydroxylamine as substrate
0.19
GTP
pH 7.7, 25°C, wild-type, hydroxylamine as substrate
1.7
GTP
pH 7.7, 25°C, mutant T129A
91
hydroxylamine
pH 7.7, 25°C, mutant T301A
110
hydroxylamine
pH 7.7, 25°C, mutant V273N
140
hydroxylamine
pH 7.7, 25°C, mutant V273T
230
hydroxylamine
pH 7.7, 25°C, wild-type
255
hydroxylamine
pH 7.7, 25°C, mutant V273A
0.017
IMP
pH 7.7, 25°C, mutant V273A
0.019
IMP
pH 7.7, 25°C, mutant T300A
0.024
IMP
pH 7.7, 25°C, mutant V273N
0.028
IMP
pH 7.7, 25°C, wild-type
0.033
IMP
pH 7.7, 25°C, mutant T300V
0.043
IMP
pH 7.7, 25°C, mutant V273T
0.066
IMP
pH 7.7, 25°C, wild-type, hydroxylamine as substrate
0.077
IMP
pH 7.7, 25°C, mutant V273T, hydroxylamine as substrate
0.113
IMP
pH 7.7, 25°C, mutant V273N, hydroxylamine as substrate
0.14
IMP
pH 7.7, 25°C, mutant V273A, hydroxylamine as substrate
0.31
IMP
pH 7.7, 25°C, mutant T128A
0.32
IMP
pH 7.7, 25°C, mutant T301A, hydroxylamine as substrate
0.89
IMP
pH 7.7, 25°C, mutant T129A
0.013
L-Asp
22°C, cosubstrate: 2'-dIMP
0.23
L-Asp
22°C, cosubstrate: dIMP
0.17
L-aspartate
pH 7.7, 25°C, mutant T128A
0.23
L-aspartate
pH 7.7, 25°C, wild-type
0.24
L-aspartate
pH 7.7, 25°C, mutant T129A
0.82
L-aspartate
pH 7.7, 25°C, mutant T300V
3.4
L-aspartate
pH 7.7, 25°C, mutant V273T
6.2
L-aspartate
pH 7.7, 25°C, mutant T300A
7
L-aspartate
pH 7.7, 25°C, mutant V273A
9
L-aspartate
pH 7.7, 25°C, mutant V273N
0.03
Asp
-
-
0.03
Asp
-
IMP, wild-type
0.0657
Asp
-
mutant R303L
0.115
Asp
-
GTP, mutant S240A
0.23
Asp
-
Asp, wild-type
0.308
Asp
-
Asp, mutant K16Q
0.35
Asp
-
Asp, wild-type, and mutant Q224M
0.44
Asp
-
GTP, mutant K331R
0.17
aspartate
-
pH 7.7, 25°C, mutant D21A
0.23
aspartate
-
pH 7.7, 25°C, wild-type
0.24
aspartate
-
pH 7.7, 25°C, mutant N38E
0.3
aspartate
-
pH 7.7, 25°C, mutant N38A
0.34
aspartate
-
pH 7.7, 25°C, mutant R419L
0.5
aspartate
-
pH 5.6, 25°C, mutant N38D
0.9
aspartate
-
pH 5.6, 25°C, wild-type
1.4
aspartate
-
pH 7.7, 25°C, mutant T42A
2
aspartate
-
pH 7.7, 25°C, mutant H41N
2.6
aspartate
-
pH 7.7, 25°C, mutant N38D
0.01 - 0.048
GTP
-
-
0.01
GTP
-
Asp, mutant R305L
0.011
GTP
-
pH 5.6, 25°C, wild-type
0.0201
GTP
-
mutant R303L
0.023
GTP
-
GTP, mutant K16Q
0.026
GTP
-
pH 7.7, 25°C, wild-type
0.0265
GTP
-
mutant R304L
0.0306
GTP
-
mutant R305L
0.031
GTP
-
GTP, mutant E14A
0.035
GTP
-
IMP, mutant G15V
0.035
GTP
-
IMP, mutant R131L
0.035
GTP
-
GTP, mutant R131L
0.041
GTP
-
pH 7.7, 25°C, mutant N38A
0.052
GTP
-
pH 7.7, 25°C, mutant D21A
0.054
GTP
-
pH 7.7, 25°C, mutant N38E
0.0605
GTP
-
mutant Q224M
0.0689
GTP
-
mutant Q224E
0.0839
GTP
-
mutant L228A
0.116
GTP
-
pH 5.6, 25°C, mutant N38D
0.13
GTP
-
pH 7.7, 25°C, mutant H41N
0.25
GTP
-
pH 7.7, 25°C, mutant R419L
0.27
GTP
-
pH 7.7, 25°C, mutant N38D
0.28
GTP
-
pH 7.7, 25°C, mutant T42A
0.02
IMP
-
-
0.028
IMP
-
pH 7.7, 25°C, wild-type and mutant N38E
0.0296
IMP
-
mutant R304L
0.0305
IMP
-
mutant R305L
0.0352
IMP
-
mutant R303L
0.047
IMP
-
IMP, mutant K331R
0.048
IMP
-
pH 7.7, 25°C, mutant D21A
0.049
IMP
-
pH 7.7, 25°C, mutant N38A
0.0505
IMP
-
IMP, mutant Q224E
0.054
IMP
-
XTP, mutant D333Q
0.07
IMP
-
pH 5.6, 25°C, wild-type
0.0825
IMP
-
mutant S240A
0.123
IMP
-
pH 7.7, 25°C, mutant T42A
0.2
IMP
-
pH 7.7, 25°C, mutant R419L
0.32
IMP
-
Asp, mutant Q224E
0.4
IMP
-
pH 7.7, 25°C, mutant H41N
1.6
IMP
-
pH 7.7, 25°C, mutant N38D
1.73
IMP
-
Asp, mutant K331R
3.8
IMP
-
pH 5.6, 25°C, mutant N38D
1.07
ITP
-
mutant D333Q
1.27
UTP
-
mutant D333N
0.0286
XTP
-
mutant D333E
0.0331
XTP
-
mutant D333N
additional information
additional information
-
-
-
additional information
additional information
-
effect of metal ions on Km-values
-
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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
R147L
-
mutant R147L shows increased Km for IMP and GTP relative to the wild-type enzyme, Km for Asp exhibits a modest decrease
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
H41N
-
mutant enzyme D13A shows no measurable activity, mutant enzymes E14A and H41N exhibit 1% of the activity of the wild-type enzyme and 2-7fold increases in Km of substrates. The mutant enzyme K16Q has 34% of the activity of wild-type enzyme and Km values for substrates are virtually unchanged from those of the wild-type enzyme
H41N
-
site-directed mutagenesis
N38A
-
site-directed mutagenesis
N38A
-
directed mutagenesis
R143L
-
mutant enzyme R143L with no change in catalytic constant or Km for Asp, but significantly impaired nucleotide binding, 60fold increased Km for IMP and 10fold increased Km for GTP
R143L
-
although the mutants R143L and D13A have low or no activity independently, when they are mixed, a significant amount of activity is obtained. These results indicate that the subunits exchange with each other to form heterodimers with a single viable active site
R143L
-
site-directed mutagenesis
R303L
-
mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable
R303L
-
site-directed mutagenesis
R304L
-
mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable
R304L
-
site-directed mutagenesis
R305L
-
mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable
R305L
-
site-directed mutagenesis
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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
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
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