BRENDA - Enzyme Database
show all sequences of 4.3.2.2

Elucidation of the substrate specificity, kinetic and catalytic mechanism of adenylosuccinate lyase from Plasmodium falciparum

Bulusu, V.; Srinivasan, B.; Bopanna, M.P.; Balaram, H.; Biochim. Biophys. Acta 1794, 642-654 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha
Plasmodium falciparum
Engineering
Amino acid exchange
Commentary
Organism
S298A
site-directed mutagenesis, the mutation does not lead to gross changes in the structural properties of ASL, but the specific activity of S298A mutant is 1000fold lower than that of the wild enzyme, the specific activity remains unchanged upon variation of pH
Plasmodium falciparum
S298C
site-directed mutagenesis, the mutation does not lead to gross changes in the structural properties of ASL, but the activity of the S298C mutant is completely lost
Plasmodium falciparum
Inhibitors
Inhibitors
Commentary
Organism
Structure
5-aminoimidazole-4-carboxamide ribonucleoside
50% inhibition at 0.167 mM
Plasmodium falciparum
AMP
product inhibition competitive versus succinyladenosine monophosphate
Plasmodium falciparum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
thermodynamics and kinetics, initial velocity and transient kinetics of succinyladenosine monophosphate cleavage, overview
Plasmodium falciparum
0.032
-
succinyladenosine monophosphate
pH 7.4, 25°C
Plasmodium falciparum
0.034
-
AMP
pH 7.4, 25°C
Plasmodium falciparum
0.76
-
fumarate
pH 7.4, 25°C
Plasmodium falciparum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry
Plasmodium falciparum
56235
-
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry
Plasmodium falciparum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
Plasmodium falciparum
first step common to both de novo and the salvage pathways in purine biosynthesis
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
?
additional information
Plasmodium falciparum
adenylosuccinate lyase is the only enzyme in the purine biosynthetic pathway that catalyzes two distinct, but chemically similar reactions
?
-
-
-
succinyladenosine monophosphate
Plasmodium falciparum
second step common to both de novo and the salvage pathways in purine biosynthesis
AMP + fumarate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Plasmodium falciparum
O15918
-
-
Reaction
Reaction
Commentary
Organism
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
kinetic and catalytic uni-bi rapid equilibrium ordered mechanism, key role for the conserved Ser298 in catalysis and pivotal role of the substrate in the activation of the catalytic base, detailed overview
Plasmodium falciparum
N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP
kinetic and catalytic mechanism, the enzyme follows a rapid equilibrium ordered bi-uni mechanism in the reverse direction in which AMP binds first to the enzyme followed by fumarate, key role for the conserved Ser298 in catalysis and pivotal role of the substrate in the activation of the catalytic base, detailed overview
Plasmodium falciparum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
first step common to both de novo and the salvage pathways in purine biosynthesis
691116
Plasmodium falciparum
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
i.e. SAICAR, SAICAR synthesis in vitro
691116
Plasmodium falciparum
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
i.e. AICAR
-
-
r
additional information
adenylosuccinate lyase is the only enzyme in the purine biosynthetic pathway that catalyzes two distinct, but chemically similar reactions
691116
Plasmodium falciparum
?
-
-
-
-
succinyladenosine monophosphate
-
691116
Plasmodium falciparum
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
second step common to both de novo and the salvage pathways in purine biosynthesis
691116
Plasmodium falciparum
AMP + fumarate
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry
Plasmodium falciparum
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Plasmodium falciparum
37
-
reverse reaction SAICAR synthesis
Plasmodium falciparum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.9
-
AMP
pH 7.4, 25°C
Plasmodium falciparum
2.9
-
fumarate
pH 7.4, 25°C
Plasmodium falciparum
7.5
-
succinyladenosine monophosphate
pH 7.4, 25°C
Plasmodium falciparum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Plasmodium falciparum
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.8
9
-
Plasmodium falciparum
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.093
-
AMP
pH 7.4, 25°C
Plasmodium falciparum
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha
Plasmodium falciparum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
S298A
site-directed mutagenesis, the mutation does not lead to gross changes in the structural properties of ASL, but the specific activity of S298A mutant is 1000fold lower than that of the wild enzyme, the specific activity remains unchanged upon variation of pH
Plasmodium falciparum
S298C
site-directed mutagenesis, the mutation does not lead to gross changes in the structural properties of ASL, but the activity of the S298C mutant is completely lost
Plasmodium falciparum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
5-aminoimidazole-4-carboxamide ribonucleoside
50% inhibition at 0.167 mM
Plasmodium falciparum
AMP
product inhibition competitive versus succinyladenosine monophosphate
Plasmodium falciparum
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.093
-
AMP
pH 7.4, 25°C
Plasmodium falciparum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
thermodynamics and kinetics, initial velocity and transient kinetics of succinyladenosine monophosphate cleavage, overview
Plasmodium falciparum
0.032
-
succinyladenosine monophosphate
pH 7.4, 25°C
Plasmodium falciparum
0.034
-
AMP
pH 7.4, 25°C
Plasmodium falciparum
0.76
-
fumarate
pH 7.4, 25°C
Plasmodium falciparum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry
Plasmodium falciparum
56235
-
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry
Plasmodium falciparum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
Plasmodium falciparum
first step common to both de novo and the salvage pathways in purine biosynthesis
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
?
additional information
Plasmodium falciparum
adenylosuccinate lyase is the only enzyme in the purine biosynthetic pathway that catalyzes two distinct, but chemically similar reactions
?
-
-
-
succinyladenosine monophosphate
Plasmodium falciparum
second step common to both de novo and the salvage pathways in purine biosynthesis
AMP + fumarate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
first step common to both de novo and the salvage pathways in purine biosynthesis
691116
Plasmodium falciparum
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
i.e. SAICAR, SAICAR synthesis in vitro
691116
Plasmodium falciparum
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
i.e. AICAR
-
-
r
additional information
adenylosuccinate lyase is the only enzyme in the purine biosynthetic pathway that catalyzes two distinct, but chemically similar reactions
691116
Plasmodium falciparum
?
-
-
-
-
succinyladenosine monophosphate
-
691116
Plasmodium falciparum
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
second step common to both de novo and the salvage pathways in purine biosynthesis
691116
Plasmodium falciparum
AMP + fumarate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry
Plasmodium falciparum
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Plasmodium falciparum
37
-
reverse reaction SAICAR synthesis
Plasmodium falciparum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.9
-
AMP
pH 7.4, 25°C
Plasmodium falciparum
2.9
-
fumarate
pH 7.4, 25°C
Plasmodium falciparum
7.5
-
succinyladenosine monophosphate
pH 7.4, 25°C
Plasmodium falciparum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Plasmodium falciparum
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.8
9
-
Plasmodium falciparum
Other publictions for EC 4.3.2.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
749293
Galina
-
Biochemical, thermodynamic an ...
Leishmania braziliensis
RSC Adv.
7
54347-54360
2017
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747484
Gooding
Adenylosuccinate is an insuli ...
Rattus norvegicus
Cell Rep.
13
157-167
2015
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729717
Banerjee
Structural and kinetic studies ...
Mycobacterium tuberculosis, Mycolicibacterium smegmatis
FEBS J.
281
1642-1658
2014
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2
2
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6
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2
2
729296
Ray
Inherent properties of adenylo ...
Homo sapiens
Biochim. Biophys. Acta
1834
1545-1553
2013
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7
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2
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6
6
729218
Ray
Structural and biochemical cha ...
Homo sapiens
Biochemistry
51
6701-6713
2012
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1
1
1
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1
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2
2
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1
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3
1
1
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1
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1
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1
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1
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2
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1
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1
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3
1
1
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1
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2
2
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714232
De Zoysa Ariyananda
In vitro hybridization and sep ...
Homo sapiens
Biochemistry
50
1336-1346
2011
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4
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2
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2
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12
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1
1
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4
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12
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1
1
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716175
Yuan
Molecular cloning, characteriz ...
Ctenopharyngodon idella
Mol. Biol. Rep.
38
2059-2065
2011
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8
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730526
Bierau
An HPLC-based assay of adenylo ...
Homo sapiens
Nucleosides Nucleotides Nucleic Acids
30
908-917
2011
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2
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708663
Zikanova
Biochemical and structural ana ...
Homo sapiens
Hum. Mutat.
31
445-455
2010
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1
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15
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709392
Chen
Adenylosuccinate lyase deficie ...
Homo sapiens
J. Inherit. Metab. Dis.
33
S159-162
2010
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709768
Chauhan
The purB gene controls rhizosp ...
Pantoea agglomerans
Lett. Appl. Microbiol.
50
205-210
2010
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710076
Camici
Pediatric neurological syndrom ...
Homo sapiens
Neurochem. Int.
56
367-378
2010
-
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710131
Henneke
In vivo proton MR spectroscopy ...
Homo sapiens
NMR Biomed.
23
441-445
2010
-
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1
1
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713618
Fyfe
Structure of Staphylococcus au ...
Staphylococcus aureus
Acta Crystallogr. Sect. D
66
881-888
2010
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692168
Gitiaux
Misleading behavioural phenoty ...
Homo sapiens
Eur. J. Hum. Genet.
17
133-136
2009
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Casey
Metabolism of threo-beta-fluor ...
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Porter
Nitro analogs of substrates fo ...
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34451
Pinto
Adenylosuccinate lyase from Ar ...
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3
3
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1
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1
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1
1
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1541
Spector
Specificity of adenylosuccinat ...
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6
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9
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6
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34467
Shaw
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Purines, pyrimidines, and imid ...
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34454
Woodward
Adenylosuccinate AMP-lyase (Ne ...
Neurospora crassa
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1978
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1
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Brand
Effect of diet on adenylosucci ...
Gallus gallus, Rattus norvegicus
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34456
Brand
Inhibition of adenylosuccinase ...
Rattus norvegicus
Biochemistry
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1365-1370
1978
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3
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15
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34457
Spector
Mammalian adenylosuccinate lya ...
Mus musculus, Rattus norvegicus
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741-745
1977
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34458
Carter
The preparation and properties ...
Saccharomyces cerevisiae
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1956
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