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Literature summary extracted from

  • Sivendran, S.; Colman, R.F.
    Effect of a new non-cleavable substrate analog on wild-type and serine mutants in the signature sequence of adenylosuccinate lyase of Bacillus subtilis and Homo sapiens (2008), Protein Sci., 17, 1162-1174.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
4.3.2.2 D69N site-directed mutagenesis, the mutant shows altered binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme Bacillus subtilis
4.3.2.2 H141Q site-directed mutagenesis, the mutant shows altered binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme Bacillus subtilis
4.3.2.2 H68A site-directed mutagenesis, the mutant shows altered binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme Bacillus subtilis
4.3.2.2 H89Q site-directed mutagenesis, the mutant shows altered binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme Bacillus subtilis
4.3.2.2 H89R site-directed mutagenesis, the mutant shows altered binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme Bacillus subtilis
4.3.2.2 S262A site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme Bacillus subtilis
4.3.2.2 S262H site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme Bacillus subtilis
4.3.2.2 S263A site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme Bacillus subtilis
4.3.2.2 S263H site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme Bacillus subtilis
4.3.2.2 S289A site-directed mutagenesis, the mutant shows no activity, and altered molecular weight and binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme Homo sapiens
4.3.2.2 S289H site-directed mutagenesis, the mutant shows no activity, and altered molecular weight and binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme Homo sapiens
4.3.2.2 S290A site-directed mutagenesis, the mutant shows altered molecular weight and binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme Homo sapiens
4.3.2.2 S290H site-directed mutagenesis, the mutant shows no activity, and altered molecular weight and binding of inhibitory substrate analogue adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate compared to the wild-type enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.2.2 adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate i.e. APBADP, the non-cleavable substrate analogue acts as a competitive inhibitor with respect to either substrate. ASL binds up to 4 mol of APBADP per mole of enzyme tetramer, the enzyme exhibits negative cooperativity. Binding to enzyme mutants, overview Bacillus subtilis
4.3.2.2 adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate i.e. APBADP, the non-cleavable substrate analogue acts as a competitive inhibitor with respect to either substrate. ASL binds up to 4 mol of APBADP per mole of enzyme tetramer, the enzyme exhibits positive cooperativity Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.2.2 0.0003
-
 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide pH 7.0, 25°C, mutant S290A Homo sapiens
4.3.2.2 0.0016
-
 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide pH 7.0, 25°C, wild-type enzyme Homo sapiens
4.3.2.2 0.0029
-
 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide pH 7.0, 25°C, wild-type enzyme Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.2.2 191000
-
 wild-type enzyme, light scattering Bacillus subtilis
4.3.2.2 192000
-
 mutant S263H, light scattering Bacillus subtilis
4.3.2.2 196000
-
 mutant S262A, light scattering Bacillus subtilis
4.3.2.2 197000
-
 mutant S263A, light scattering Bacillus subtilis
4.3.2.2 199000
-
 mutant S262H, light scattering Bacillus subtilis
4.3.2.2 221000
-
 mutant S290H, light scattering Homo sapiens
4.3.2.2 227000
-
 wild-type enzyme and mutant S289H, light scattering Homo sapiens
4.3.2.2 234000
-
 mutant S290A, light scattering Homo sapiens
4.3.2.2 237000
-
 mutant S289A, light scattering Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide Bacillus subtilis i.e. SAICAR 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate i.e. AICAR ?
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide Homo sapiens i.e. SAICAR 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate i.e. AICAR ?
4.3.2.2 additional information Bacillus subtilis adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides ?
-
 ?
4.3.2.2 additional information Homo sapiens adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides ?
-
 ?
4.3.2.2 succinyladenosine monophosphate Bacillus subtilis
-
 AMP + fumarate
-
 ?
4.3.2.2 succinyladenosine monophosphate Homo sapiens
-
 AMP + fumarate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.2 Bacillus subtilis
-
-
-
4.3.2.2 Homo sapiens P30566
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.3.2.2 (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism Bacillus subtilis
a
4.3.2.2 (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism Homo sapiens
a
4.3.2.2 N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism Bacillus subtilis
a
4.3.2.2 N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP uni-bi mechanism, where fumarate is removed by beta-elimination via a general base-general acid mechanism Homo sapiens
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.2.2 additional information
-
-
 Bacillus subtilis
4.3.2.2 additional information
-
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide i.e. SAICAR Bacillus subtilis 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate i.e. AICAR ?
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide i.e. SAICAR Homo sapiens 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate i.e. AICAR ?
4.3.2.2 additional information adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides Bacillus subtilis ?
-
 ?
4.3.2.2 additional information adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides Homo sapiens ?
-
 ?
4.3.2.2 additional information residue Ser289 is essential for catalysis Homo sapiens ?
-
 ?
4.3.2.2 additional information residues Ser262 and Ser263 in a flexible loop of the enzyme are essential for catalysis Bacillus subtilis ?
-
 ?
4.3.2.2 succinyladenosine monophosphate
-
 Bacillus subtilis AMP + fumarate
-
 ?
4.3.2.2 succinyladenosine monophosphate
-
 Homo sapiens AMP + fumarate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.3.2.2 ASL
-
 Bacillus subtilis
4.3.2.2 ASL
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.2.2 25
-
 assay at Bacillus subtilis
4.3.2.2 25
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.2.2 7
-
 assay at Bacillus subtilis
4.3.2.2 7
-
 assay at Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.3.2.2 0.16
-
 adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate inhibition kinetics, overview Bacillus subtilis
4.3.2.2 0.21
-
 adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate inhibition kinetics, overview Homo sapiens