Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(Nomega-L-arginino)succinate
fumarate + L-arginine
-
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
5'-phosphoribosyl-5-amino-4-imidazolecarboxamide + fumarate
2',3'-dideoxyadenylosuccinate
dideoxyadenosine 5'-monophosphate + ?
-
at 1.44% of the activity with the natural substrate
-
?
2'-deoxy-succino-AMP
2'-deoxy-AMP + fumarate
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
8-aza-succino-AMP
8-aza-AMP + fumarate
-
-
-
?
adenylosuccinate
adenosine monophosphate + fumarate
adenylosuccinate
AMP + fumarate
adenylosuccinate 2',3'-acyclic dialcohol
adenylic 2',3'-acyclic dialcohol + fumarate
-
-
-
-
?
adenylosuccinate 2',3'-acyclic dialdehyde
?
-
-
-
?
arabinosyl-succino-AMP
arabinosyl-AMP + ?
fumarate + AMP
N6-(1,2-dicarboxyethyl)AMP
mercaptopurinosuccinate
?
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
phosphoribosylsuccinyl-aminoimidazole carboxamide
phosphoribosylaminoimidazole carboxamide + fumarate
-
-
-
-
?
succino-4-aminopyrazolo[3,4-d]pyrimidine ribose 5'-phosphate
4-aminopyrazolo[3,4-d]pyrimidine ribose 5'-phosphate + ?
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
additional information
?
-
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the enzyme is involved in both de novo and salvage pathways of purine biosynthesis
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
5'-phosphoribosyl-5-amino-4-imidazolecarboxamide + fumarate
-
-
-
-
?
1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
5'-phosphoribosyl-5-amino-4-imidazolecarboxamide + fumarate
-
-
-
?
1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
5'-phosphoribosyl-5-amino-4-imidazolecarboxamide + fumarate
-
-
-
?
1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
5'-phosphoribosyl-5-amino-4-imidazolecarboxamide + fumarate
-
i.e. 4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide ?
-
-
?
2'-deoxy-succino-AMP
2'-deoxy-AMP + fumarate
-
-
-
?
2'-deoxy-succino-AMP
2'-deoxy-AMP + fumarate
-
-
-
?
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
reaction in the biosynthesis of AMP
-
-
?
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
enzyme catalyzes two nonsequential reactions in purine biosynthesis
-
-
?
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
reaction in the biosynthesis of AMP
-
-
?
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
reaction in the biosynthesis of AMP
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
-
-
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
-
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
-
-
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
-
-
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
-
-
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
-
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
-
-
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
i.e. SAICAR
i.e. AICAR
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
i.e. SAICAR
i.e. AICAR
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
ZMP accumulation in the brain of Lesch-Nyhan disease patients induces inhibition of mitochondrial oxidative phosphorylation and adenylosuccinate lyase activity, followed by dowregulation of ATP levels and multifocal cell death in the cerebellum. ZMP is an inhibitor of the bifunctional enzyme adenylosuccinate lyase, a deficiency of this enzyme causes psychomotor and mental retardation in humans, overview, i.e. AICAR or ZMP
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
i.e. SAICAR
i.e. AICAR
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
i.e. SAICAR
i.e. AICAR
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
the 8th step in the purine nucleotide de novo pathway
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
first step common to both de novo and the salvage pathways in purine biosynthesis
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
i.e. SAICAR, SAICAR synthesis in vitro
i.e. AICAR
-
r
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
adenylosuccinate
adenosine monophosphate + fumarate
-
-
-
-
?
adenylosuccinate
adenosine monophosphate + fumarate
-
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
?
arabinosyl-succino-AMP
arabinosyl-AMP + ?
-
-
-
?
arabinosyl-succino-AMP
arabinosyl-AMP + ?
-
i.e. beta-D-arabinosyladenylosuccinate
beta-D-arabinosyl-AMP
?
fumarate + AMP
N6-(1,2-dicarboxyethyl)AMP
-
-
-
r
fumarate + AMP
N6-(1,2-dicarboxyethyl)AMP
-
-
-
r
fumarate + AMP
N6-(1,2-dicarboxyethyl)AMP
-
-
-
r
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
i.e. adenylosuccinate
-
r
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
i.e. adenylosuccinate
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
reaction in the biosynthesis of AMP
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
the enzyme is involved in both de novo and salvage pathways of purine biosynthesis
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
the enzyme follows a Uni-Bi ordered kinetic mechanism, in which release of fumarate is followed by AMP to yield free enzyme
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
i.e. adenylosuccinate
-
r
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
i.e. adenylosuccinate
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
terminal step in AMP biosynthesis
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
reaction in the biosynthesis of AMP
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
i.e. adenylosuccinate
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
i.e. adenylosuccinate
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
i.e. adenylosuccinate
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
reaction in the biosynthesis of AMP
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
i.e. adenylosuccinate
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
i.e. adenylosuccinate
-
r
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
enzyme catalyzes the last step in the pathway of AMP biosynthesis
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
conversion of adenylosuccinate to adenylate in the purine nucleotide cycle
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
-
r
succinyladenosine monophosphate
AMP + fumarate
-
-
-
r
succinyladenosine monophosphate
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
second step common to both de novo and the salvage pathways in purine biosynthesis
-
-
?
additional information
?
-
-
adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides
-
-
?
additional information
?
-
-
residues Ser262 and Ser263 in a flexible loop of the enzyme are essential for catalysis
-
-
?
additional information
?
-
adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides
-
-
?
additional information
?
-
-
adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides
-
-
?
additional information
?
-
adenylosuccinate lyase deficiency is a rare autosomal disorder of de novo purine synthesis, which results in the accumulation of succinylpurines in body fluids. Patients with adenylosuccinate lyase deficiency show a variable combination of mental retardation, epilepsy and autistic features, overview
-
-
?
additional information
?
-
-
adenylosuccinate lyase deficiency is a rare autosomal disorder of de novo purine synthesis, which results in the accumulation of succinylpurines in body fluids. Patients with adenylosuccinate lyase deficiency show a variable combination of mental retardation, epilepsy and autistic features, overview
-
-
?
additional information
?
-
-
adenylosuccinate lyase deficiency is an autosomal recessive disorder of the purine de novo synthesis pathway and purine nucleotide cycleby severe neurological involvement including hypotonia, seizures, developmental delay and autistic features. Epilepsy in ADSL deficiency is frequent and occurs in approximately two-thirds of patients, beginning either early in the neonatal period or after the first year of life
-
-
?
additional information
?
-
-
ZMP is an activator of the AMP-activated protein kinase, AMPK, and is toxic in human B lymphocytes and neuroblastoma cell lines, physiological functions of ZMP, overview
-
-
?
additional information
?
-
residue Ser289 is essential for catalysis
-
-
?
additional information
?
-
-
residue Ser289 is essential for catalysis
-
-
?
additional information
?
-
-
development of a rapid and simple HPLC-based assay method to quantitatively measure ADSL activity with succinyladenosine monophosphate in erythrocytes using isocratic ionpairing reversed-phase HPLC with UV-detection, overview
-
-
?
additional information
?
-
interaction between the enzyme and phosphoribosylsuccinyl-aminoimidazole carboxamide, isothermal titration calorimetry, overview. Modeling of AMPand phosphoribosylaminoimidazole carboxamide, and fumarate binding in the active site of wild-type and R303C mutant enzymes
-
-
?
additional information
?
-
-
interaction between the enzyme and phosphoribosylsuccinyl-aminoimidazole carboxamide, isothermal titration calorimetry, overview. Modeling of AMPand phosphoribosylaminoimidazole carboxamide, and fumarate binding in the active site of wild-type and R303C mutant enzymes
-
-
?
additional information
?
-
-
the activity of the Mycobacterium tuberculosis enzyme is particularly low
-
-
?
additional information
?
-
adenylosuccinate lyase is the only enzyme in the purine biosynthetic pathway that catalyzes two distinct, but chemically similar reactions
-
-
?
additional information
?
-
-
adenylosuccinate lyase is the only enzyme in the purine biosynthetic pathway that catalyzes two distinct, but chemically similar reactions
-
-
?
additional information
?
-
-
the low activity of the enzyme in liver of severely starved rats is inconsistent with the proposal that the purine nucleotide cycle plays a major role in ammonia production for urea synthesis at least under these conditions
-
-
?
additional information
?
-
-
roles of adenylosuccinate lyase and of AMP deaminase in the anti-HIV activity of 2',3'-dideoxyadenosine and 2',3'-dideoxyinosine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
5'-phosphoribosyl-5-amino-4-imidazolecarboxamide + fumarate
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
adenylosuccinate
AMP + fumarate
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
phosphoribosylsuccinyl-aminoimidazole carboxamide
phosphoribosylaminoimidazole carboxamide + fumarate
-
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
additional information
?
-
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the enzyme is involved in both de novo and salvage pathways of purine biosynthesis
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
5'-phosphoribosyl-5-amino-4-imidazolecarboxamide + fumarate
-
-
-
-
?
1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
5'-phosphoribosyl-5-amino-4-imidazolecarboxamide + fumarate
-
-
-
?
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
reaction in the biosynthesis of AMP
-
-
?
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
enzyme catalyzes two nonsequential reactions in purine biosynthesis
-
-
?
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
reaction in the biosynthesis of AMP
-
-
?
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
reaction in the biosynthesis of AMP
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
-
-
-
-
?
5-aminoimidazole-(N-succinylocarboxamide) ribotide
5-aminoimidazole-4-carboxamide ribotide + fumarate
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
i.e. SAICAR
i.e. AICAR
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
ZMP accumulation in the brain of Lesch-Nyhan disease patients induces inhibition of mitochondrial oxidative phosphorylation and adenylosuccinate lyase activity, followed by dowregulation of ATP levels and multifocal cell death in the cerebellum. ZMP is an inhibitor of the bifunctional enzyme adenylosuccinate lyase, a deficiency of this enzyme causes psychomotor and mental retardation in humans, overview
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
i.e. SAICAR
i.e. AICAR
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
the 8th step in the purine nucleotide de novo pathway
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
first step common to both de novo and the salvage pathways in purine biosynthesis
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
-
?
adenylosuccinate
AMP + fumarate
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
reaction in the biosynthesis of AMP
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
the enzyme is involved in both de novo and salvage pathways of purine biosynthesis
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
terminal step in AMP biosynthesis
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
reaction in the biosynthesis of AMP
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
reaction in the biosynthesis of AMP
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
enzyme catalyzes the last step in the pathway of AMP biosynthesis
-
-
?
N6-(1,2-dicarboxyethyl)AMP
fumarate + AMP
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
conversion of adenylosuccinate to adenylate in the purine nucleotide cycle
-
-
?
succinyladenosine monophosphate
AMP + fumarate
-
-
-
-
r
succinyladenosine monophosphate
AMP + fumarate
-
-
-
r
succinyladenosine monophosphate
AMP + fumarate
second step common to both de novo and the salvage pathways in purine biosynthesis
-
-
?
additional information
?
-
-
adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides
-
-
?
additional information
?
-
adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides
-
-
?
additional information
?
-
-
adenylosuccinate lyase catalyzes two reactions in the biosynthesis of purine nucleotides
-
-
?
additional information
?
-
adenylosuccinate lyase deficiency is a rare autosomal disorder of de novo purine synthesis, which results in the accumulation of succinylpurines in body fluids. Patients with adenylosuccinate lyase deficiency show a variable combination of mental retardation, epilepsy and autistic features, overview
-
-
?
additional information
?
-
-
adenylosuccinate lyase deficiency is a rare autosomal disorder of de novo purine synthesis, which results in the accumulation of succinylpurines in body fluids. Patients with adenylosuccinate lyase deficiency show a variable combination of mental retardation, epilepsy and autistic features, overview
-
-
?
additional information
?
-
-
adenylosuccinate lyase deficiency is an autosomal recessive disorder of the purine de novo synthesis pathway and purine nucleotide cycleby severe neurological involvement including hypotonia, seizures, developmental delay and autistic features. Epilepsy in ADSL deficiency is frequent and occurs in approximately two-thirds of patients, beginning either early in the neonatal period or after the first year of life
-
-
?
additional information
?
-
-
ZMP is an activator of the AMP-activated protein kinase, AMPK, and is toxic in human B lymphocytes and neuroblastoma cell lines, physiological functions of ZMP, overview
-
-
?
additional information
?
-
-
the activity of the Mycobacterium tuberculosis enzyme is particularly low
-
-
?
additional information
?
-
adenylosuccinate lyase is the only enzyme in the purine biosynthetic pathway that catalyzes two distinct, but chemically similar reactions
-
-
?
additional information
?
-
-
adenylosuccinate lyase is the only enzyme in the purine biosynthetic pathway that catalyzes two distinct, but chemically similar reactions
-
-
?
additional information
?
-
-
the low activity of the enzyme in liver of severely starved rats is inconsistent with the proposal that the purine nucleotide cycle plays a major role in ammonia production for urea synthesis at least under these conditions
-
-
?
additional information
?
-
-
roles of adenylosuccinate lyase and of AMP deaminase in the anti-HIV activity of 2',3'-dideoxyadenosine and 2',3'-dideoxyinosine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-aminopyrazolo[3,4-d]pyrimidine ribose 5'-phosphate
-
-
5-aminoimidazole-4-carboxamide ribonucleoside
50% inhibition at 0.167 mM
5-aminoimidazole-4-carboxamide riboside 5'-monophosphate
-
i.e. ZMP or AICAR, product inhibition, accumulation in the brain of Lesch-Nyhan disease patients induces inhibition of mitochondrial oxidative phosphorylation and adenylosuccinate lyase activity, followed by dowregulation of ATP levels and multifocal cell death in the cerebellum
adenosine phosphonobutyric acid, 2'(3'),5'-diphosphate
adenosine phosphonobutyric, 2'(3'), 5'-diposphate
-
-
adenyloethylphosphonate
-
-
adenylosuccinate 2',3'-acyclic (N,N-ethyl) diamine
-
weak
adenylosuccinate 2',3'-acyclic dialcohol
-
-
adenylosuccinate 2',3'-acyclic dialdehyde
-
-
ammonium salt of N6-malonyl adenosine 5'-phosphate
-
noncompetitive inhibitor, irreversible
CuSO4
-
complete inhibition at 0.05 mM
DL-3-phosphonoalanine
-
-
erythro-beta-fluoro-4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
-
-
erythro-beta-fluoroadenylosuccinate
-
-
erythro-beta-fluoroaspartate
-
-
KBr
presence of increasing concentrations of KBr of 0.12.5 M disrupt electrostatic interactions leading to ASL dissociation and loss of catalytic activity
KCl
-
stimulates up to maximum concentration of 80 mM, inhibition at higher concentration
mercaptopurinosuccinate
-
substrate inhibition
Mg2+
-
concentration of Mg2+ approaching that of EDTA
N-(5-amino-1-(beta-D-ribofuranosyl)imidazole-4-carbonyl)-L-threo-beta-methylaspartic acid 5'-phosphate
-
-
N6-(2-carboxyethyl)-AMP
-
i.e. adenylopropionate
N6-(D-1,2-dicarboxyethyl)-AMP
-
i.e. D-adenylosuccinate
N6-(DL-1,2-dicarboxy-threo-2-hydroxyethyl)-AMP
-
i.e. adenylomalate
N6-(DL-1-carboxy-2-phosphonoethyl)AMP
-
i.e. adenylophosphonopropionate
N6-(L-1,3-dicarboxyprop-1-yl)-AMP
-
i.e. adenyloglutarate
N6-(L-1-carboxy-2-cyanoethyl)-AMP
-
i.e. adenylocyanopropionate
N6-(L-1-carboxy-2-methylsulfoxyethyl)-AMP
-
i.e. adenylomethylsulfoxypropionate
N6-(L-1-carboxy-2-nitroethyl)-AMP
-
competitive
N6-(L-1-carboxy-2-sulfinoethyl)-AMP
-
i.e. adenylosulfinopropionate
N6-(L-1-carboxy-2-sulfoethyl)-AMP
-
i.e. adenylosulfopropionate
nitroacrylate
-
0.02 mM, 70% inactivation
phosphopropionoadenosine
-
-
PO43-
-
activates at low concentration, inhibits at high concentrations above 25 mM
SO42-
-
activates at low concentrations, inhibits at concentrations above 25 mM
threo-beta-4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
-
-
threo-beta-fluoroadenylosuccinate
-
-
trans-4-hydroxy-2-nonenal
virazole 5'-phosphate
-
-
2'-deoxy-AMP
-
-
2'-deoxy-AMP
-
competitive
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
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
AMP
-
competitive
AMP
product inhibition competitive versus succinyladenosine monophosphate
arabinosyl-AMP
-
-
arabinosyl-AMP
-
beta-D-arabinosyl-AMP, competitive
fumarate
-
noncompetitive
fumarate
-
noncompetitive
fumarate
-
noncompetitive
nonenal
-
-
trans-4-hydroxy-2-nonenal
-
10-15 µM, inhibitor reacts both with the free enzyme and the enzyme substrate complex
trans-4-hydroxy-2-nonenal
-
10-15 µM, inhibitor reacts both with the free enzyme and the enzyme substrate complex
trans-4-hydroxy-2-nonenal
-
10-15 µM, inhibitor reacts both with the free enzyme and the enzyme substrate complex
trans-4-hydroxy-2-nonenal
-
10-15 µM, inhibitor reacts both with the free enzyme and the enzyme substrate complex
additional information
-
dithiothreitol increases inhibition of trans-4-hydroxy-2-nonenal; hydroxylamine reverses inhibition of trans-4-hydroxy-2-nonenal
-
additional information
as hydrophobic interactions are weakened at 8°C and 4°C, the catalytic activity of ASL decreases strikingly and the enzyme dissociates to a mixture of monomer-dimer-trimer, with small amounts of tetramer
-
additional information
-
as hydrophobic interactions are weakened at 8°C and 4°C, the catalytic activity of ASL decreases strikingly and the enzyme dissociates to a mixture of monomer-dimer-trimer, with small amounts of tetramer
-
additional information
-
dithiothreitol increases inhibition of trans-4-hydroxy-2-nonenal; hydroxylamine reverses inhibition of trans-4-hydroxy-2-nonenal
-
additional information
-
dithiothreitol increases inhibition of trans-4-hydroxy-2-nonenal; hydroxylamine reverses inhibition of trans-4-hydroxy-2-nonenal
-
additional information
-
dithiothreitol increases inhibition of trans-4-hydroxy-2-nonenal; hydroxylamine reverses inhibition of trans-4-hydroxy-2-nonenal
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0111
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
pH 7.5, 25°C
0.0437
2',3'-dideoxyadenylosuccinate
-
-
0.0008 - 0.003
2'-deoxy-succino-AMP
0.001 - 0.0081
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
0.0003 - 0.0029
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
0.0095
8-aza-succino-AMP
-
-
0.00146 - 0.023
adenylosuccinate
0.0013 - 0.0551
adenylsuccinate
0.0027 - 0.0056
arabinosyl-succino-AMP
0.02
mercaptopurinosuccinate
-
-
0.0012 - 0.013
N6-(1,2-dicarboxyethyl)AMP
0.0007 - 0.009
phosphoribosylsuccinyl-aminoimidazole carboxamide
0.011
succino-4-aminopyrazolo[3,4-d]pyrimidine ribose 5'-phosphate
-
-
0.0014 - 0.2042
succinyladenosine monophosphate
additional information
additional information
-
0.0008
2'-deoxy-succino-AMP
-
-
0.003
2'-deoxy-succino-AMP
-
-
0.001
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
-
-
0.0081
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide
-
-
0.0003
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
pH 7.0, 25°C, mutant S290A
0.0016
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
pH 7.0, 25°C, wild-type enzyme
0.0029
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
-
pH 7.0, 25°C, wild-type enzyme
0.00146
adenylosuccinate
-
histidine-tagged enzyme
0.0015
adenylosuccinate
-
mutant D69E
0.00177
adenylosuccinate
-
wild-type enzyme
0.00178
adenylosuccinate
-
none-tagged enzyme
0.0021
adenylosuccinate
-
wild-type enzyme
0.00224
adenylosuccinate
-
mutant S94A
0.0027
adenylosuccinate
-
wild type, 50 mM HEPES, pH 7.0, 25°C
0.0071
adenylosuccinate
-
mutant R310K
0.0093
adenylosuccinate
-
mutant D69N
0.0128
adenylosuccinate
-
mutant S306A
0.0177
adenylosuccinate
-
mutant T93A
0.0192
adenylosuccinate
-
mutant T140A
0.023
adenylosuccinate
-
mutant R310Q
0.0013
adenylsuccinate
-
mutant D69E, 50 mM HEPES, pH 7.0, 25°C
0.002
adenylsuccinate
-
mutant D65R/D69E, 50 mM HEPES, pH 7.0, 25°C
0.004
adenylsuccinate
-
50 mM HEPES, pH 7.0, 25°C
0.0043
adenylsuccinate
-
mutant I62E/D69E, 50 mM HEPES, pH 7.0, 25°C
0.0046
adenylsuccinate
-
mutant D65R, 50 mM HEPES, pH 7.0, 25°C
0.0061
adenylsuccinate
-
mutant I62E/D65R/D69E, 50 mM HEPES, pH 7.0, 25°C
0.0107
adenylsuccinate
-
mutant I62D/D65R/D69E, 50 mM HEPES, pH 7.0, 25°C
0.0166
adenylsuccinate
-
mutant Q212E, 50 mM HEPES, pH 7.0, 25°C
0.0175
adenylsuccinate
-
mutant I62E, 50 mM HEPES, pH 7.0, 25°C
0.0177
adenylsuccinate
-
mutant I62D/D69E, 50 mM HEPES, pH 7.0, 25°C
0.0181
adenylsuccinate
-
mutant I62E/D65R, 50 mM HEPES, pH 7.0, 25°C
0.0488
adenylsuccinate
-
mutant I62D/D65R, 50 mM HEPES, pH 7.0, 25°C
0.0551
adenylsuccinate
-
mutant I62D, 50 mM HEPES, pH 7.0, 25°C
0.004
AMP
-
-
0.0027
arabinosyl-succino-AMP
-
-
0.0056
arabinosyl-succino-AMP
-
-
0.035
fumarate
-
-
0.76
fumarate
pH 7.4, 25°C
0.0012
N6-(1,2-dicarboxyethyl)AMP
-
-
0.0015
N6-(1,2-dicarboxyethyl)AMP
-
-
0.00254
N6-(1,2-dicarboxyethyl)AMP
-
enzyme from cell line 1751
0.00289
N6-(1,2-dicarboxyethyl)AMP
-
enzyme from cell line 1753
0.0033
N6-(1,2-dicarboxyethyl)AMP
-
-
0.0033
N6-(1,2-dicarboxyethyl)AMP
-
enzyme from wild-type cell lines
0.0047
N6-(1,2-dicarboxyethyl)AMP
-
-
0.012
N6-(1,2-dicarboxyethyl)AMP
-
-
0.013
N6-(1,2-dicarboxyethyl)AMP
-
-
0.0007
phosphoribosylsuccinyl-aminoimidazole carboxamide
-
recombinant His-tagged mutant R426H, pH 7.4, 25°C
0.00174
phosphoribosylsuccinyl-aminoimidazole carboxamide
-
recombinant His-tagged wild-type enzyme, pH 7.4, 25°C
0.009
phosphoribosylsuccinyl-aminoimidazole carboxamide
-
recombinant His-tagged mutant R303C, pH 7.4, 25°C
0.0014
succinyladenosine monophosphate
-
recombinant His-tagged mutant R426H, pH 7.4, 25°C
0.0021
succinyladenosine monophosphate
-
recombinant His-tagged wild-type enzyme, pH 7.4, 25°C
0.0027
succinyladenosine monophosphate
-
recombinant His-tagged mutant R303C, pH 7.4, 25°C
0.0091
succinyladenosine monophosphate
-
wild-type enzyme, pH 8.1, 37°C
0.032
succinyladenosine monophosphate
pH 7.4, 25°C
0.0437
succinyladenosine monophosphate
pH 7.6, 37°C
0.2042
succinyladenosine monophosphate
-
pH 7.6, 37°C
additional information
additional information
-
pH-dependence of Km-value
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
thermodynamics and kinetics, initial velocity and transient kinetics of succinyladenosine monophosphate cleavage, overview
-
additional information
additional information
-
thermodynamics and kinetics, initial velocity and transient kinetics of succinyladenosine monophosphate cleavage, overview
-
additional information
additional information
-
non-linear dependence of the activities on the substrate ratios due to competitive binding. The enzyme does not follow simple Michaelis-Menten kinetics, kinetic analysis of wild-type and mutant enzymes, overview. Wild-type enzyme and mutant R426H appear to have equivalent cooperative binding on both substrates, while mutant R303C demonstrates no cooperativity
-
additional information
additional information
the enzyme shows cooperativity and does not follow simple Michaelis-Menten kinetics, kinetic analysis, overview
-
additional information
additional information
-
the enzyme shows cooperativity and does not follow simple Michaelis-Menten kinetics, kinetic analysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000083
-
mutant R310Q, pH 7.0
0.004
mutant S295A, pH 7.0
0.008
mutant H171N, pH 7.0
0.009
mutant H171A, pH 7.0
0.031
mutant H171A, pH 8.5
0.063
-
mutant I62D/D65R, adenylsuccinate, 50 mM HEPES, pH 7.0, 25°C
0.068
-
complementation of inactive mutant ASLs, maximum specific activity, T93A + H141Q, 3.0% wild-type activity
0.069
-
mutant I62D/D65R, succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
0.072
-
mutant I62D/D65R/D69E, adenylsuccinate, 50 mM HEPES, pH 7.0, 25°C
0.094
-
mutant I62D/D65R/D69E, succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
0.096
-
complementation of inactive mutant ASLs, maximum specific activity, S306A + H141Q, 4.6% wild-type activity
0.1
-
mutant R310K, pH 7.0
0.18
-
mutant I62D/D65R + I62E/D65R/D69E, adenylsuccinate, 50 mM HEPES, pH 7.0, 25°C
0.2
wild-type enzyme at 4 mg/ml and 4°C
0.21
-
complementation of inactive mutant ASLs, maximum specific activity, T93A + K268Q, 10.1% wild-type activity
0.33
-
mutant I62E/D65R/D69E, adenylsuccinate, 50 mM HEPES, pH 7.0, 25°C
0.46
-
mutant I62E/D65R/D69E, succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
0.53
-
mutant I62E/D65R/D69E, succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
0.54
-
mutant I62E/D65R, adenylsuccinate, 50 mM HEPES, pH 7.0, 25°C
0.97
-
mutant I62E/D65R/D69E, adenylsuccinate + succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
1
-
mutant R396H, pH 7.4, 25°C
1.07
-
adenylsuccinate and succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
1.09
-
mutant I62D/D65R, adenylsuccinate + succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
1.1
-
mutant R396H, after treatment with guanidiniumHCl, pH 7.4, 25°C
1.29
-
mutant I62D/D65R + I62E/D65R/D69E, adenylsuccinate + succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
1.3
-
mutant I62D/D65R/D69E, adenylsuccinate + succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
1.4
-
mutant I62E/D65R/D69E, adenylsuccinate + succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
1.58
-
adenylsuccinate, 50 mM HEPES, pH 7.0, 25°C
1.6
-
mutant R396C, after treatment with guanidiniumHCl, pH 7.4, 25°C
1.75
-
wild-type enzyme, pH 7.0
1.8
-
mutant R396C, pH 7.4, 25°C
13.9
-
purified recombinant His-tagged wild-type enzyme, substrate succinyladenosine monophosphate, pH 7.4, 25°C
16.47
wild-type protein, pH 8.5
20
-
crude cell extract, presence of 1 M KCl, pH 7.5, temperature not specified in the publication
23.3
-
purified recombinant His-tagged wild-type enzyme, substrate phosphoribosylsuccinyl-aminoimidazole carboxamide, pH 7.4, 25°C
4.65
wild-type protein, pH 7.0
40
-
crude cell extract, presence of 1 M KCl, pH 7.5, temperature not specified in the publication
6.4
-
purified recombinant His-tagged mutant R426H enzyme, substrate phosphoribosylsuccinyl-aminoimidazole carboxamide, pH 7.4, 25°C
6.7
-
purified recombinant His-tagged mutant R426H enzyme, substrate succinyladenosine monophosphate, pH 7.4, 25°C
7.5
-
His-tagged mutant L311V, after treatment with guanidiniumHCl, pH 7.4, 25°C
7.8
-
His-tagged mutant L311V, pH 7.4, 25°C
8.3
-
His-tagged wild-type, after treatment with guanidiniumHCl, pH 7.4, 25°C
8.4
-
wild-type, after treatment with guanidiniumHCl, pH 7.4, 25°C
8.5
-
His-tagged wild-type, pH 7.4, 25°C
8.6
-
wild-type, pH 7.4, 25°C
8.7
-
His-tagged mutant R194C, pH 7.4, 25°C
8.9
-
His-tagged mutant R194C, after treatment with guanidiniumHCl, pH 7.4, 25°C
0.04
-
mutant D69N, pH 7.0
0.04
mutant H171N, pH 8.5
0.24
-
mutant I62D/D65R + I62E/D65R/D69E, succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
0.24
-
complementation of inactive mutant ASLs, maximum specific activity, T140A + H68Q, 11.5% wild-type activity
0.32
-
complementation of inactive mutant ASLs, maximum specific activity, S306A + K268Q, 15.4% wild-type activity
0.32
-
complementation of inactive mutant ASLs, maximum specific activity, T140A + K268Q, 15.4% wild-type activity
0.4
-
mutant D69E, pH 7.0
0.4
wild-type enzyme at 4 mg/ml and 8°C
1.7
wild-type enzyme at 4 mg/ml and 25°C
1.7
-
succinylaminoimidazole carboxamide, 50 mM HEPES, pH 7.0, 25°C
3.6
-
final purified human enzyme
3.6
-
imidazole gradient elution
additional information
-
-
additional information
-
complementation of inactive mutant ASLs, maximum specific activity, T140A + H141Q, T93A + H68Q, S306A + H68Q 0% wild-type activity
additional information
specific activities of different enzyme variants with different subunit numbers
additional information
-
specific activities of different enzyme variants with different subunit numbers
additional information
-
-
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
147000
-
determined by native polyacrylamide gel electrophoresis, wild-type enzyme
148000
-
determined by native polyacrylamide gel electrophoresis, mutant R310K
152000
-
mutant N270L, light scattering measurements, 0.2 mg/ml enzyme in a filtered 20 mM potassium phosphate buffer at pH 7.0, containing 20 mM potassium chloride
153000
-
wild type, light scattering measurements, 0.2 mg/ml enzyme in a filtered 20 mM potassium phosphate buffer at pH 7.0, containing 20 mM potassium chloride
155000
-
mutant D69E, light scattering method, 0.25 mg/ml
166000
-
mutant N270D, light scattering measurements, 0.2 mg/ml enzyme in a filtered 20 mM potassium phosphate buffer at pH 7.0, containing 20 mM potassium chloride
174000
-
mutant Q212M, light scattering measurements, 0.2 mg/ml enzyme in a filtered 20 mM potassium phosphate buffer at pH 7.0, containing 20 mM potassium chloride
181000
-
light scattering method, 0.25 mg/ml
182000
-
determined by light scattering, mutant R310K
192000
-
mutant S263H, light scattering
193000
-
determined by native polyacrylamide gel electrophoresis, mutant S93A
194800
-
determined by analytical ultracentrifugation, mutant T140A
197000
-
mutant S263A, light scattering
199000
-
mutant S262H, light scattering
199700
-
determined by analytical ultracentrifugation, wild-type enzyme
201000
-
mutant enzyme S413P, gel filtration
209000
-
mutant I62E/D65R, native PAGE
214500
recombinant His-tagged R303C mutant enzyme
216400
-
determined by analytical ultracentrifugation, mutant S306A
217000
-
mutant I62D/D65R, native PAGE
219000
-
mutant R301Q, light scattering measurements, 0.2 mg/ml enzyme in a filtered 20 mM potassium phosphate buffer at pH 7.0, containing 20 mM potassium chloride
221000
mutant S290H, light scattering
222000
-
analytical ultracentrifugation
223000
gel filtration, at 22°C
225000
recombinant His-tagged wild-type enzyme
228000
-
gel filtration, His-tagged protein
230000
analytical ultracentrifugation, at 25°C
237000
mutant S289A, light scattering
49490
-
x * 49490, calculation from nucleotide sequence
49600
4 * 49600, calculated. Enzyme forms a dimer of dimers, crystallization data
54552
x * 54552, calculated
56235
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry
159000
-
mutant I62E/D65R/D69E, light scattering method, 0.25 mg/ml
159000
-
mutant Q212E, light scattering measurements, 0.2 mg/ml enzyme in a filtered 20 mM potassium phosphate buffer at pH 7.0, containing 20 mM potassium chloride
173000
-
mutant I62E, light scattering method, 0.25 mg/ml
173000
-
mutant R301K, light scattering measurements, 0.2 mg/ml enzyme in a filtered 20 mM potassium phosphate buffer at pH 7.0, containing 20 mM potassium chloride
176000
-
mutant I62D, light scattering method, 0.25 mg/ml
176000
-
determined by light scattering, mutant D69N
191000
-
determined by light scattering, wild-type enzyme
191000
-
wild-type enzyme, light scattering
194000
-
determined by light scattering, mutant D69E
194000
-
determined by native polyacrylamide gel electrophoresis, mutant T93A
196000
-
wild-type enzyme, gel filtration
196000
-
determined by native polyacrylamide gel electrophoresis, wild-type enzyme
196000
-
mutant S262A, light scattering
200000
-
-
227000
wild-type enzyme and mutant S289H, light scattering
227000
analytical ultracentrifugation, at 37°C
234000
-
mutant I62D/D65R/D69E, light scattering method, 0.25 mg/ml
234000
mutant S290A, light scattering
50000
-
2 * 50000, SDS-PAGE
50000
-
4 * 50000, SDS-PAGE
50000
-
4 * 50000, SDS-PAGE
52000
-
monomer
52000
-
4 * 52000, SDS-PAGE
55000
-
x * 55000, calculation from nucleotide sequence
55000
4 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 56235, recombinant His-tagged enzyme, mass spectrometry
56000
-
x * 56000, SDS-PAGE
56000
4 * 56000, analytical ultracentrifugation
57000
-
histidine-tagged enzyme, determined by SDS-PAGE
57000
4 * 57000, SDS-PAGE
57000
-
4 * 57000, calculated, His-tagged protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D65R
-
mutant with differences in thermal stability, catalytic activity and substrate binding
D65R/D69E
-
mutant with differences in thermal stability, catalytic activity and substrate binding
E239M
site-directed mutagenesis, the mutant shows reduced Vmax, increased Km, and lower molecular weight compared to the wild-type enzyme, subunit structure analysis
E239Q
site-directed mutagenesis, the mutant shows reduced Vmax, increased Km, and lower molecular weight compared to the wild-type enzyme, subunit structure analysis
E239R
site-directed mutagenesis, the mutant shows reduced Vmax, increased Km, and lower molecular weight compared to the wild-type enzyme, subunit structure analysis
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
H299K
site-directed mutagenesis, the mutant shows reduced Vmax, increased Km, and lower molecular weight compared to the wild-type enzyme, subunit structure analysis
H299R
site-directed mutagenesis, the mutant shows reduced Vmax, increased Km, and lower molecular weight compared to the wild-type enzyme, subunit structure analysis
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
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
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
I62D
-
mutant with differences in thermal stability, catalytic activity and substrate binding
I62D/D65R
-
mutant with differences in thermal stability, catalytic activity and substrate binding
I62D/D65R/D69E
-
mutant with differences in thermal stability, catalytic activity and substrate binding
I62D/D69E
-
mutant with differences in thermal stability, catalytic activity and substrate binding
I62E
-
mutant with differences in thermal stability, catalytic activity and substrate binding
I62E/D65R
-
"humanized" normal enzyme
I62E/D65R/D69E
-
mutant with differences in thermal stability, catalytic activity and substrate binding
I62E/D69E
-
mutant with differences in thermal stability, catalytic activity and substrate binding
N270D
-
mutant with impaired activity
N270L
-
mutant with impaired activity
Q212E
-
mutant with impaired activity
Q212M
-
mutant with impaired activity
R167E
site-directed mutagenesis, the mutant shows reduced Vmax, increased Km, and lower molecular weight compared to the wild-type enzyme, subunit structure analysis
R167Q
site-directed mutagenesis, the mutant shows reduced Vmax, increased Km, and lower molecular weight compared to the wild-type enzyme, subunit structure analysis
R301K
-
mutant with impaired activity
R301Q
-
mutant with impaired activity
R310K
-
mutant shows little change in pK2
R310Q
-
mutant exibits a decrease in its pK2
S262A
-
site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme
S262H
-
site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme
S263A
-
site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme
S263H
-
site-directed mutagenesis, the mutant shows no activity and altered molecular weight compared to the wild-type enzyme
S306A
-
conserved amino acid in all adenylosuccinate lyases, mutant for testing the involvement of the residue in the enzyme function
S94A
-
conserved amino acid in all adenylosuccinate lyases, mutant for testing the involvement of the residue in the enzyme function
T140A
-
conserved amino acid in all adenylosuccinate lyases, mutant for testing the involvement of the residue in the enzyme function
T93A
-
conserved amino acid in all adenylosuccinate lyases, mutant for testing the involvement of the residue in the enzyme function
H171A
mutant to map out the residues involved in adenylosuccinate binding, and to identify the putative catalytic groups
H171N
mutant to map out the residues involved in adenylosuccinate binding, and to identify the putative catalytic groups
S295A
mutant to probe the role of S295 in the catalytic mechanism
A219V
-
site-directed mutagenesis, inactive mutant
A260GfsX24
-
the mutation is associated with ADSL deficiency
D422Y
-
mutant without enzyme activity
D87E
the mutation is associated with ADSL deficiency and shows 91% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
E376D
the mutation is associated with ADSL deficiency and shows 49% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
E80D
the mutation is associated with ADSL deficiency and shows 102% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
E80D/D87E
-
australian patient with autism
K246E
the mutation is associated with adenylosuccinate lyase deficiency, the Vmax for the K246E mutant enzyme is about 2% that of the wild type enzyme, K246E exists mainly as dimer or monomer
L423V
-
mutant without enzyme activity
P100A/D422Y
-
the mutation leads to a defective enzyme which is inhibited by micromolar concentrations of trans-4-hydroxy-2-nonenal
P110A/D422Y
-
heat sensitive mutant
R141W
-
thermostable mutant with decreased activity
R149G
-
the mutation is associated with ADSL deficiency
R190Q
the mutation is associated with ADSL deficiency and shows 119% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
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
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
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
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
S395R
-
thermostable mutant with decreased activity
S413P
-
the mutation leads to structural instability of the mutant enzyme, this instability lowers the enzyme level in lymphocytes. The mutation segregates with mental retardation in the affected family
S438P
-
heat sensitive mutant without enzyme activity
T450S
the mutation is associated with ADSL deficiency and shows 68% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
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
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
D69E
-
mutant with differences in thermal stability, catalytic activity and substrate binding
D69E
-
mutant exibits an increase in its pK2
D69N
-
mutant exibits a decrease in its pK2
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
D215H
-
naturally occuring mutation, two homozygous and two compound heterozygous mutant variants
D215H
the mutation is associated with ADSL deficiency and shows 92% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
D268H
-
naturally occuring mutation, two homozygous and two compound heterozygous mutant variants
D268H
the mutation is associated with ADSL deficiency and shows 20% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
D430N
-
mutant without enzyme activity
D430N
the mutation is associated with ADSL deficiency and shows 151% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
I351T
-
naturally occuring mutation, two homozygous and two compound heterozygous mutant variants
I351T
the mutation is associated with ADSL deficiency and shows 151% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
L311V
the mutation is associated with adenylosuccinate lyase deficiency, the Vmax for the L311V mutant enzyme is 72% about 2% that of the wild type enzyme
L311V
-
about 90% of wild-type actitivy
R194C
the mutation is associated with adenylosuccinate lyase deficiency,Vmax (at 25°C) for R194C is comparable to that of wild type, R194C is rapidly inactivated at 60°C
R194C
the mutation is associated with ADSL deficiency and shows 101% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
R194C
-
about 100% of wild-type actitivy
R303C
-
thermostable mutant with decreased activity
R303C
-
naturally occuring mutation, causing the mild form, Type II, of enzyme deficiency, the mutant shows reduced activity compared to the wild-type enzyme, mutation R303C increases the KM value
R303C
naturally occuring type II mutation, observed as a homozygous mutation in two unrelated patients, the mutant shows reduced activity compared to the wild-type enzyme, KM values of R303C enzyme mutant increase 4fold for phosphoribosylsuccinyl-aminoimidazole carboxamide compared to that of wild-type enzyme, for succinyladenosine monophosphate the change is almost negligible, substrate binding of the enzyme is latered compared to the wild-type
R396C
the mutation is associated with adenylosuccinate lyase deficiency the Vmax for the R396C mutant enzyme is about 16% that of the wild type enzyme
R396C
the mutation is associated with ADSL deficiency and shows 32% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
R396C
-
about 20% of wild-type actitivy
R396H
the mutation is associated with adenylosuccinate lyase deficiency, Vmax (at 25°C) for R194C is considerably reduced and affinity for adenylosuccinate is retained
R396H
-
about 10% of wild-type actitivy
R426H
-
mutant without enzyme activity
R426H
-
naturally occuring mutation, two homozygous and two compound heterozygous mutant variants
R426H
the mutation is associated with ADSL deficiency and shows 89% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
R426H
-
naturally occuring mutation, causing the severe form, Type I, of enzyme deficiency, the mutant shows reduced activity compared to the wild-type enzyme, mutation R426H reduces the KM value
S23R
-
naturally occuring mutation, two homozygous and two compound heterozygous mutant variants
S23R
the mutation is associated with ADSL deficiency and shows 108% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
T242I
-
naturally occuring mutation, two homozygous and two compound heterozygous mutant variants
T242I
the mutation is associated with ADSL deficiency and shows 108% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
Y114H
-
naturally occuring mutation, two homozygous and two compound heterozygous mutant variants
Y114H
the mutation is associated with ADSL deficiency and shows 37% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme
additional information
-
the review gives an overview of the characteristics of patients with ADSL deficiency in dependence of amino acid changes
additional information
enzyme deficiency due to homozygous missense mutation T674C leading to the amino acid exchange M225T in the exon 6 of the ADSL gene causes a phenotype with global developmental delay, motor apraxia, severe speech deficits, seizures and behavioural features, which combines excessive laughter, a very happy disposition, hyperactivity, a short attention span, the mouthing of objects, tantrums and stereotyped movements that give a behavioural profile mimicking Angelman syndrome, the patients have an increased succinyladenosine/5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide ratio of 1.6 compared to wild-type humans, overview
additional information
-
enzyme deficiency due to homozygous missense mutation T674C leading to the amino acid exchange M225T in the exon 6 of the ADSL gene causes a phenotype with global developmental delay, motor apraxia, severe speech deficits, seizures and behavioural features, which combines excessive laughter, a very happy disposition, hyperactivity, a short attention span, the mouthing of objects, tantrums and stereotyped movements that give a behavioural profile mimicking Angelman syndrome, the patients have an increased succinyladenosine/5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide ratio of 1.6 compared to wild-type humans, overview
additional information
-
genotype is related to severity of the mental retardation phenotype, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ebbole, D.J.; Zalkin, H.
Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis
J. Biol. Chem.
262
8274-8287
1987
Bacillus subtilis
brenda
Porter, D.J.T.; Rudie, N.G.; Bright, H.J.
Nitro analogs of substrates for adenylosuccinate synthetase and adenylosuccinate lyase
Arch. Biochem. Biophys.
225
157-163
1983
Saccharomyces cerevisiae
brenda
Spector, T.; Jones, T.E.; Elion, G.B.
Specificity of adenylosuccinate synthetase and adenylosuccinate lyase from Leishmania donovani. Selective amination of an antiprotozoal agent
J. Biol. Chem.
254
8422-8426
1979
Leishmania donovani
brenda
Casey, P.J.; Lowenstein, J.M.
Purification of adenylosuccinate lyase from rat skeletal muscle by a novel affinity column. Stabilization of the enzyme, and effects of anions and fluoro analogues of the substrate
Biochem. J.
246
263-269
1987
Rattus norvegicus
brenda
Casey, P.J.; Abeles, R.H.; Lowenstein, J.M.
Metabolism of threo-beta-fluoroaspartate by H4 cells. Inhibition of adenylosuccinate lyase by fluoro analogs of its substrates
J. Biol. Chem.
261
13637-13642
1986
Rattus norvegicus
brenda
Pinto, R.M.; Faraldo, A.; Fernandez, A.; Canales, J.; Sillero, A.; Sillero, M.A.G.
Adenylosuccinate lyase from Artemia embryos. Purification and properties
J. Biol. Chem.
258
12513-12519
1983
Artemia sp.
brenda
Woodward, D.O.
Adenylosuccinate AMP-lyase (Neurospora crassa)
Methods Enzymol.
11
202-207
1978
Neurospora crassa
brenda
Brand, L.M.; Lowenstein, J.M.
Effect of diet on adenylosuccinase activity in various organs of rat and chicken
J. Biol. Chem.
253
6872-6878
1978
Gallus gallus, Rattus norvegicus
brenda
Brand, L.M.; Lowenstein, J.M.
Inhibition of adenylosuccinase by adenylophosphonopropionate and related compounds
Biochemistry
17
1365-1370
1978
Rattus norvegicus
brenda
Spector, T.
Mammalian adenylosuccinate lyase. Participation in the conversion of 2 -dIMP and beta-D-arabinosyl-IMP to adenine nucleotides
Biochim. Biophys. Acta
481
741-745
1977
Mus musculus, Rattus norvegicus
brenda
Carter, C.E.; Cohen, L.H.
The preparation and properties of adenylosuccinase and adenylosuccinic acid
J. Biol. Chem.
222
17-30
1956
Saccharomyces cerevisiae
brenda
Mashall, V.M.; Coppel, R.L.
Characterisation of the gene encoding adenylosuccinate lyase of Plasmodium falciparum
Mol. Biochem. Parasitol.
88
237-241
1997
Plasmodium falciparum
brenda
Redinbo, M.R.; Eide, S.M.; Stone, R.L.; Dixon, J.E.; Yeates, T.O.
Crystallization and preliminary structural analysis of Bacillus subtilis adenylosuccinate lyase, an enzyme implicated in infantile autism
Protein Sci.
5
786-788
1996
Bacillus subtilis
brenda
Stone, R.L.; Zalkin, H.; Dixon, J.E.
Expression, purification, and kinetic characterization of recombinant human adenylosuccinate lyase
J. Biol. Chem.
268
19710-19716
1993
Homo sapiens
brenda
Barshop, B.A.; Alberts, A.S.; Gruber, H.E.
Kinetic studies of mutant human adenylosuccinase
Biochim. Biophys. Acta
999
19-23
1989
Homo sapiens
brenda
Hartgers, W.A.; de Boer, R.F.; Wanner, M.J.; Koomen, G.J.
A potential suicide inhibitor of adenylosuccinate lyase
Nucleosides Nucleotides
11
1325-1332
1992
Saccharomyces cerevisiae
-
brenda
Nair, V.; Sells, T.B.
Interpretation of the roles of adenylosuccinate lyase and of AMP deaminase in the anti-HIV activity of 2 ,3 -dideoxyadenosine and 2 ,3 -dideoxyinosine
Biochim. Biophys. Acta
1119
201-204
1992
Saccharomyces cerevisiae
brenda
Crifo, C.; Lomonte, A.; Salerno, C.
Inhibition of adenylosuccinate lyase by 2,3 -acyclic substrate analogs
Adv. Exp. Med. Biol.
431
245-248
1998
Homo sapiens
brenda
Van den Bergh, F.; Vincent, M.F.; Jaeken, J.; van den Berghe, G.
Radiochemical assay of adenylosuccinase: demonstration of parallel loss of activity toward both adenylosuccinate and succinylaminoimidazole carboxamide ribotide in liver of patients with the enzyme defect
Anal. Biochem.
193
287-291
1991
Homo sapiens
brenda
Shaw, G.; Thomas, P.S.; Patey, C.A.H.; Thomas, S.E.
Purines, pyrimidines, and imidazoles. Part 50. Inhibition and adenylosuccinate AMP-lyase No. 4.3.2.2. by derivatives of N-(5-amino-1-beta-D-ribofuranosylimidazole-4-carbonyl)-L-aspartic acid 5'-phosphate (SAICAR) and virazole 5'-phosphate
J. Chem. Soc. Perkin Trans.
1
1415-1424
1979
Saccharomyces cerevisiae
-
brenda
Stone, R.L.; Aimi, J.; Barshop, B.A.; Jaeken, J.; van den Berghe, G.; Zalkin, H.; Dixon, J.E.
A mutation in adenylosuccinate lyase associated with mental retardation and autistic features
Nature Genet.
1
59-63
1992
Homo sapiens
brenda
Segall, M.L.; Colman, R.F.
Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis
Biochemistry
43
7391-7402
2004
Bacillus subtilis
brenda
Crifo, C.; Siems, W.; Soro, S.; Salerno, C.
Inhibition of defective adenylosuccinate lyase by HNE: a neurological disease that may be affected by oxidative stress
Biofactors
24
131-136
2005
Bacillus subtilis, Homo sapiens, Pyrobaculum aerophilum, Thermotoga maritima
brenda
Sivendran, S.; Patterson, D.; Spiegel, E.; McGown, I.; Cowley, D.; Colman, R.F.
Two novel mutant human adenylosuccinate lyases (ASLs) associated with autism and characterization of the equivalent mutant Bacillus subtilis ASL
J. Biol. Chem.
279
53789-53797
2004
Bacillus subtilis, Homo sapiens
brenda
Tsai, M.; Koo, J.; Yip, P.; Colman, R.F.; Segall, M.L.; Howell, P.L.
Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism
J. Mol. Biol.
370
541-554
2007
Escherichia coli (P0AB89), Escherichia coli
brenda
Spiegel, E.K.; Colman, R.F.; Patterson, D.
Adenylosuccinate lyase deficiency
Mol. Genet. Metab.
89
19-31
2006
Bacillus subtilis, Homo sapiens, Mus musculus, Pyrobaculum aerophilum, Thermotoga maritima (Q9X0I0)
brenda
Lee, P.; Colman, R.F.
Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyase
Protein Expr. Purif.
51
227-234
2007
Homo sapiens
brenda
Sivendran, S.; Segall, M.L.; Rancy, P.C.; Colman, R.F.
Effect of Asp69 and Arg310 on the pK of His68, a key catalytic residue of adenylosuccinate lyase
Protein Sci.
16
1700-1707
2007
Bacillus subtilis
brenda
Segall, M.L.; Cashman, M.A.; Colman, R.F.
Important roles of hydroxylic amino acid residues in the function of Bacillus subtilis adenylosuccinate lyase
Protein Sci.
16
441-448
2007
Bacillus subtilis
brenda
De Zoysa Ariyananda, L.; Colman, R.F.
Evaluation of types of interactions in subunit association in Bacillus subtilis adenylosuccinate lyase
Biochemistry
47
2923-2934
2008
Bacillus subtilis (P12047), Bacillus subtilis
brenda
Bulusu, V.; Srinivasan, B.; Bopanna, M.P.; Balaram, H.
Elucidation of the substrate specificity, kinetic and catalytic mechanism of adenylosuccinate lyase from Plasmodium falciparum
Biochim. Biophys. Acta
1794
642-654
2008
Plasmodium falciparum (O15918), Plasmodium falciparum
brenda
Gitiaux, C.; Ceballos-Picot, I.; Marie, S.; Valayannopoulos, V.; Rio, M.; Verrieres, S.; Benoist, J.F.; Vincent, M.F.; Desguerre, I.; Bahi-Buisson, N.
Misleading behavioural phenotype with adenylosuccinate lyase deficiency
Eur. J. Hum. Genet.
17
133-136
2009
Homo sapiens (P30566), Homo sapiens
brenda
Lopez, J.M.
Is ZMP the toxic metabolite in Lesch-Nyhan disease?
Med. Hypotheses
71
657-663
2008
Homo sapiens
brenda
Jurecka, A.; Zikanova, M.; Tylki-Szymanska, A.; Krijt, J.; Bogdanska, A; Gradowska, W.; Mullerova, K.; Sykut-Cegielska, J.; Kmoch, S.; Pronicka, E.
Clinical, biochemical and molecular findings in seven Polish patients with adenylosuccinate lyase deficiency
Mol. Genet. Metab.
94
435-442
2008
Homo sapiens
brenda
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
Protein Sci.
17
1162-1174
2008
Bacillus subtilis, Homo sapiens (P30566), Homo sapiens
brenda
Jurecka, A.; Tylki-Szymanska, A.; Zikanova, M.; Krijt, J.; Kmoch, S.
D-Ribose therapy in four Polish patients with adenylosuccinate lyase deficiency: absence of positive effect
J. Inherit. Metab. Dis.
31
S329-332
2008
Homo sapiens
brenda
Kozlov, G.; Nguyen, L.; Pearsall, J.; Gehring, K.
The structure of phosphate-bound Escherichia coli adenylosuccinate lyase identifies His171 as a catalytic acid
Acta Crystallogr. Sect. F
65
857-861
2009
Escherichia coli (Q8X737), Escherichia coli
brenda
Ariyananda, L.d.e..Z.; Lee, P.; Antonopoulos, C.; Colman, R.F.
Biochemical and biophysical analysis of five disease-associated human adenylosuccinate lyase mutants
Biochemistry
48
5291-5302
2009
Homo sapiens (P30566), Homo sapiens
brenda
Mierzewska, H.; Schmidt-Sidor, B.; Jurkiewicz, E.; Bogdanska, A.; Kusmierska, K.; Stepien, T.
Severe encephalopathy with brain atrophy and hypomyelination due to adenylosuccinate lyase deficiency--MRI, clinical, biochemical and neuropathological findings of Polish patients
Folia Neuropathol.
47
314-320
2009
Homo sapiens
brenda
Zikanova, M.; Skopova, V.; Hnizda, A.; Krijt, J.; Kmoch, S.
Biochemical and structural analysis of 14 mutant ADSL enzyme complexes and correlation to phenotypic heterogeneity of adenylosuccinate lyase deficiency
Hum. Mutat.
31
445-455
2010
Homo sapiens (P30566), Homo sapiens
brenda
Chen, B.C.; McGown, I.N.; Thong, M.K.; Pitt, J.; Yunus, Z.M.; Khoo, T.B.; Ngu, L.H.; Duley, J.A.
Adenylosuccinate lyase deficiency in a Malaysian patient, with novel adenylosuccinate lyase gene mutations
J. Inherit. Metab. Dis.
33
S159-162
2010
Homo sapiens
brenda
Chauhan, P.S.; Nautiyal, C.S.
The purB gene controls rhizosphere colonization by Pantoea agglomerans
Lett. Appl. Microbiol.
50
205-210
2010
Pantoea agglomerans
brenda
Camici, M.; Micheli, V.; Ipata, P.L.; Tozzi, M.G.
Pediatric neurological syndromes and inborn errors of purine metabolism
Neurochem. Int.
56
367-378
2010
Homo sapiens
brenda
Henneke, M.; Dreha-Kulaczewski, S.; Brockmann, K.; van der Graaf, M.; Willemsen, M.A.; Engelke, U.; Dechent, P.; Heerschap, A.; Helms, G.; Wevers, R.A.; Gaertner, J.
In vivo proton MR spectroscopy findings specific for adenylosuccinate lyase deficiency
NMR Biomed.
23
441-445
2010
Homo sapiens
brenda
Fyfe, P.K.; Dawson, A.; Hutchison, M.T.; Cameron, S.; Hunter, W.N.
Structure of Staphylococcus aureus adenylosuccinate lyase (PurB) and assessment of its potential as a target for structure-based inhibitor discovery
Acta Crystallogr. Sect. D
66
881-888
2010
Staphylococcus aureus (Q7A0G9), Staphylococcus aureus
brenda
De Zoysa Ariyananda, L.; Antonopoulos, C.; Currier, J.; Colman, R.F.
In vitro hybridization and separation of hybrids of human adenylosuccinate lyase from wild-type and disease-associated mutant enzymes
Biochemistry
50
1336-1346
2011
Homo sapiens
brenda
Yuan, T.; Gu, J.R.; Gu, W.B.; Wu, J.; Ge, S.R.; Xu, H.
Molecular cloning, characterization and expression analysis of adenylosuccinate lyase gene in grass carp (Ctenopharyngodon idella)
Mol. Biol. Rep.
38
2059-2065
2011
Ctenopharyngodon idella (B2LS18), Ctenopharyngodon idella
brenda
Toth, E.A.; Worby, C.; Dixon, J.E.; Goedken, E.R.; Marqusee, S.; Yeates, T.O.
The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds
J. Mol. Biol.
301
433-450
2000
Pyrobaculum aerophilum (Q8ZY28), Pyrobaculum aerophilum, Pyrobaculum aerophilum DSM 7523 (Q8ZY28)
brenda
Ray, S.P.; Deaton, M.K.; Capodagli, G.C.; Calkins, L.A.; Sawle, L.; Ghosh, K.; Patterson, D.; Pegan, S.D.
Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation
Biochemistry
51
6701-6713
2012
Homo sapiens (P30566), Homo sapiens
brenda
Ray, S.P.; Duval, N.; Wilkinson, T.G.; Shaheen, S.E.; Ghosh, K.; Patterson, D.
Inherent properties of adenylosuccinate lyase could explain S-Ado/SAICAr ratio due to homozygous R426H and R303C mutations
Biochim. Biophys. Acta
1834
1545-1553
2013
Homo sapiens
brenda
Banerjee, S.; Agrawal, M.J.; Mishra, D.; Sharan, S.; Balaram, H.; Savithri, H.S.; Murthy, M.R.
Structural and kinetic studies on adenylosuccinate lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzyme
FEBS J.
281
1642-1658
2014
Mycobacterium tuberculosis, Mycolicibacterium smegmatis (A0R4I6)
brenda
Bierau, J.; Pooters, I.N.; Visser, D.; Bakker, J.A.
An HPLC-based assay of adenylosuccinate lyase in erythrocytes
Nucleosides Nucleotides Nucleic Acids
30
908-917
2011
Homo sapiens
brenda
Stuer-Lauridsen, B.; Nygaard, P.
Purine salvage in two halophilic archaea: characterization of salvage pathways and isolation of mutants resistant to purine analogs
J. Bacteriol.
180
457-463
1998
Halobacterium salinarum, Haloferax volcanii
brenda
Gooding, J.R.; Jensen, M.V.; Dai, X.; Wenner, B.R.; Lu, D.; Arumugam, R.; Ferdaoussi, M.; MacDonald, P.E.; Newgard, C.B.
Adenylosuccinate is an insulin secretagogue derived from glucose-induced purine metabolism
Cell Rep.
13
157-167
2015
Rattus norvegicus (D3ZW08)
brenda
Galina, L.; Dalberto, P.; Martinelli, L.; Roth, C.; Pinto, A.; Villela, A.; Bizarro, C.; MacHado, P.; Timmers, L.; De Souza, O.; De Carvalho Filho, E.; Basso, L.; Santos, D.
Biochemical, thermodynamic and structural studies of recombinant homotetrameric adenylosuccinate lyase from Leishmania braziliensis
RSC Adv.
7
54347-54360
2017
Leishmania braziliensis (A4H3W5)
-
brenda