Adenylosuccinate Lyase: An enzyme that, in the course of purine ribonucleotide biosynthesis, catalyzes the conversion of 5'-phosphoribosyl-4-(N-succinocarboxamide)-5-aminoimidazole to 5'-phosphoribosyl-4-carboxamide-5-aminoimidazole and the conversion of adenylosuccinic acid to AMP. EC 4.3.2.2.Adenylosuccinate Synthase: A carbon-nitrogen ligase. During purine ribonucleotide biosynthesis, this enzyme catalyzes the synthesis of adenylosuccinate from GTP; IMP; and aspartate with the formation of orthophosphate and GDP. EC 6.3.4.4.Purine-Pyrimidine Metabolism, Inborn ErrorsLyases: A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.Aminoimidazole Carboxamide: An imidazole derivative which is a metabolite of the antineoplastic agents BIC and DIC. By itself, or as the ribonucleotide, it is used as a condensation agent in the preparation of nucleosides and nucleotides. Compounded with orotic acid, it is used to treat liver diseases.Purines: A series of heterocyclic compounds that are variously substituted in nature and are known also as purine bases. They include ADENINE and GUANINE, constituents of nucleic acids, as well as many alkaloids such as CAFFEINE and THEOPHYLLINE. Uric acid is the metabolic end product of purine metabolism.Inosine Monophosphate: Inosine 5'-Monophosphate. A purine nucleotide which has hypoxanthine as the base and one phosphate group esterified to the sugar moiety.Ribonucleotides: Nucleotides in which the purine or pyrimidine base is combined with ribose. (Dorland, 28th ed)Adenosine Monophosphate: Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position.Thermotoga maritima: A rod-shaped bacterium surrounded by a sheath-like structure which protrudes balloon-like beyond the ends of the cell. It is thermophilic, with growth occurring at temperatures as high as 90 degrees C. It is isolated from geothermally heated marine sediments or hot springs. (From Bergey's Manual of Determinative Bacteriology, 9th ed)Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.Mutation, Missense: A mutation in which a codon is mutated to one directing the incorporation of a different amino acid. This substitution may result in an inactive or unstable product. (From A Dictionary of Genetics, King & Stansfield, 5th ed)Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Kinetics: The rate dynamics in chemical or physical systems.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
(1/51) Capillary electrophoresis for detection of inherited disorders of purine and pyrimidine metabolism.

BACKGROUND: Measurement of purine and pyrimidine metabolites presents complex problems for separations currently performed by HPLC and thin-layer chromatography in clinical practice. We developed a novel capillary electrophoresis method for this purpose. METHODS: Separations were performed in 60 mmol/L borate-2-amino-2-methyl-1-propanol-80 mmol/L sodium dodecyl sulfate (pH 9.6) at 35 degrees C. RESULTS: The conditions reported allowed separation of all diagnostic metabolites from major urinary constituents in an analysis time of 3 min and with a separation efficiency of 220 000 theoretical plates/m. The clinically important metabolites were detectable at concentrations of 0.85-4.28 micromol/L. The method was linear over the range 5-500 micromol/L (r >0.99). The within-run and intra- and interday imprecision (CV) was <5%. Characteristic abnormalities were detected in the electropherograms of urine samples from patients with purine and pyrimidine enzyme deficiencies. We provide the electrophoretic and spectral characteristics of many intermediates in purine and pyrimidine metabolism and describe common artifacts from medication and ultraviolet-absorbing compounds. CONCLUSION: Capillary electrophoresis is a valuable screening tool in the detection of inborn errors of purine and pyrimidine metabolism.  (+info)

(2/51) The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway.

BACKGROUND: Adenylosuccinate lyase is an enzyme that plays a critical role in both cellular replication and metabolism via its action in the de novo purine biosynthetic pathway. Adenylosuccinate lyase is the only enzyme in this pathway to catalyze two separate reactions, enabling it to participate in the addition of a nitrogen at two different positions in adenosine monophosphate. Both reactions catalyzed by adenylosuccinate lyase involve the beta-elimination of fumarate. Enzymes that catalyze this type of reaction belong to a superfamily, the members of which are homotetramers. Because adenylosuccinate lyase plays an integral part in maintaining proper cellular metabolism, mutations in the human enzyme can have severe clinical consequences, including mental retardation with autistic features. RESULTS: The 1.8 A crystal structure of adenylosuccinate lyase from Thermotoga maritima has been determined by multiwavelength anomalous dispersion using the selenomethionine-substituted enzyme. The fold of the monomer is reminiscent of other members of the beta-elimination superfamily. However, its active tetrameric form exhibits striking differences in active-site architecture and cleft size. CONCLUSIONS: This first structure of an adenylosuccinate lyase reveals that, along with the catalytic base (His141) and the catalytic acid (His68), Gln212 and Asn270 might play a vital role in catalysis by properly orienting the succinyl moiety of the substrates. We propose a model for the dual activity of adenylosuccinate lyase: a single 180 degrees bond rotation must occur in the substrate between the first and second enzymatic reactions. Modeling of the pathogenic human S413P mutation indicates that the mutation destabilizes the enzyme by disrupting the C-terminal extension.  (+info)

(3/51) Succinylpurinemic autism: increased sensitivity of defective adenylosuccinate lyase towards 4-hydroxy-2-nonenal.

We studied the effect of trans-4-hydroxy-2-nonenal on the wild-type human adenylosuccinate lyase and on the enzyme from a patient compound-heterozygous for two missense mutations (P75A/D397Y; McKusick 103050.0003/103050.0004). Both the enzymes were inhibited by 10-50 microM trans-4-hydroxy-2-nonenal in a concentration-dependent manner by means of a mixed-type co-operative mechanism. A significantly stronger inhibition was noticed in the presence of the defective enzyme. Nonanal and trans-2,3-nonenal inhibited the enzymes to a less extent and at about 10-times higher concentrations. Hydroxylamine reversed the inhibition by trans-4-hydroxy-2-nonenal, trans-2,3-nonenal or nonanal in the case of the wild-type enzyme, but it was ineffective to reverse the inhibition by trans-4-hydroxy-2-nonenal on the defective enzyme. Dithiothreitol slightly decreased the inhibition exerted by trans-4-hydroxy-2-nonenal on both the wild-type and the defective adenylosuccinate lyase, while it did not produce practically any change in the presence of trans-2,3-nonenal or nonanal.  (+info)

(4/51) Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients.

Adenylosuccinate lyase (ADSL) is a bifunctional enzyme acting in de novo purine synthesis and purine nucleotide recycling. ADSL deficiency is a selectively neuronopathic disorder with psychomotor retardation and epilepsy as leading traits. Both dephosphorylated enzyme substrates, succinylaminoimidazole-carboxamide riboside (SAICAr) and succinyladenosine (S-Ado), accumulate in the cerebrospinal fluid (CSF) of affected individuals with S-Ado/SAICAr concentration ratios proportional to the phenotype severity. We studied the disorder at various levels in a group of six patients with ADSL deficiency. We identified the complete ADSL cDNA and its alternatively spliced isoform resulting from exon 12 skipping. Both mRNA isoforms were expressed in all the tissues studied with the non-spliced form 10-fold more abundant. Both cDNAs were expressed in Escherichia coli and functionally characterized at the protein level. The results showed only the unspliced ADSL to be active. The gene consists of 13 exons spanning 23 kb. The promotor region shows typical features of the housekeeping gene. Eight mutations were identified in a group of six patients. The expression studies of the mutant proteins carried out in an attempt to study genotype-phenotype correlation showed that the level of residual enzyme activity correlates with the severity of the clinical phenotype. All the mutant enzymes studied in vitro displayed a proportional decrease in activity against both of their substrates. However, this was not concordant with strikingly different concentration ratios in the CSF of individual patients. This suggests either different in vivo enzyme activities against each of the substrates and/or their different turnover across the CSF-blood barrier, which may be decisive in determining disease severity.  (+info)

(5/51) Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency.

Adenylosuccinate lyase (ADSL) deficiency (MIM 103050) is an autosomal recessive inborn error of purine synthesis characterized by the accumulation in body fluids of succinylaminoimidazolecarboxamide (SAICA) riboside and succinyladenosine (S-Ado), the dephosphorylated derivatives of the two substrates of the enzyme. Because ADSL-deficient patients display widely variable degrees of psychomotor retardation, we have expressed eight mutated ADSL enzymes as thioredoxin fusions and compared their properties with the clinical and biochemical characteristics of 10 patients. Three expressed mutated ADSL enzymes (M26L, R426H and T450S) were thermolabile, four (A2V, R141W, R303C and S395R) were thermostable and one (del206-218), was inactive. Thermolabile mutations decreased activities with SAICA ribotide (SAICAR) and adenylosuccinate (S-AMP) in parallel, or more with SAICAR than with S-AMP. Patients homozygous for one of these mutations, R426H, displayed similarly decreased ADSL activities in their fibroblasts, S-Ado:SAICA riboside ratios of approximately 1 in their cerebrospinal fluid and were profoundly retarded. With the exception of A2V, thermostable mutations decreased activity with S-AMP to a much more marked extent than with SAICAR. Two unrelated patients homozygous for one of the thermostable mutations, R303C, also displayed a much more marked decrease in the activity of fibroblast ADSL with S-AMP than with SAICAR, had S-Ado:SAICA riboside ratios between 3 and 4 in their cerebrospinal fluid and were mildly retarded. These results suggest that, in some cases, the genetic lesion of ADSL determines the ratio of its activities with S-AMP versus SAICAR, which in turn defines the S-Ado:SAICA riboside ratio and the patients' mental status.  (+info)

(6/51) Mutation of a nuclear respiratory factor 2 binding site in the 5' untranslated region of the ADSL gene in three patients with adenylosuccinate lyase deficiency.

Adenylosuccinate lyase (ADSL; also called "adenylosuccinase") catalyzes two steps in the synthesis of purine nucleotides: (1) the conversion of succinylaminoimidazolecarboxamide ribotide into aminoimidazolecarboxamide ribotide and (2) the conversion of adenylosuccinate into adenosine monophosphate. ADSL deficiency, a recessively inherited disorder, causes variable-but most often severe-mental retardation, frequently accompanied by epilepsy and/or autism. It is characterized by the accumulation, in body fluids, of succinylaminoimidazolecarboxamide riboside and succinyladenosine, the dephosphorylated derivatives of the two substrates of the enzyme. Analysis of the ADSL gene of three unrelated patients with ADSL deficiency, in whom one of the ADSL alleles displayed a normal coding sequence, revealed a -49T-->C mutation in the 5' untranslated region of this allele. Measurements of the amount of mRNA transcribed from the latter allele showed that it was reduced to approximately 33% of that transcribed from the alleles mutated in their coding sequence. Further investigations showed that the -49T-->C mutation provokes a reduction to 25% of wild-type control of promoter function, as evaluated by luciferase activity and mRNA level in transfection experiments. The mutation also affects the binding of nuclear respiratory factor 2 (NRF-2), a known activator of transcription, as assessed by gel-shift studies. Our findings indicate that a mutation of a regulatory region of the ADSL gene might be an unusually frequent cause of ADSL deficiency, and they suggest a role for NRF-2 in the gene regulation of the purine biosynthetic pathway.  (+info)

(7/51) Splicing graphs and EST assembly problem.

MOTIVATION: The traditional approach to annotate alternative splicing is to investigate every splicing variant of the gene in a case-by-case fashion. This approach, while useful, has some serious shortcomings. Recent studies indicate that alternative splicing is more frequent than previously thought and some genes may produce tens of thousands of different transcripts. A list of alternatively spliced variants for such genes would be difficult to build and hard to analyse. Moreover, such a list does not show the relationships between different transcripts and does not show the overall structure of all transcripts. A better approach would be to represent all splicing variants for a given gene in a way that captures the relationships between different splicing variants. RESULTS: We introduce the notion of the splicing graph that is a natural and convenient representation of all splicing variants. The key difference with the existing approaches is that we abandon the linear (sequence) representation of each transcript and replace it with a graph representation where each transcript corresponds to a path in the graph. We further design an algorithm to assemble EST reads into the splicing graph rather than assembling them into each splicing variant in a case-by-case fashion.  (+info)

(8/51) The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human adenylosuccinate lyase deficiencies.

Adenylosuccinate lyase is a homotetramer that catalyzes two discrete reactions in the de novo synthesis of purines: the cleavage of adenylosuccinate and succinylaminoimidazole carboxamide ribotide (SAICAR). Several point mutations in the gene encoding the enzyme have been implicated in human disease. Bacillus subtilis adenylosuccinate lyase was used as a model system in which mutations were constructed corresponding to those mutations associated with severe human adenylosuccinate lyase deficiency. Site-directed mutagenesis was utilized to construct amino acid substitutions in B. subtilis adenylosuccinate lyase; Met(10), Ile(123), and Thr(367) were replaced by Leu, Trp, and Arg, respectively, and the altered enzymes were expressed in Escherichia coli. These purified enzymes containing amino acid substitutions were found to have substantial catalytic activity and exhibit relatively small changes in their kinetic parameters. The major deviations from the wild-type-like behavior were observed upon biophysical characterization. All of these enzymes with amino acid replacements are associated with marked thermal instability. I123W adenylosuccinate lyase exhibits notable changes in the circular dichroism spectra, and a native gel electrophoresis pattern indicative of some protein aggregation. T367R also exhibits alterations at the quarternary level, as reflected in native gel electrophoresis. Experimental results, combined with homology modeling, suggest that the altered enzymes are primarily structurally impaired. The enzyme instability was found to be lessened by subunit complementation with the wild-type enzyme, under mild conditions; these studies may have implications for the in vivo behavior of adenylosuccinate lyase in heterozygous patients. Residues Met(10), Ile(123), and Thr(367) appear to be located in regions of the enzyme important for maintaining the structural integrity required for a stable, functional enzyme.  (+info)

*  Adenylosuccinate lyase
... (or adenylosuccinase) is an enzyme that in humans is encoded by the ADSL gene. Adenylosuccinate lyase ... Mutated adenylosuccinate lyase (ASL) causes clinical disease in patients that is referred to as adenylosuccinate lyase ... "The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human adenylosuccinate lyase ... of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase ...
*  Adenylosuccinate lyase deficiency
Adenylosuccinate Adenylosuccinate lyase List of genetic disorders "Adenylosuccinase deficiency". rarediseases.info.nih.gov. ... and adenylosuccinate (S-AMP), the two substrates of adenylosuccinate lyase (ADSL), which catalyzes an important reaction in the ... Treatment of adenylosuccinate lyase deficiency can be done via epilepsy management with anticonvulsive drugs.Additionally the ... "Adenylosuccinate lyase deficiency - Conditions - GTR - NCBI". www.ncbi.nlm.nih.gov. Retrieved 22 December 2016. RESERVED, ...
*  Nucleotide
This step is catalyzed by adenylosuccinate lyase. Inosine monophosphate is converted to guanosine monophosphate by the ... First, GTP hydrolysis fuels the addition of aspartate to IMP by adenylosuccinate synthase, substituting the carbonyl oxygen for ... a nitrogen and forming the intermediate adenylosuccinate. Fumarate is then cleaved off forming adenosine monophosphate. ...
*  Bacillus subtilis
Adenylosuccinate lyase deficiency Extremophile Guthrie test Euzéby JP (2008). "Bacillus". List of Prokaryotic names with ...
*  Morpheein
... of a Mutant Bacillus subtilis Adenylosuccinate Lyase Equivalent to a Mutant Enzyme Found in Human Adenylosuccinate Lyase ... "Evaluation of Types of Interactions in Subunit Association in Bacillus subtilis Adenylosuccinate Lyase". Biochemistry. 47 (9): ...
*  Purine metabolism
GMP back into IMP adenylosuccinate synthase converts IMP to adenylosuccinate adenylosuccinate lyase converts adenylosuccinate ... CAIR + L-Aspartate + ATP → SAICAR + ADP + Pi The eight is catalyzed by adenylosuccinate lyase. SAICAR → AICAR + Fumarate The ...
*  Asli
... the Ethiopian male name Adenylosuccinate lyase. ...
*  GABPB2
... untranslated region of the ADSL gene in three patients with adenylosuccinate lyase deficiency". Am. J. Hum. Genet. 71 (1): 14- ...
*  Adenylosuccinate
... lyase deficiency Purine nucleotide cycle Figures 20.4 and 20.7 in Textbook of Biochemistry, with clinical ... Adenylosuccinate is an intermediate in the interconversion of purine nucleotides inosine monophosphate (IMP) and adenosine ... monophosphate (AMP). The enzyme adenylosuccinate synthase carries out the reaction by the addition of aspartate to IMP and ...
*  Fumarate lyase
Adenylosuccinase, EC 4.3.2.2 (adenylosuccinate lyase), which catalyzes the eighth step in the de novo biosynthesis of purines, ... Aspartate ammonia-lyase, EC 4.3.1.1 (aspartase), which catalyzes the reversible conversion of aspartate to fumarate and ammonia ... A number of enzymes, belonging to the lyase class, for which fumarate is a substrate, have been shown to share a short ... Delta-crystallin shares around 90% sequence identity with arginosuccinate lyase, showing that it is an example of a 'hijacked' ...
*  List of diseases (A)
... anemia due to Adenylosuccinate lyase deficiency Adie syndrome Adiposis dolorosa, aka Dercum's disease Adolescent benign focal ...
*  SAICA
... a molecule whose appearance is characteristic of the disease adenylosuccinate lyase deficiency Saica may refer to : Saica ( ...
*  Purine nucleotide cycle
Adenylosuccinate + GDP + Pi Finally, Adenylosuccinate is cleaved by the enzyme adenylosuccinate lyase to release fumarate and ... to sustain mitochondrial membrane potential during anoxic stress by utilizing fumarate produced by adenylosuccinate lyase as an ... NH4+ The second stage is the formation of adenylosuccinate from IMP and the amino acid aspartate, which is coupled to the ... regenerate the starting material of AMP: Adenylosuccinate → AMP + Fumarate A recent study conducted by Sridharan et al. (AJP ...
*  List of MeSH codes (D08)
... tyrosine phenol-lyase MeSH D08.811.520.232.300 --- amidine-lyases MeSH D08.811.520.232.300.200 --- adenylosuccinate lyase MeSH ... oxo-acid-lyases MeSH D08.811.520.224.600.200 --- anthranilate synthase MeSH D08.811.520.224.600.700 --- isocitrate lyase MeSH ... ethanolamine ammonia-lyase MeSH D08.811.520.232.400.500 --- histidine ammonia-lyase MeSH D08.811.520.232.400.600 --- l-serine ... lyase MeSH D08.811.520.241.300 --- hydro-lyases MeSH D08.811.520.241.300.050 --- aconitate hydratase MeSH D08.811.520.241. ...
*  List of EC numbers (EC 4)
... argininosuccinate lyase EC 4.3.2.2: adenylosuccinate lyase EC 4.3.2.3: ureidoglycolate lyase EC 4.3.2.4: purine imidazole-ring ... pectin lyase EC 4.2.2.11: poly(a-L-guluronate) lyase EC 4.2.2.12: xanthan lyase EC 4.2.2.13: exo-(1-4)-α-D-glucan lyase EC 4.2. ... pectate lyase EC 4.2.2.3: poly(b-D-mannuronate) lyase EC 4.2.2.4: chondroitin ABC lyase EC 4.2.2.5: chondroitin AC lyase EC 4.2 ... oligogalacturonide lyase EC 4.2.2.7: heparin lyase EC 4.2.2.8: heparin-sulfate lyase EC 4.2.2.9: pectate disaccharide-lyase EC ...
*  List of EC numbers (EC 6)
... lyase) ligase EC 6.2.1.23: dicarboxylate-CoA ligase EC 6.2.1.24: phytanate-CoA ligase EC 6.2.1.25: benzoate-CoA ligase EC 6.2. ... adenylosuccinate synthase EC 6.3.4.5: argininosuccinate synthase EC 6.3.4.6: urea carboxylase EC 6.3.4.7: ribose-5-phosphate- ...
Adenylosuccinate lyase definition | Drugs.com  Adenylosuccinate lyase definition | Drugs.com
Definition of adenylosuccinate lyase. Provided by Stedman's medical dictionary and Drugs.com. Includes medical terms and ... adenylosuccinate lyase. Pronunciation: ad′e-nil-ō-sŭk′sin-āt lī′ās ...
more infohttps://www.drugs.com/dict/adenylosuccinate-lyase.html
RCSB PDB 









- 1F1O: STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES Literature Report Page  RCSB PDB - 1F1O: STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES Literature Report Page
The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three ... ADENYLOSUCCINATE LYASE A 431 Bacillus subtilis EC#: 4.3.2.2 IUBMB Gene Name(s): purB purE BSU06440 ...
more infohttp://www.rcsb.org/pdb/explore/litView.do?structureId=1F1O
Mthe 1218 - Adenylosuccinate lyase - Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT) - Mthe 1218...  Mthe 1218 - Adenylosuccinate lyase - Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT) - Mthe 1218...
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.UniRule annotation. ,p>Information which has been generated by ... IPR019468. AdenyloSucc_lyase_C. IPR024083. Fumarase/histidase_N. IPR020557. Fumarate_lyase_CS. IPR000362. Fumarate_lyase_fam. ... IPR019468. AdenyloSucc_lyase_C. IPR024083. Fumarase/histidase_N. IPR020557. Fumarate_lyase_CS. IPR000362. Fumarate_lyase_fam. ... Adenylosuccinate lyase (Mthe_1218). This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is ...
more infohttp://www.uniprot.org/uniprot/A0B8H3
ADE13 (YLR359W) Result Summary | BioGRID  ADE13 (YLR359W) Result Summary | BioGRID
Adenylosuccinate Lyase; Catalyzes Two Steps In The 'de Novo' Purine Nucleotide Biosynthetic Pathway; Expression Is Repressed By ... Adenylosuccinate lyase; catalyzes two steps in the 'de novo' purine nucleotide biosynthetic pathway; expression is repressed by ...
more infohttps://thebiogrid.org/31620/table/saccharomyces-cerevisiae/ade13.html
ADE13 (YLR359W) Result Summary | BioGRID  ADE13 (YLR359W) Result Summary | BioGRID
Adenylosuccinate Lyase; Catalyzes Two Steps In The 'de Novo' Purine Nucleotide Biosynthetic Pathway; Expression Is Repressed By ... Adenylosuccinate lyase; catalyzes two steps in the 'de novo' purine nucleotide biosynthetic pathway; expression is repressed by ...
more infohttps://thebiogrid.org/31620/summary/saccharomyces-cerevisiae/ade13.html
Browse by Author - ePrints@IISc  Browse by Author - [email protected]
Structural and kinetic studies on adenylosuccinate lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide ...
more infohttp://eprints.iisc.ernet.in/view/people/Banerjee=3ASanchari=3A=3A.html
Adenylosuccinate lyase C-terminal (IPR019468) | InterPro | EMBL-EBI  Adenylosuccinate lyase C-terminal (IPR019468) | InterPro | EMBL-EBI
Adenylosuccinate lyase C-terminal (IPR019468). Short name: AdenyloSucc_lyase_C Overlapping homologous superfamilies *L- ... Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole- ... This entry represents the seven alpha-helical, C-terminal domain of adenylosuccinate lyase [PMID: 9274883]. It is also found in ... Adenylosuccinate lyase deficiency: the first identified polish patient.. Brain Dev. 29 600-2 2007 ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR019468
Adenylosuccinate lyase - Wikipedia  Adenylosuccinate lyase - Wikipedia
Adenylosuccinate lyase (or adenylosuccinase) is an enzyme that in humans is encoded by the ADSL gene. Adenylosuccinate lyase ... Mutated adenylosuccinate lyase (ASL) causes clinical disease in patients that is referred to as adenylosuccinate lyase ... "The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human adenylosuccinate lyase ... of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase ...
more infohttps://en.wikipedia.org/wiki/Adenylosuccinate_lyase
Adenylosuccinate lyase deficiency - Wikipedia  Adenylosuccinate lyase deficiency - Wikipedia
Adenylosuccinate Adenylosuccinate lyase List of genetic disorders "Adenylosuccinase deficiency". rarediseases.info.nih.gov. ... and adenylosuccinate (S-AMP), the two substrates of adenylosuccinate lyase (ADSL), which catalyzes an important reaction in the ... Treatment of adenylosuccinate lyase deficiency can be done via epilepsy management with anticonvulsive drugs.Additionally the ... "Adenylosuccinate lyase deficiency - Conditions - GTR - NCBI". www.ncbi.nlm.nih.gov. Retrieved 22 December 2016. RESERVED, ...
more infohttps://en.wikipedia.org/wiki/Adenylosuccinate_lyase_deficiency
Sequence Similarity 









- 1F1O: STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES Sequence Similarity Report Page  Sequence Similarity - 1F1O: STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES Sequence Similarity Report Page
The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three ... Adenylosuccinate lyase 1392 4.3.2.2 , Details 4 5HW2 1 A, B, C, D Adenylosuccinate lyase 263 4.3.2.2 , Details ... Adenylosuccinate lyase 263 4.3.2.2 , Details 3 2PFM 1 A, B ... ADENYLOSUCCINATE LYASE 13773 4.3.2.2 , Details 8 5XNZ 1 A CreD ... PROTEIN (ADENYLOSUCCINATE LYASE) 2336 4.3.2.2 , Details 2 4EEI 1 A, B ...
more infohttp://www.rcsb.org/pdb/explore/sequenceCluster.do?structureId=1F1O&entity=1&seqid=30
Ajs 4026 - Adenylosuccinate lyase - Acidovorax sp. (strain JS42) - Ajs 4026 gene & protein  Ajs 4026 - Adenylosuccinate lyase - Acidovorax sp. (strain JS42) - Ajs 4026 gene & protein
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.UniRule annotation. ,p>Information which has been generated by ... IPR000362. Fumarate_lyase_fam. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. IPR004769. Pur_lyase. IPR013539. PurB_ ... IPR000362. Fumarate_lyase_fam. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. IPR004769. Pur_lyase. IPR013539. PurB_ ... Adenylosuccinate lyase (Ajs_4026). This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself ...
more infohttp://www.uniprot.org/uniprot/A1WD05
ADSL elisa kit | Human Adenylosuccinate lyase (ADSL) ELISA Kit-YP 004341812.1  ADSL elisa kit | Human Adenylosuccinate lyase (ADSL) ELISA Kit-YP 004341812.1
Human Adenylosuccinate lyase (ADSL) ELISA Kit-YP_004341812.1 (MBS7236022) product datasheet at MyBioSource, ELISA Kits ... ADSL elisa kit :: Human Adenylosuccinate lyase (ADSL) ELISA Kit. Catalog #. MBS7236022 .mycenter { display: block; margin-left ... Kit for analyzing the presence of the Adenylosuccinate lyase (ADSL) ELISA Kit target analytes in biological samples. The ... Adenylosuccinate lyase (ADSL), ELISA Kit. ★Popular Item★ Also Known As Human Adenylosuccinate lyase (ADSL) ELISA Kit. ...
more infohttps://www.mybiosource.com/prods/ELISA-Kit/Human/Adenylosuccinate-lyase-ADSL/ADSL/datasheet.php?products_id=7236022
Gentaur Molecular :EIAab \ Adenylosuccinase,Adenylosuccinate lyase,Adl,Adsl,ASase,ASL,Mouse,Mus musculus \ EIAAB33171  Gentaur Molecular :EIAab \ Adenylosuccinase,Adenylosuccinate lyase,Adl,Adsl,ASase,ASL,Mouse,Mus musculus \ EIAAB33171
Adenylosuccinate lyase,Adl,Adsl,ASase,ASL,Mouse,Mus musculus \ EIAAB33171 for more molecular products just contact us ... Adenylosuccinate lyase,Adl,Adsl,ASase,ASL,Mouse,Mus musculus mus musculus murine Adenylosuccinase,Adenylosuccinate lyase,Adl, ... Adenylosuccinate lyase,Adl,Adsl,ASase,ASL,Mouse,Mus musculus. Related products : Adenylosuccinase,Adenylosuccinate lyase,Adl, ... Adenylosuccinate lyase,Adl,Adsl,ASase,ASL,Mouse,Mus musculus / Product Detail : EIAAB33171 Adenylosuccinase,Adenylosuccinate ...
more infohttp://www.antibody-antibodies.com/product2884507-search-Adenylosuccinase,Adenylosuccinate_lyase,Adl,Adsl,ASase,ASL,Mouse,Mus_musculus.html
Gentaur antibody-antibodies.com The Marketplace for Antibodies : Gln212, Asn270, and Arg301 are critical for catalysis by...  Gentaur antibody-antibodies.com The Marketplace for Antibodies : Gln212, Asn270, and Arg301 are critical for catalysis by...
... and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis. ... and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis. In adenylosuccinate lyase from Bacillus ... 15182182] Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis.. ... metC yjcJ BSU11880] Cystathionine beta-lyase MetC (CBL) (EC 4.4.1.13) (Beta-cystathionase MetC) (Cysteine lyase MetC) (Cysteine ...
more infohttps://www.antibody-antibodies.com/pubmed-PubMed=15182182-PubMedArticl.html
ADSL gene - Genetics Home Reference - NIH  ADSL gene - Genetics Home Reference - NIH
adenylosuccinate lyase. Enable Javascript to view the expand/collapse boxes.. Printable PDF Open All Close All ... OMIM: ADENYLOSUCCINATE LYASE. *. Ariyananda Lde Z, Lee P, Antonopoulos C, Colman RF. Biochemical and biophysical analysis of ... A reduction of adenylosuccinate lyase function, possibly due to a shortage of purinosomes, leads to buildup of SAICAR and SAMP ... Adenylosuccinate lyase and other enzymes involved in purine synthesis form a group of proteins (a protein complex) called the ...
more infohttps://ghr.nlm.nih.gov/gene/ADSL
Product Search for peptides and proteins: Novus Biologicals  Product Search for peptides and proteins: Novus Biologicals
Adenylosuccinate Lyase Deficiency (disorder) (2). *. Atrophy (2). *. Autistic Disorder (2). *. Cholangiocarcinoma (2) ...
more infohttps://www.novusbio.com/search?keywords=peptides%20and%20proteins&related_diseases=Encephalopathies&gene_symbol=ADSL
Enzyme Explorer Assay Library | Sigma-Aldrich  Enzyme Explorer Assay Library | Sigma-Aldrich
Adenylosuccinate Lyase 4.3.2.2. ADP-Ribosylcyclase none. Agarase 3.2.1.81. Alanine Aminopeptidase 3.4.11.14. ...
more infohttps://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/learning-center/assay-library.html
A - Genes - Genetics Home Reference - NIH  A - Genes - Genetics Home Reference - NIH
ADSL: adenylosuccinate lyase. *AFF2: AF4/FMR2 family member 2. *AFF4: AF4/FMR2 family member 4 ...
more infohttps://ghr.nlm.nih.gov/gene
Gene Ontology Classifications  Gene Ontology Classifications
adenylosuccinate lyase. MGI:103202 Go Annotations as Summary Text (Tabular View) (GO Graph). Automated description from the ... Orthologous to human ADSL (adenylosuccinate lyase).. Go Annotations in Tabular Form (Text View) (GO Graph) Filter annotations ... Predicted to have (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity ... Human ortholog(s) of this gene implicated in adenylosuccinase lyase deficiency. ...
more infohttp://www.informatics.jax.org/go/marker/MGI:103202
  • It was previously thought that the mechanism of action for adenylosuccinate lyase was a concerted catalysis where the hydrogen on the β-carbon (with respect to the leaving nitrogen) was abstracted by the catalytic base at the same time that the leaving nitrogen was protonated by the catalytic acid for E2 elimination. (wikipedia.org)