Adenylosuccinate Lyase
Adenylosuccinate Synthase
Purine-Pyrimidine Metabolism, Inborn Errors
Lyases
Aminoimidazole Carboxamide
Purines
Inosine Monophosphate
Ribonucleotides
Adenosine Monophosphate
Thermotoga maritima
Mutation, Missense
Molecular Sequence Data
Capillary electrophoresis for detection of inherited disorders of purine and pyrimidine metabolism. (1/51)
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)The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway. (2/51)
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)Succinylpurinemic autism: increased sensitivity of defective adenylosuccinate lyase towards 4-hydroxy-2-nonenal. (3/51)
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)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. (4/51)
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)Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency. (5/51)
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)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. (6/51)
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)Splicing graphs and EST assembly problem. (7/51)
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)The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human adenylosuccinate lyase deficiencies. (8/51)
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 is a crucial enzyme in the purine nucleotide biosynthesis pathway. Its primary function is to catalyze the conversion of adenylosuccinate into adenosine monophosphate (AMP) and fumarate in two consecutive steps. This enzyme plays an essential role in the metabolism of purines, which are vital components of DNA, RNA, and energy transfer molecules like ATP. Deficiency in this enzyme can lead to a rare genetic disorder known as Adenylosuccinase Deficiency or Adenylosuccinate Lyase Deficiency, characterized by neurological symptoms, developmental delays, and physical disabilities.
Adenylosuccinate synthase is a crucial enzyme in the purine nucleotide biosynthesis pathway. It catalyzes the reaction of inosine monophosphate (IMP) with aspartic acid to form adenylosuccinic acid, which is subsequently converted into adenosine monophosphate (AMP). This enzyme exists as two isoforms, Adenylosuccinate Synthase 1 (ADSS1) and Adenylosuccinate Synthase 2 (ADSS2), encoded by separate genes. ADSS1 is primarily expressed in the cytosol of various tissues, while ADSS2 is mitochondrial and has been implicated in cancer progression. Defects in ADSS1 are associated with a rare neurological disorder called adenylosuccinase deficiency.
Inborn errors of purine-pyrimidine metabolism refer to genetic disorders that result in dysfunctional enzymes involved in the metabolic pathways of purines and pyrimidines. These are essential components of nucleotides, which in turn are building blocks of DNA and RNA.
Inherited as autosomal recessive or X-linked recessive traits, these disorders can lead to an accumulation of toxic metabolites, a deficiency of necessary compounds, or both. Clinical features vary widely depending on the specific enzyme defect but may include neurologic symptoms, kidney problems, gout, and/or immunodeficiency.
Examples of such disorders include Lesch-Nyhan syndrome (deficiency of hypoxanthine-guanine phosphoribosyltransferase), adenosine deaminase deficiency (leading to severe combined immunodeficiency), and orotic aciduria (due to defects in pyrimidine metabolism). Early diagnosis and management are crucial to improve outcomes.
A lyase is a type of enzyme that catalyzes the breaking of various chemical bonds in a molecule, often resulting in the formation of two new molecules. Lyases differ from other types of enzymes, such as hydrolases and oxidoreductases, because they create double bonds or rings as part of their reaction mechanism.
In the context of medical terminology, lyases are not typically discussed on their own, but rather as a type of enzyme that can be involved in various biochemical reactions within the body. For example, certain lyases play a role in the metabolism of carbohydrates, lipids, and amino acids, among other molecules.
One specific medical application of lyase enzymes is in the diagnosis of certain genetic disorders. For instance, individuals with hereditary fructose intolerance (HFI) lack the enzyme aldolase B, which is a type of lyase that helps break down fructose in the liver. By measuring the activity of aldolase B in a patient's blood or tissue sample, doctors can diagnose HFI and recommend appropriate dietary restrictions to manage the condition.
Overall, while lyases are not a medical diagnosis or condition themselves, they play important roles in various biochemical processes within the body and can be useful in the diagnosis of certain genetic disorders.
Aminoimidazole carboxamide is a compound that is involved in the metabolic pathways of nucleotide synthesis in cells. It is also known as AICA ribonucleotide, and is a precursor to an important energy molecule in the body called adenosine triphosphate (ATP).
In medical terms, aminoimidazole carboxamide is sometimes used as a research tool to study cellular metabolism and has been investigated for its potential therapeutic use in various conditions such as neurodegenerative disorders and ischemia-reperfusion injury. However, it is not commonly used as a medication in clinical practice.
Purines are heterocyclic aromatic organic compounds that consist of a pyrimidine ring fused to an imidazole ring. They are fundamental components of nucleotides, which are the building blocks of DNA and RNA. In the body, purines can be synthesized endogenously or obtained through dietary sources such as meat, seafood, and certain vegetables.
Once purines are metabolized, they are broken down into uric acid, which is excreted by the kidneys. Elevated levels of uric acid in the body can lead to the formation of uric acid crystals, resulting in conditions such as gout or kidney stones. Therefore, maintaining a balanced intake of purine-rich foods and ensuring proper kidney function are essential for overall health.
Inosine monophosphate (IMP) is a nucleotide that plays a crucial role in the metabolic pathways of energy production and purine synthesis in cells. It is an ester of the nucleoside inosine and phosphoric acid. IMP is an important intermediate in the conversion of adenosine monophosphate (AMP) to guanosine monophosphate (GMP) in the purine nucleotide cycle, which is critical for maintaining the balance of purine nucleotides in the body. Additionally, IMP can be converted back to AMP through the action of the enzyme adenylosuccinate lyase. IMP has been studied for its potential therapeutic benefits in various medical conditions, including neurodegenerative disorders and ischemia-reperfusion injury.
Ribonucleotides are organic compounds that consist of a ribose sugar, a phosphate group, and a nitrogenous base. They are the building blocks of RNA (ribonucleic acid), one of the essential molecules in all living organisms. The nitrogenous bases found in ribonucleotides include adenine, uracil, guanine, and cytosine. These molecules play crucial roles in various biological processes, such as protein synthesis, gene expression, and cellular energy production. Ribonucleotides can also be involved in cell signaling pathways and serve as important cofactors for enzymatic reactions.
Adenosine monophosphate (AMP) is a nucleotide that is the monophosphate ester of adenosine, consisting of the nitrogenous base adenine attached to the 1' carbon atom of ribose via a β-N9-glycosidic bond, which in turn is esterified to a phosphate group. It is an important molecule in biological systems as it plays a key role in cellular energy transfer and storage, serving as a precursor to other nucleotides such as ADP and ATP. AMP is also involved in various signaling pathways and can act as a neurotransmitter in the central nervous system.
"Thermotoga maritima" is not a medical term, but rather a scientific name for a specific type of bacterium. It belongs to the domain Archaea and is commonly found in marine environments with high temperatures, such as hydrothermal vents. The bacterium is known for its ability to survive in extreme conditions and has been studied for its potential industrial applications, including the production of biofuels and enzymes.
In a medical context, "Thermotoga maritima" may be relevant in research related to the development of new drugs or therapies, particularly those that involve extremophile organisms or their enzymes. However, it is not a term used to describe a specific medical condition or treatment.
'Bacillus subtilis' is a gram-positive, rod-shaped bacterium that is commonly found in soil and vegetation. It is a facultative anaerobe, meaning it can grow with or without oxygen. This bacterium is known for its ability to form durable endospores during unfavorable conditions, which allows it to survive in harsh environments for long periods of time.
'Bacillus subtilis' has been widely studied as a model organism in microbiology and molecular biology due to its genetic tractability and rapid growth. It is also used in various industrial applications, such as the production of enzymes, antibiotics, and other bioproducts.
Although 'Bacillus subtilis' is generally considered non-pathogenic, there have been rare cases of infection in immunocompromised individuals. It is important to note that this bacterium should not be confused with other pathogenic species within the genus Bacillus, such as B. anthracis (causative agent of anthrax) or B. cereus (a foodborne pathogen).
A missense mutation is a type of point mutation in which a single nucleotide change results in the substitution of a different amino acid in the protein that is encoded by the affected gene. This occurs when the altered codon (a sequence of three nucleotides that corresponds to a specific amino acid) specifies a different amino acid than the original one. The function and/or stability of the resulting protein may be affected, depending on the type and location of the missense mutation. Missense mutations can have various effects, ranging from benign to severe, depending on the importance of the changed amino acid for the protein's structure or function.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."
1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.
2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.
3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.
4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).
Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Adenylosuccinate lyase
Adenylosuccinate lyase deficiency
Roberta F. Colman
Nucleotide
Bacillus subtilis
Morpheein
Purine metabolism
GMP synthase
GABPB2
Adenylosuccinate
Brachycephaly
Fumarate lyase
List of diseases (A)
Angelman syndrome
SAICA
Purine nucleotide cycle
Causes of autism
List of MeSH codes (D08)
List of EC numbers (EC 4)
List of EC numbers (EC 6)
Adenylosuccinate lyase - Wikipedia
Adenylosuccinate lyase deficiency: MedlinePlus Genetics
Adenylosuccinate lyase deficiency - PubMed
Towards a suggestive facial dysmorphism in adenylosuccinate lyase deficiency? | Journal of Medical Genetics
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NDF-RT Code NDF-RT Name
Deficiency29
- Point mutations in adenylosuccinate that cause lowered enzymatic activity cause clinical symptoms that mark the condition adenylosuccinate lyase deficiency. (wikipedia.org)
- Adenylosuccinate lyase deficiency is a neurological disorder that causes brain dysfunction (encephalopathy) leading to delayed development of mental and movement abilities (psychomotor delay), autistic characteristics that affect communication and social interaction, and seizures. (medlineplus.gov)
- Adenylosuccinate lyase deficiency is classified into three forms based on the severity of the signs and symptoms. (medlineplus.gov)
- Adenylosuccinate lyase deficiency type I (also known as the severe form) is the most common. (medlineplus.gov)
- In individuals with adenylosuccinate lyase deficiency type II (also known as the moderate or mild form), development is typically normal for the first few years of life but then slows. (medlineplus.gov)
- All forms of adenylosuccinate lyase deficiency are caused by mutations in the ADSL gene. (medlineplus.gov)
- Most of the mutations involved in adenylosuccinate lyase deficiency change single protein building blocks (amino acids) in the adenylosuccinate lyase enzyme, which impairs its function. (medlineplus.gov)
- damage to brain tissue caused by one or both of these substances likely underlies the neurological problems that occur in adenylosuccinate lyase deficiency. (medlineplus.gov)
- Studies suggest that the amount of SAICAr relative to S-Ado reflects the severity of adenylosuccinate lyase deficiency. (medlineplus.gov)
- MediFind found 0 doctor with experience in Adenylosuccinate Lyase Deficiency. (medifind.com)
- How do I know if I should see an Adenylosuccinate Lyase Deficiency doctor near me? (medifind.com)
- Typically, your primary care physician will refer you to an Adenylosuccinate Lyase Deficiency doctor near me if they believe it to be necessary based on your symptoms or a formal diagnosis. (medifind.com)
- You can also explore your symptoms or research your diagnosis to find doctors who focus on Adenylosuccinate Lyase Deficiency near me, evaluated based on their level of expertise. (medifind.com)
- How do I find the best Adenylosuccinate Lyase Deficiency doctor near me? (medifind.com)
- It can be important to find a doctor near me who has extensive experience treating Adenylosuccinate Lyase Deficiency. (medifind.com)
- But it can be challenging to know which doctors near me have the most experience in Adenylosuccinate Lyase Deficiency. (medifind.com)
- User review sites like Yelp are often of minimal help, especially since there can be a number of problems with relying on reviews of Adenylosuccinate Lyase Deficiency doctors near me from other patients. (medifind.com)
- Here at MediFind, we evaluate physicians according to their expertise so you can quickly find the best Adenylosuccinate Lyase Deficiency doctor near me to fit your needs. (medifind.com)
- Each Adenylosuccinate Lyase Deficiency doctor near me is assessed based on research, patient volume, standing among peers, and connectedness to other physicians who focus specifically on Adenylosuccinate Lyase Deficiency. (medifind.com)
- MediFind analyzes data across thousands of health conditions, including Adenylosuccinate Lyase Deficiency, so a doctor who is an expert in one condition may not necessarily be an expert in another. (medifind.com)
- How does MediFind identify the best Adenylosuccinate Lyase Deficiency doctors near me? (medifind.com)
- When evaluating expertise in Adenylosuccinate Lyase Deficiency, we go beyond simply looking at the number of patients a doctor near me sees for Adenylosuccinate Lyase Deficiency. (medifind.com)
- We consider many additional factors such as the number of articles about Adenylosuccinate Lyase Deficiency a doctor has published in medical journals, participation in clinical trials studying Adenylosuccinate Lyase Deficiency, speaking at industry conferences about Adenylosuccinate Lyase Deficiency, prescribing and referral patterns related to Adenylosuccinate Lyase Deficiency (including those located near me), and strength of connections with other experts in Adenylosuccinate Lyase Deficiency. (medifind.com)
- Elite Adenylosuccinate Lyase Deficiency doctors near me are global leaders in their fields. (medifind.com)
- In addition to seeing a high volume of patients and referrals for Adenylosuccinate Lyase Deficiency, they publish many articles in medical journals, speak at medical conferences, and participate in multiple clinical trials on Adenylosuccinate Lyase Deficiency, often located near me. (medifind.com)
- They are likely to be on the cutting edge of new treatments for Adenylosuccinate Lyase Deficiency. (medifind.com)
- Adenylosuccinate lyase deficiency is a neurometabolic disorder associated by accumulation of succinylpurines in body fluids that causes encephalopathy. (ajsuccr.org)
- Corinna's research specifically uses the model organism, C. elegans, to study the neurological aspects of the rare inborn error of purine metabolism disease known as adenylosuccinate lyase deficiency (ASLD). (psu.edu)
- Corinna's research uses C. elegans with a reduced adenylosuccinate lyase activity to study neurobehavioral manifestations associated with the human disease adenylosuccinate lyase deficiency (ASLD). (psu.edu)
ADSL1
- Adenylosuccinate lyase (or adenylosuccinase) is an enzyme that in humans is encoded by the ADSL gene. (wikipedia.org)
Enzyme2
- Adenylosuccinate lyase (ASL) is an enzyme that catalyzes two reactions in the de novo purine biosynthetic pathway. (wikipedia.org)
- This gene provides instructions for making an enzyme called adenylosuccinate lyase, which performs two steps in the process that produces purine nucleotides. (medlineplus.gov)
Protein1
- protein_coding" "AAC74323","adhE","Escherichia coli","fused acetaldehyde-CoA dehydrogenase/iron-dependent alcohol dehydrogenase/pyruvate-formate lyase deactivase [Ensembl]. (ntu.edu.sg)
Ensembl2
- adenylosuccinate lyase [Ensembl]. (ntu.edu.sg)
- pyruvate formate-lyase 1 [Ensembl]. (ntu.edu.sg)
Adenosine monophosphate3
- AICAR proceeds through three more reactions before it becomes adenylosuccinate (also called succinyladenosine monophosphate or SAMP), which ASL then splits into adenosine monophosphate (AMP) and fumarate. (wikipedia.org)
- In the ASL-catalyzed reaction splitting adenylosuccinate into adenosine monophosphate (AMP) and fumarate, the AMP must rotate slightly after the reaction is complete and before fumarate is released in order for both products to fit in the active site. (wikipedia.org)
- Adenylosuccinate lyase converts a molecule called succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR) and converts succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP). (medlineplus.gov)
Interproscan2
- Adenylosuccinate lyase C-terminal [Interproscan]. (ntu.edu.sg)
- Glycine radical, Pyruvate formate lyase-like [Interproscan]. (ntu.edu.sg)
Purine1
- Adenylosuccinate lyase converts adenylosuccinate to AMP and fumarate as part of the purine nucleotide cycle. (wikipedia.org)
Fumarate1
- ASL cleaves adenylosuccinate into AMP and fumarate, and cleaves SAICAR into AICAR and fumarate. (wikipedia.org)
Bacillus1
- Adenylosuccinate lyase in humans and Bacillus subtilis can be competitively inhibited by the substrate analog adenosine phosphonobutyric acid 2'(3'), 5'-diphosphate (APBADP). (wikipedia.org)
Enzymatic1
- Understanding the structurel experience involving enzymatic conformations for adenylosuccinate lyase receptor in malarial parasite Plasmodium falciparum. (alksignaling.com)
Reaction1
- Adenylosuccinate lyase is part of the β-elimination superfamily of enzymes and it proceeds through an E1cb reaction mechanism. (wikipedia.org)
Studies1
- APBADP is a competitive inhibitor for both of the reactions catalyzed by adenylosuccinate lyase, and kinetic studies with APBADP show that the substrates for both reactions use the same active site. (wikipedia.org)
Activity1
- Adenylosuccinate lyase mutants can have considerably reduced activity whether the mutation is in or away from the active site. (wikipedia.org)
Synthetase3
- 17. Specificity of adenylosuccinate synthetase and adenylosuccinate lyase from Leishmania donovani. (nih.gov)
- 16211) para-aminobenzoate synthetase/4-amino-4-deoxychorismate lyase pabBC BBZA01000002 CDS ARMA_0015 192. (go.jp)
- For the case that M. pneumoniae does not require adenine as a substrate, we suggest adenylosuccinate synthetase (EC 6.3.4.4), adenylosuccinate lyase (EC 4.3.2.2) and GMP reductase (EC 1.7.1.7) to be operative. (embl.de)
Enzymes1
- Adenylosuccinate lyase is part of the β-elimination superfamily of enzymes and it proceeds through an E1cb reaction mechanism. (wikipedia.org)
Kinetic studies1
- APBADP is a competitive inhibitor for both of the reactions catalyzed by adenylosuccinate lyase, and kinetic studies with APBADP show that the substrates for both reactions use the same active site. (wikipedia.org)
Adenosine4
- AICAR proceeds through three more reactions before it becomes adenylosuccinate (also called succinyladenosine monophosphate or SAMP), which ASL then splits into adenosine monophosphate (AMP) and fumarate. (wikipedia.org)
- Adenylosuccinate lyase in humans and Bacillus subtilis can be competitively inhibited by the substrate analog adenosine phosphonobutyric acid 2'(3'), 5'-diphosphate (APBADP). (wikipedia.org)
- In the ASL-catalyzed reaction splitting adenylosuccinate into adenosine monophosphate (AMP) and fumarate, the AMP must rotate slightly after the reaction is complete and before fumarate is released in order for both products to fit in the active site. (wikipedia.org)
- Adenylosuccinate lyase converts a molecule called succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR) and converts succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP). (medlineplus.gov)
Mutants1
- Adenylosuccinate lyase mutants can have considerably reduced activity whether the mutation is in or away from the active site. (wikipedia.org)
SAICAR1
- ASL cleaves adenylosuccinate into AMP and fumarate, and cleaves SAICAR into AICAR and fumarate. (wikipedia.org)
Substrate1
- Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer. (nih.gov)
Group1
- A group of carbon-oxygen lyases. (lookformedical.com)