Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two kinetically and regulatory similar isoforms of AMP-deaminase were demonstrated in adult human skeletal muscle. In an extract from normal muscle, 5-10% of the AMP-deaminase activity was released from a phosphocellulose column in the 0.75 mol/l potassium chloride eluate, the remaning activity being eluted with 2.0 mol/l potassium chloride. In a muscle extract from a patient with myoadenylate deaminase deficiency the total AMP-deaminase activity was only 2% of the control, and it eluted mainly in 0.75 mol/l KCl fraction. The AMP-deaminase variant, which eluted with 2.0 mol/l KCl from the deficient muscle extract displayed kinetic properties distinctly different from those of normal muscle and resembled in this respect the isoform from fetal tissue. The experiments presented suggest that disturbances in the mechanisms regulating an alternative splicing of the primary transcript of skeletal muscle AMP-deaminase gene might be the molecular basis of the defect.
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PMID:Myoadenylate deaminase deficiency studies on normal and deaminase-deficient skeletal muscle. 225 94

The three major isoforms of AMP-deaminase (AMPda) were localized in human skeletal muscle and cultured muscle cells by immunocytochemistry. The M isoform was mainly located in Type II muscle fibers and showed a clear cross-striation. Particularly strong staining was present at the neuromuscular junction. Capillaries were also immunoreactive. The L isoform was predominantly observed in nerve bundles and to a minor extent in smooth muscle cells and endothelial cells. The E isoform was predominantly present in smooth muscle cells, and to a lesser extent in Type I muscle fibers and nerve bundles. In quadriceps muscle of patients with myoadenylate deaminase deficiency, no immunostaining for the M isozyme was observed, whereas reactivity for the L and E isoforms was unaltered. In human muscle cell cultures, mononuclear cells, including myoblasts, were immunoreactive for the L isoform and to a lesser extent the E isoform, whereas the M isoform was absent. In myotubes, diffuse or fibrillar staining was present for all three isoforms, but only the M isoform showed a clear cross-striation pattern in highly differentiated myotubes.
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PMID:Immunolocalization of AMP-deaminase isozymes in human skeletal muscle and cultured muscle cells: concentration of isoform M at the neuromuscular junction. 801 69

Myophosphorylase deficiency is characterized by exercise intolerance, muscle cramps, and recurrent myoglobinuria. Some patients are severely affected, whereas others are minimally affected or asymptomatic. The molecular basis of the disease has been elucidated but does not provide an explanation for the clinical variability. In a large cohort of patients with myophosphorylase deficiency, we tested the hypothesis that polymorphic variants in either myoadenylate deaminase (MADA) or angiotensin-converting enzyme (ACE) could act as modulators of phenotype expression. Forty-seven patients were evaluated. Clinical severity was assessed according to a severity scale of four grades. MADA activity was studied by histochemical and biochemical analysis of muscle, and the Q12X mutation in the adenine monophosphate deaminase 1 gene (AMPD1) and the insertion/deletion polymorphism in the ACE gene were assessed genetically. A complete MADA defect together with the Q12X mutation was detected in one severely affected patient. Eleven patients were heterozygous for the Q12X mutation. There was no association between clinical grading and MADA status. In contrast, we found a highly significant (p < 0.01) association between ACE genotype and clinical severity, with strong correlation between severe phenotype and number of D alleles. We show that ACE insertion/deletion polymorphism may play a significant role as phenotype modulator in McArdle's disease.
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PMID:Phenotype modulators in myophosphorylase deficiency. 1266 17

Approximately 1-2% of the population has a deficiency of the enzyme myoadenylate deaminase. Early reports suggested that patients with myoadenylate deaminase deficiency had various forms of myalgia, and exercise intolerance. However, a deficiency of the enzyme has been described in many conditions, including myopathies, neuropathies, and motor neuron disease. We report a patient with clinical diagnosis of myotonia congenita and absent myoadenylate deaminase reaction on the muscle biopsy. This is the first description of myoadenilate deaminase deficiency with myotonia congenita. Myoadenylate deaminase deficiency is the most common enzymatic deficit of muscle, and the association with other neuromuscular diseases is coincidental.
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PMID:Myotonia congenita and myoadenylate deaminase deficiency: case report. 1280 8

AMP-deaminase (AMPD, EC 3.5.4.6), which catalyzes the irreversible hydrolytic deamination of AMP to IMP and ammonia, is an important energy-related enzyme. The partial genomic sequence of the gene encoding myoadenylate deaminase (AMPD1) from the teleost fish Platichthys flesus was determined. The amino acid sequence of P. flesus AMPD1 shows 82% homology with that of the teleost fish Danio rerio. Comparison of genomic sequences of P. flesus and Rattus norvegicus reveals a high degree of conservation of both sequence and structural organization. A phylogenetic analysis of AMPD sequences shows that bony fish and mammalian AMPD1s arise by duplication of a common primordial gene.
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PMID:Partial characterization of the gene encoding myoadenylate deaminase from the teleost fish Platichthys flesus. 1982 Nov 38

Severe rhabdomyolysis (creatine phosphokinase = 29,400 U/L) developed in a 16-year-old boy from Manaus, Brazil, after he started treatment with chloroquine for infection with Plasmodium vivax. Treatment led to myoglobinuria and acute renal failure. After hemodialysis, the patient improved and a muscle biopsy specimen showed no myophosphorylase or deaminase deficiency. This case of rhabdomyolysis associated with P. vivax infection showed no comorbidities. The pathogenesis is still unclear. Although rhabdomyolysis is generally reported as a complication of Plasmodium falciparum malaria, leading to metabolic and renal complications,1 it has been reported in a patient with P. vivax infection with myoadenylate deaminase deficiency.2 We report a case in a patient without typical muscle enzyme deficiencies in which severe rhabdomyolysis developed while the patients was being treated with chloroquine for a confirmed P. vivax infection.
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PMID:Severe rhabdomyolysis caused by Plasmodium vivax malaria in the Brazilian Amazon. 2068 66