Two siblings with tyrosinaemia type 2

Aydın, Ömer; Zorlu, Pelin; Kunak, Benal; Teziç, Tahsin; Eken, Alev

doi:10.1007/s00431-002-0962-4

Eur J Pediatr

2003

DOI: 10.1007/s00431-002-0962-4

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Two siblings with tyrosinaemia type 2

Ömer Aydın

Pelin Zorlu

Benal Kunak

et al.

Abstract: We report on two siblings with tyrosinaemia type 2, a 6-year-old girl and her 3.5-year-old brother with a main complaint of painful palmo-plantar hyperkeratosis. The boy presented also conjunctival injection, photophobia, lacrimation and conjunctivitis. Blood tyrosine levels were increased in both patients, 150.6 and 202.3 lmol/dl, respectively (reference value: 5.8±2.2 lmol/dl). After 1 month of dietary treatment with low protein, low phenylalanine and tyrosine, tyrosine levels decreased to 37.7 and 65.6 lmol… Show more

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Cited by 4 publications

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“…Mental retardation is variably associated with this disorder and ranges from severe retardation to slight decreases in intelligence [7]. Current intervention is limited to a strict tyrosine‐ phenylalanine‐restricted diet, initiated at infancy, that results in reversal of clinical symptoms [8]. However, some reports of long‐term patient follow‐up state that recurrence of clinical symptoms occurs with cessation of dietary therapy [9].…”

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The narrow substrate specificity of human tyrosine aminotransferase – the enzyme deficient in tyrosinemia type II

Sivaraman

Kirsch

2006

The FEBS Journal

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Tyrosinemia type II [Richner-Hanhart syndrome, Online Mendelian Inheritance in Man (OMIM) no. 276 600] is a rare autosomal recessive disorder caused by a deficiency of hepatic cytosolic tyrosine aminotransferase (E.C.2.6.1.5), the rate-determining enzyme of tyrosine catabolism that catalyzes the transamination reaction converting tyrosine to p-hydroxyphenylpyruvate (HPP) [1][2][3]. The clinical syndromes include elevated plasma tyrosine levels, skin and eye lesions [4][5][6]. The lesions are the result of local deposition of cellular tyrosine crystals resulting in an inflammatory response. Ophthalmologic features of tyrosinemia type II typically occur before skin lesions develop; the early signs consist of excessive tearing, redness, pain and photophobia. Age at onset of skin lesions can range from the first few weeks of life to the second decade. Mental retardation is variably associated with this disorder and ranges from severe Human tyrosine aminotransferase (hTATase) is the pyridoxal phosphatedependent enzyme that catalyzes the reversible transamination of tyrosine to p-hydrophenylpyruvate, an important step in tyrosine metabolism. hTATase deficiency is implicated in the rare metabolic disorder, tyrosinemia type II. This enzyme is a member of the poorly characterized Ic subfamily of the family I aminotransferases. The full length and truncated forms of recombinant hTATase were expressed in Escherichia coli, and purified to homogeneity. The pH-dependent titration of wild-type reveals a spectrum characteristic of family I aminotransferases with an aldimine pK a of 7.22. I249A mutant hTATase exhibits an unusual spectrum with a similar aldimine pK a (6.85). hTATase has very narrow substrate specificity with the highest enzymatic activity for the Tyr ⁄ a-ketoglutarate substrate pair, which gives a steady state k cat value of 83 s )1 . In contrast there is no detectable transamination of aspartate or other cosubstrates. The present findings show that hTATase is the only known aminotransferase that discriminates significantly between Tyr and Phe: the k cat ⁄ K m value for Tyr is about four orders of magnitude greater than that for Phe. A comparison of substrate specificities of representative Ia and Ic aminotransferases is described along with the physiological significance of the discrimination between Tyr and Phe by hTATase as applied to the understanding of the molecular basis of phenylketonuria.Abbreviations

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The narrow substrate specificity of human tyrosine aminotransferase – the enzyme deficient in tyrosinemia type II

Sivaraman

Kirsch

2006

The FEBS Journal

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Clinical and mutational investigations of tyrosinemia type II in Northern Tunisia: Identification and structural characterization of two novel TAT mutations

Charfeddine

Monastiri

Mokni

et al. 2006

Molecular Genetics and Metabolism

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Evaluation of the Marine AlgaUlva rigidaas a Food Supplement: Effect of Intake on Intestinal, Hepatic, and Renal Enzyme Activities in Rats

Taboada

Millán²,

Míguez

2011

Journal of Medicinal Food

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The use of seaweeds as a food is more widespread in Eastern than in Western countries, although demand for these plants has increased in the West because their possible usefulness as dietary supplements. However, very little is known about the effects of regular consumption of algae. The aim of the present study was to determine the composition of Ulva rigida and to evaluate the effects of dietary supplementation of the diet with 10% alga for 4 weeks on dietary intake, growth, protein efficiency ratio, diet conversion ratio, and some organ weights in growing male rats. We also studied the effect of inclusion of the alga in the diet on intestinal, hepatic, and renal enzymatic activities. U. rigida was found to be a good source of protein and carbohydrates. Food intake was higher in the U. rigida group than in the control group, but ingestion of alga did not have any effect on the other trophic parameters. The intestinal disaccharidase and leucine aminopeptidase activities were lower in rats fed with alga than in control rats, but γ-glutamyl transpeptidase activity was higher in the kidneys of alga-fed rats than in control rats. U. rigida contains high amounts of protein, carbohydrates, vitamins, and minerals and low amounts of lipids. Analysis of the amino acid composition revealed good-quality protein. The addition of alga to the diet inhibited disaccharidase activities, which suggested that alga consumption could be useful in some chronic disorders associated with pertubations of glucose homeostasis caused by carbohydrate absorption.

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Two siblings with tyrosinaemia type 2

Cited by 4 publications

References 5 publications

The narrow substrate specificity of human tyrosine aminotransferase – the enzyme deficient in tyrosinemia type II

The narrow substrate specificity of human tyrosine aminotransferase – the enzyme deficient in tyrosinemia type II

Clinical and mutational investigations of tyrosinemia type II in Northern Tunisia: Identification and structural characterization of two novel TAT mutations

Evaluation of the Marine AlgaUlva rigidaas a Food Supplement: Effect of Intake on Intestinal, Hepatic, and Renal Enzyme Activities in Rats

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