Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.12 (biotinidase)
 392 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The multiple carboxylase deficiencies are inborn errors in the metabolism of biotin in which there is defective activity of propionyl CoA carboxylase, 3-methylcrotonyl CoA carboxylase and pyruvate carboxylase. 2. Two distinct disorders have been described. 3. In one the fundamental defect is in the enzyme holocarboxylase synthetase which catalyzes the molecular activation of the apocarboxylase proteins. 4. In the other the fundamental defect is in biotinidase which catalyzes the reutilization of biotin and may be involved in its digestion and intestinal absorption.
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PMID:Multiple carboxylase deficiency. 328 72

The important role of biotin in human physiology has been highlighted by the recognition of two newly discovered human inborn errors of the metabolism of biotin. The molecular defect in the neonatal-onset disease is in the enzyme holocarboxylase synthetase. The defect in the later infantile-onset disease is in the enzyme biotinidase. Both disorders present with impressive clinical manifestations involving the skin and hair. In the neonatal disease, alopecia totalis is associated with a bright red scaly total body eruption. In biotinidase deficiency, the alopecia is more patchy and the skin lesions resemble acrodermatitis enteropathica. Both disorders are complicated by recurrent episodes of life-threatening acidosis and massive ketosis.
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PMID:Inborn errors of biotin metabolism. 331 10

Biotinidase deficiency satisfies all the criteria for incorporation into neonatal mass screening programmes for inborn errors of metabolism. We report our preliminary experiences with screening of 24,300 newborns during a 6 month-period when 1 infant with biotinidase deficiency was detected. On the basis of these results, this disorder appears to be as common as other well known metabolic disorders for which mass screening is available.
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PMID:Neonatal screening for biotinidase deficiency in north eastern Italy. 339 Dec 28

Biotinidase deficiency leads to a biotin-deficient state, with cardinal symptoms of ataxia, alopecia, and skin rash presenting in infancy. Previous reports of head CTs in patients with biotinidase deficiency did not note basal ganglia calcifications. We report the first case of biotinidase deficiency with basal ganglia calcifications. There were no symptoms referable to basal ganglia dysfunction.
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PMID:Basal ganglia calcifications in a case of biotinidase deficiency. 339 84

Biotinidase activity in 19 samples of human breast milk was investigated with the sensitive high-performance liquid chromatography (HPLC)-fluorometric method that we developed. All samples exhibited biotinidase activity. For mature milk the mean activity of 17 samples was 0.208 nmol.min-1.mL-1 milk (range, 0.087-0.516 nmol.min-1.mL-1) and mean specific activity was 7.51 pmol.min-1.mg-1 protein (range, 2.17-17.2 pmol.min-1.mg-1). These values are relatively low compared with the activity in human serum (5.26 +/- 2.92 nmol.min-1.mL-1 serum and 95.6 +/- 53.1 pmol.min-1.mg-1 protein; n = 246). Biotinidase activities of milk obtained at various times after birth were not significantly different. However, biotinidase activity in colostrum was about five times higher than that of mature milk. The existence of biotinidase activity in all specimens suggests that this enzyme plays an important nutritional role during infancy.
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PMID:Biotinidase in human breast milk. 340 8

Screening for biotinidase deficiency has been added recently to some national screening programmes. To clarify the problem of false-positive screening tests in premature infants, we have studied biotinidase activities in the plasma of this population in more detail. In 64 newborns (premature and term babies) biotinidase activities correlated positively with gestational age from the 2nd to the 30th day of life. During the 1st-3rd day the activities were below the normal adult range in all 64 infants. In 56 infants the activities subsequently increased gradually and reached the normal adult range during the 4th-40th day of life. In contrast, the biotinidase activities in eight preterm infants dropped during the 3rd-7th day of life. Impaired liver function as a possible cause for this finding could be ruled out in these infants. The lowest activities in these infants were measured during the 4th-6th day of life, i.e. unfortunately at a time when samples for the screening are normally taken. According to our data, 4-8 out of 48 preterm or small-for-date infants with biotinidase activities ranging from 4.7%-26% of the mean adult value would have given false-positive screening tests. A positive screening test was also obtained in a newborn and in an older unrelated child with a partial biotinidase deficiency. In these children the biotinidase activity did not rise but remained slightly below or at the lower range for heterozygotes (at 31% and 38% of the mean adult value). Currently we do not know whether such individuals are heterozygotes, or whether they have a variant of biotinidase deficiency. However, these children have developed normally without biotin therapy.
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PMID:Low biotinidase activity in plasma of some preterm infants: possible source of false-positive screening results. 340 23

DL-ethionine increases the activity of liver biotinidase, an enzyme which hydrolyzes biotinylesters and biotinylpeptides. Chronic DL-ethionine feeding increases transiently the activity of biotinidase in mouse and rat liver, after which it remains elevated in the serum. In the present work we show that both isomers of DL-ethionine are equally good enhancers of the liver biotinidase, while, 3-ethylthiopropionate, the toxic metabolite of DL-ethionine, has no effect on the biotinidase activity of either liver or serum. We have also employed two different combinations of inhibitors of the hydrolytic pathway of SAH, a transmethylation product and potent inhibitor of methylation. It was found that these inhibitors (EHNA and Ara-A, 2-deoxycoformycin and adenosine) increase the activity of serum biotinidase as was the case with ethionine. Because SAH does not ethylate biomolecules, these changes in biotinidase activity, which can not be prevented by adenine, biotin or lecithin are most probably related to the inhibition of methylation.
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PMID:Enhancement of biotinidase activity in mouse serum by inhibitors of methylation. 349 18

Screening programs for late-onset, biotin-responsive, multiple carboxylase deficiency (LMCD) detect colormetrically the presence of biotinidase activity in dried samples of whole-blood spotted on filter-papers as used in the neonatal screening of phenylketonuria. A sensitive and stable qualitative technique is described using 10 microliter of serum that avoids problems associated with poor sample collection, improper drying of blood-spots and transient color development. The modified assay is timely and suitable for the clinical laboratory not involved in mass screening programs.
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PMID:A qualitative assessment of biotinidase deficiency. 350 Jun 73

There are two distinct forms of multiple carboxylase deficiency. A neonatal onset form is due to deficiency of holocarboxylase-synthetase. A later onset form in which neurological abnormalities are seen as well as those of the skin and hair is due to biotinidase deficiency. It is the purpose of this report to describe a patient with biotinidase deficiency who presents bilateral optic atrophy. The dosage of biotinidase enzyme in the patient's serum and in other members of his family confirms the autosomal recessive transmission of this condition.
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PMID:Ocular aspects in biotinidase deficiency. Clinical and genetic original studies. 365 39

A simple and reliable method for quantification of biotinidase (EC.3.5.1.12) activity in dried blood spot was devised by a modification of the colorimetric screening test developed by Heard et al. (1984). The enzyme reaction and hemoglobin denaturation were carried out in a U-bottomed microplate. An aliquot of the reaction solution was transferred to a flat-bottomed microplate. After the coupling reaction was started, the adsorbance was measured in situ by a microplate-reader. Both intra- and inter-assay coefficient of variation (CV) values were less than 10%. Biotinidase activity in dried blood spot showed a good correlation to that in serum (r = 0.912, n = 8). This method was applied in a pilot screening of 18,945 newborns in Sapporo City. No positive results have been obtained as yet.
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PMID:A simple method for quantification of biotinidase activity in dried blood spot and its application to screening of biotinidase deficiency. 366 Apr 4


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