Heterozygote Expression in Propionyl Coenzyme A Carboxylase Deficiency
نویسندگان
چکیده
منابع مشابه
Propionyl coenzyme A carboxylase deficiency presenting as non-ketotic hyperglycinaemia.
A 4-month-old girl presented with myoclonic seizures and an electroencephalogram showing hypsarrhythmia. Hyperglycinuria and a cerebrospinal fluid to plasma glycine ratio of 0.2 suggested the diagnosis of non-ketotic hyperglycinaemia. Propionic acid and methyl citric acid were present in the urine, and propionyl coenzyme A carboxylase was deficient in leucocytes and fibroblasts. The ketotic and...
متن کاملPropionyl coenzyme A carboxylase is required for development of Myxococcus xanthus.
A dcm-1 mutant, obtained by transposon mutagenesis of Myxococcus xanthus, could aggregate and form mounds but was unable to sporulate under nutrient starvation. A sequence analysis of the site of insertion of the transposon showed that the insertion lies within the 3' end of a 1,572-bp open reading frame (ORF) designated the M. xanthus pccB ORF. The wild-type form of the M. xanthus pccB gene, o...
متن کاملThe Enzymatic Carboxylation of Propionyl Coenzyme A
(R)and (S)-Z-deuteriopropionyl coenzyme A of approximately 75% optical purity were prepared by a series of reactions starting from optically pure alanine. With these compounds as substrates for propionyl-CoA carboxylase, the deuterium isotope effect was found to be small and probably secondary. No tritium isotope effect was observed when enzymatically prepared 2-3H-propionyl-CoA was used as sub...
متن کاملMechanism of the Propionyl Carboxylase Reaction
A study of the exchange reactions between adenosine triphosphate and either radioactive inorganic phosphate, or adenosine diphosphate (l), catalyzed by propionyl carboxylase, showed that inorganic phosphate was required for adenosine triphosphate-adenosine diphosphate exchange and, conversely, adenosine diphosphate was required for adenosine triphosphateinorganic phosphate exchange. A requireme...
متن کاملBiochemical characterization of a Rhizobium etli monovalent cation-stimulated acyl-coenzyme A carboxylase with a high substrate specificity constant for propionyl-coenzyme A.
Biotin has a profound effect on the metabolism of rhizobia. It is reported here that the activities of the biotin-dependent enzymes acetyl-coenzyme A carboxylase (ACC; EC 6.4.1.2) and propionyl-coenzyme A carboxylase (PCC; EC 6.4.1.3) are present in all species of the five genera comprising the Rhizobiaceae which were examined. Evidence is presented that the ACC and PCC activities detectable in...
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ژورنال
عنوان ژورنال: Journal of Clinical Investigation
سال: 1978
ISSN: 0021-9738
DOI: 10.1172/jci109221