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Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency.
Hum Mol Genet 1996; 5(7):1011-6HM

Abstract

Holocarboxylase synthetase (HCS) catalyses the biotinylation of the four biotin-dependent carboxylases found in humans. A deficiency in HCS results in biotin-responsive multiple carboxylase deficiency (MCD). We have identified six different point mutations in the HCS gene in nine patients with MCD. Two of the mutations are frequent among the MCD patients analyzed. Four of the mutations cluster in the putative biotin-binding domain as deduced from the corresponding Escherichia coli enzyme and consistent with an explanation for biotin-responsiveness based on altered affinity for biotin. The two others may define an additional domain involved in biotin-binding or biotin-mediated stabilization of the protein.

Authors+Show Affiliations

McGill University, Department of Biology, Montreal Children's Hospital Research Institute, Quebec, Canada.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8817339

Citation

Dupuis, L, et al. "Clustering of Mutations in the Biotin-binding Region of Holocarboxylase Synthetase in Biotin-responsive Multiple Carboxylase Deficiency." Human Molecular Genetics, vol. 5, no. 7, 1996, pp. 1011-6.
Dupuis L, Leon-Del-Rio A, Leclerc D, et al. Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency. Hum Mol Genet. 1996;5(7):1011-6.
Dupuis, L., Leon-Del-Rio, A., Leclerc, D., Campeau, E., Sweetman, L., Saudubray, J. M., ... Gravel, R. A. (1996). Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency. Human Molecular Genetics, 5(7), pp. 1011-6.
Dupuis L, et al. Clustering of Mutations in the Biotin-binding Region of Holocarboxylase Synthetase in Biotin-responsive Multiple Carboxylase Deficiency. Hum Mol Genet. 1996;5(7):1011-6. PubMed PMID: 8817339.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency. AU - Dupuis,L, AU - Leon-Del-Rio,A, AU - Leclerc,D, AU - Campeau,E, AU - Sweetman,L, AU - Saudubray,J M, AU - Herman,G, AU - Gibson,K M, AU - Gravel,R A, PY - 1996/7/1/pubmed PY - 1996/7/1/medline PY - 1996/7/1/entrez SP - 1011 EP - 6 JF - Human molecular genetics JO - Hum. Mol. Genet. VL - 5 IS - 7 N2 - Holocarboxylase synthetase (HCS) catalyses the biotinylation of the four biotin-dependent carboxylases found in humans. A deficiency in HCS results in biotin-responsive multiple carboxylase deficiency (MCD). We have identified six different point mutations in the HCS gene in nine patients with MCD. Two of the mutations are frequent among the MCD patients analyzed. Four of the mutations cluster in the putative biotin-binding domain as deduced from the corresponding Escherichia coli enzyme and consistent with an explanation for biotin-responsiveness based on altered affinity for biotin. The two others may define an additional domain involved in biotin-binding or biotin-mediated stabilization of the protein. SN - 0964-6906 UR - https://www.unboundmedicine.com/medline/citation/8817339/Clustering_of_mutations_in_the_biotin_binding_region_of_holocarboxylase_synthetase_in_biotin_responsive_multiple_carboxylase_deficiency_ L2 - https://academic.oup.com/hmg/article-lookup/doi/10.1093/hmg/5.7.1011 DB - PRIME DP - Unbound Medicine ER -