Human Molecular Genetics, Vol 5, 1011-1016, Copyright © 1996 by Oxford University Press
L Dupuis, A Leon-Del-Rio, D Leclerc, E Campeau, L Sweetman, JM Saudubray, G Herman, KM Gibson and RA Gravel
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.
ARTICLES
Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency
McGill University, Department of Biology, Montreal Children's Hospital Research Institute, Quebec, Canada.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  A. Perez-Monjaras, R. Cervantes-Roldan, I. Meneses-Morales, R. A. Gravel, S. Reyes-Carmona, S. Solorzano-Vargas, A. Gonzalez-Noriega, and A. Leon-Del-Rio Impaired Biotinidase Activity Disrupts Holocarboxylase Synthetase Expression in Late Onset Multiple Carboxylase Deficiency J. Biol. Chem., December 5, 2008; 283(49): 34150 - 34158. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. A. Narang, R. Dumas, L. M. Ayer, and R. A. Gravel Reduced histone biotinylation in multiple carboxylase deficiency patients: a nuclear role for holocarboxylase synthetase Hum. Mol. Genet., January 1, 2004; 13(1): 15 - 23. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. S. Solorzano-Vargas, D. Pacheco-Alvarez, and A. Leon-Del-Rio Holocarboxylase synthetase is an obligate participant in biotin-mediated regulation of its own expression and of biotin-dependent carboxylases mRNA levels in human cells PNAS, April 16, 2002; 99(8): 5325 - 5330. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. N Ames, I. Elson-Schwab, and E. A Silver High-dose vitamin therapy stimulates variant enzymes with decreased coenzyme binding affinity (increased Km): relevance to genetic disease and polymorphisms Am. J. Clinical Nutrition, April 1, 2002; 75(4): 616 - 658. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. W. Polyak, A. Chapman-Smith, P. J. Brautigan, and J. C. Wallace Biotin Protein Ligase from Saccharomyces cerevisiae. THE N-TERMINAL DOMAIN IS REQUIRED FOR COMPLETE ACTIVITY J. Biol. Chem., November 12, 1999; 274(46): 32847 - 32854. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Chapman-Smith and J. E. Cronan Jr Molecular Biology of Biotin Attachment to Proteins J. Nutr., February 1, 1999; 129(2): 477S - 484S. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. Campeau and R. A. Gravel Expression in Escherichia coli of N- and C-terminally Deleted Human Holocarboxylase Synthetase. INFLUENCE OF THE N-TERMINUS ON BIOTINYLATION AND IDENTIFICATION OF A MINIMUM FUNCTIONAL PROTEIN J. Biol. Chem., April 6, 2001; 276(15): 12310 - 12316. [Abstract] [Full Text] [PDF]
|
|