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Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients
Author(s) -
Johnson Jean L.,
Coyne Katharine E.,
Garrett Robert M.,
Zabot MarieTherese,
Dorche Claude,
Kisker Caroline,
Rajagopalan K. V.
Publication year - 2002
Publication title -
human mutation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 162
eISSN - 1098-1004
pISSN - 1059-7794
DOI - 10.1002/humu.9038
Subject(s) - frameshift mutation , sulfite oxidase , missense mutation , biology , mutation , genetics , nonsense mutation , transition (genetics) , indel mutation , gene , microbiology and biotechnology , sulfite , biochemistry , genotype , single nucleotide polymorphism
We report twelve novel mutations in patients with isolated sulfite oxidase deficiency. The mutations are in SUOX, the gene that encodes the molybdohemoprotein sulfite oxidase. These include two frameshift mutations, a four‐basepair deletion (562del4) and a single‐basepair insertion (113insC), both resulting in premature termination. Nonsense mutations predicting Y343X and Q364X substitutions were identified in a homozygous state in three patients, the latter in two sibs. The remaining eight are missense mutations generating single amino acid substitutions. From the position of the substituted residues, seven of these mutations are considered to be causative of the enzyme deficiency: I201L, R211Q, G305S, R309H, K322R, Q339R, and W393R. The eighth, a C>T transition, predicts an R319C substitution, which could affect the binding of the molybdenum cofactor and thus severely reduce sulfite oxidase activity. This mutation, however, is downstream of a frameshift mutation and is therefore not the causative mutation in this individual. © 2002 Wiley‐Liss, Inc.