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J Biol Chem, Vol. 274, Issue 45, 31759-31762, November 5, 1999
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From the The flavin-dependent sulfhydryl
oxidase from chicken egg white catalyzes the oxidation of sulfhydryl
groups to disulfides with the reduction of oxygen to hydrogen peroxide.
Reduced proteins are the preferred thiol substrates of this secreted
enzyme. The egg white oxidase shows an average 64% identity (from
randomly distributed peptides comprising more than 30% of the protein
sequence) to a human protein, Quiescin Q6, involved in growth
regulation. Q6 is strongly expressed when fibroblasts enter reversible
quiescence (Coppock, D. L., Cina-Poppe, D., Gilleran, S. (1998)
Genomics 54, 460-468). A peptide antibody against Q6
cross-reacts with both the egg white enzyme and a flavin-linked
sulfhydryl oxidase isolated from bovine semen. Sequence analyses show
that the egg white oxidase joins human Q6, bone-derived growth factor,
GEC-3 from guinea pig, and homologs found in a range of multicellular organisms as a member of a new protein family. These proteins are
formed from the fusion of thioredoxin and ERV motifs. In contrast, the
flavin-linked sulfhydryl oxidase from Aspergillus niger is related to the pyridine nucleotide-dependent disulfide
oxidoreductases, and shows no detectable sequence similarity to this
newly recognized protein family.
Departments of Chemistry and Biochemistry
and § Animal and Food Sciences, University of Delaware,
Newark, Delaware 19716, the ¶ Oncology Research Laboratory,
Winthrop University Hospital, Mineola, New York 11501 and the
Department of Medicine, State University of New York Stony Brook
Medical Center, Stony Brook, New York 11790
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