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1 recently discovered enigmatic flavin-linked sulfhydryl oxidase.
2 h protein disulfide bonds in thioredoxin and sulfhydryl oxidase.
3 ases and is related to the ERV/ALR family of sulfhydryl oxidases.
4 on to the earlier reports of metal-dependent sulfhydryl oxidases.
5 , PRDX4, and the candidate oxidants quiescin-sulfhydryl oxidase 1 (QSOX1) and vitamin K epoxide reduc
7 on in the 5' untranslated region of quiescin sulfhydryl oxidase 1 isoform a (QSOX1-a), not present in
8 ing that the C-X-X-C motif was essential for sulfhydryl oxidase activity and responsible for the alte
9 lly, the assay is used to show that there is sulfhydryl oxidase activity in a number of secretory flu
10 ted from chicken egg white and found to have sulfhydryl oxidase activity with a range of small molecu
11 92 C(155)XXC(158) amino acids, important for sulfhydryl oxidase activity, were mutated to A(155)XXA(1
13 n excellent substrate of the enzyme quiescin-sulfhydryl oxidase and may find utility in the character
15 ells, the assay could detect 15fmol of avian sulfhydryl oxidase and the rates were linearly dependent
16 family of flavin adenine dinucleotide-linked sulfhydryl oxidases and is related to the ERV/ALR family
17 luble 62 kDa FAD-linked and EDTA-insensitive sulfhydryl oxidase apparently constitutes the dominant d
18 revealed GFER, a mitochondrial FAD-dependent sulfhydryl oxidase, as an essential regulator of tumor g
20 ysteine and selenomethionine residues in the sulfhydryl oxidase augmenter of liver regeneration (ALR)
21 and depend on the oxidoreductase Mia40, the sulfhydryl oxidase augmenter of liver regeneration (ALR)
22 he cysteine residues are rapidly oxidized by sulfhydryl oxidase, but activity is efficiently restored
24 sitive, continuous fluorescence assay of the sulfhydryl oxidases can be devised with careful selectio
28 lfide bond formation in partnership with the sulfhydryl oxidase Ero1 in vitro with higher turnover ra
29 ial flavin adenine dinucleotide (FAD)-linked sulfhydryl oxidase Erv1 (essential for respiration and v
33 ctions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to subst
34 us pathway with the oxidoreductase Mia40 and sulfhydryl oxidase Erv1, termed the mitochondrial interm
41 t biochemical evidence that a plant quiescin sulfhydryl oxidase homolog (QSOX1) is a redox sensor tha
44 AD prosthetic group of the ERV/ALR family of sulfhydryl oxidases is housed at the mouth of a 4-helix
48 Glucose oxidase, hexose oxidase, peroxidase, sulfhydryl oxidase, lipase, and lipoxygenase form disulf
49 s enzymes (tyrosinase, peroxidase, catalase, sulfhydryl oxidase, lipoxygenase, lipase, protein disulf
50 with the augmenter of liver regeneration, a sulfhydryl oxidase of the mitochondrial intermembrane sp
51 ies between members of the ERV/ALR family of sulfhydryl oxidases provides insights into their likely
53 es the substrate specificity of the quiescin sulfhydryl oxidase (QSOX) family of disulfide-generating
61 ously linked to cancer, most strongly on the sulfhydryl oxidase Qsox1 which we show is required for m
63 neration (ALR) is both a growth factor and a sulfhydryl oxidase that binds FAD in an unusual helix-ri
65 1-like (Gfer) is an evolutionarily conserved sulfhydryl oxidase that is enriched in embryonic and adu
66 ngs to the ERV1/ALR family of FAD-containing sulfhydryl oxidases that use oxygen as the electron acce
67 wn to be a substrate of the flavin-dependent sulfhydryl oxidases, there is little quantitative inform
70 understood flavoenzyme may not function as a sulfhydryl oxidase within the mitochondrial intermembran