FAD-linked sulfhydryl oxidase ALR

Definition:

[Isoform 1]: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.; [Isoform 2]: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.

References:

[1]. Malgorzata E Sztolsztener, et al. Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40. Traffic. 2013 Mar;14(3):309-20. [Content Brief]

[2]. Lucia Banci, et al. An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR. J Am Chem Soc. 2012 Jan 25;134(3):1442-5. [Content Brief]

[3]. Manuel Fischer, et al. Protein import and oxidative folding in the mitochondrial intermembrane space of intact mammalian cells. Mol Biol Cell. 2013 Jul;24(14):2160-70. [Content Brief]

[4]. Lucia Banci, et al. Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR. Proc Natl Acad Sci U S A. 2011 Mar 22;108(12):4811-6. [Content Brief]

[5]. Vidyadhar N Daithankar, et al. Augmenter of liver regeneration: substrate specificity of a flavin-dependent oxidoreductase from the mitochondrial intermembrane space. Biochemistry. 2009 Jun 9;48(22):4828-37. [Content Brief]

[6]. Vidyadhar N Daithankar, et al. Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy. Biochemistry. 2010 Aug 10;49(31):6737-45. [Content Brief]

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