Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II.
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Cloned the human molybdenum cofactor sulfurase (HMCS/MOCOS) gene; a nonsense variant (Arg419Ter) in two classical xanthinuria type II patients demonstrated that a functional defect of HMCS causes type II xanthinuria (combined XDH and aldehyde oxidase deficiency).
"a functional defect of the HMCS gene is responsible for classical xanthinuria type II, and that HMCS protein functions to provide a sulfur atom for the molybdenum cofactor of XDH and AO."
Next-generation sequencing to generate interactome datasets.
A proteome-scale map of the human interactome network.
Architecture of the human interactome defines protein communities and disease networks.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects.
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Defines the PLP-dependent L-cysteine desulfurase mechanism of the MOCOS NifS-like domain, with the liberated sulfur transferred to the C-terminally bound Moco.
"The NifS-like domain catalyzes the mobilization of sulfur from L-cysteine in a PLP-dependent manner via its so-called L-cysteine desulfurase activity, with the liberated sulfur serving as a substrate for sulfuration of the C-terminally bound Moco."
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Direct biochemical (IDA) characterization: the type II variant Thr349Ile in the NifS-like domain reduced PLP binding and abolished cysteine desulfurase activity of recombinant MOCOS-NifS.
"the type II-linked c.1046 C>T variant resulted in a reduced yield, reduced binding of the PLP cofactor and absence of cysteine desulfurase activity"
Exchange of oxygen with sulfur in MoCo
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Human xanthine oxidase and aldehyde oxidase require the MoCo in which an oxygen bound to molybdenum is replaced with sulfur; this exchange is catalyzed by MOCOS.
"The exchange is catalyzed by the MOCOS cysteine desulfurase (Ichida et al, 2001)."
Molybdenum cofactor biosynthesis
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In humans, sulfurated (rather than desulfurated) molybdenum cofactor is found on xanthine and aldehyde oxidases, a refinement needed for their function.
"This means, in humans we find sulfurated instead of desulfurated molybdenum cofactor on these two enzymes"