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Literature summary for 1.8.3.2 extracted from

  • Javitt, G.; Grossman-Haham, I.; Alon, A.; Resnick, E.; Mutsafi, Y.
    Tal Ilani, and Deborah Fass cis-Proline mutants of quiescin sulfhydryl oxidase 1 with altered redox properties undermine extracellular matrix integrity and cell adhesion in fibroblast cultures (2019), Protein Sci., 28, 228-238 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Mus musculus
-
-

Organism

Organism UniProt Comment Textmining
Mus musculus Q8BND5
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 dithiothreitol + O2
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Mus musculus dithiothreitol disulfide + H2O2
-
?

Synonyms

Synonyms Comment Organism
QSOx1
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Mus musculus
quiescin sulfhydryl oxidase 1
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Mus musculus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
56.2
-
midpoint of thermal denaturation, mutant enzyme H72A/P119S Mus musculus
62.4
-
midpoint of thermal denaturation, wild-type enzyme Mus musculus
63.2
-
midpoint of thermal denaturation, mutant enzyme P119S Mus musculus
63.2
-
midpoint of thermal denaturation, mutant enzyme P119T Mus musculus
67.9
-
midpoint of thermal denaturation, mutant enzyme H72A Mus musculus

General Information

General Information Comment Organism
malfunction mutations at a cis-proline in QSOX1 that is conserved across the thioredoxin superfamily result in QSOX1 variants that showed a striking detrimental effect when added exogenously to fibroblasts. They severely disrupt the extracellular matrix and cell adhesion, even in the presence of naturally secreted, wild-type enzyme (QSOX1) Mus musculus
physiological function among other potential functions, QSOX1 supports extracellular matrix assembly in fibroblast cultures Mus musculus