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Literature summary for 1.3.8.9 extracted from

  • Kabuyama, Y.; Suzuki, T.; Nakazawa, N.; Yamaki, J.; Homma, M.; Homma, Y.
    Dysregulation of very long chain acyl-CoA dehydrogenase coupled with lipid peroxidation (2010), Am. J. Physiol. Cell Physiol., 298, C107-C113.
    View publication on PubMed
Search for more literature for 1.3.8.9

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type enzyme and mutant S586A in HEK293 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
S586A naturally occuring mutation leading to phosphorylation of VLCAD at Ser586 is inhibited in myofibroblasts, resulting in a significant loss of enzyme activity coupled with lipid peroxidation. The S586A mutant shows a significant reduction in electron transfer activity Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of Ser586 is essential for VLCAD function Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
LF2 cell
-
 Homo sapiens
-
myofibroblast
-
 Homo sapiens
-
TIG-7 cell
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
very long chain acyl-CoA dehydrogenase
-
 Homo sapiens
VLCAD
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction phosphorylation of VLCAD at Ser586 is inhibited in myofibroblasts, resulting in a significant loss of enzyme activity coupled with lipid peroxidation.Thus Ser586 represents a critical site for VLCAD activity, whose dysregulation might contribute to the progression of idiopathic pulmonary fibrosis, IPF, a chronic interstitial lung disease, and other oxidative-stress mediated diseases Homo sapiens
physiological function VLCAD is a rate-limiting enzyme in fatty acid beta-oxidation and is regulated by phosphorylation at Ser586 Homo sapiens