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Literature summary for 2.3.1.291 extracted from

  • Laviad, E.L.; Kelly, S.; Merrill, A.H.; Futerman, A.H.
    Modulation of ceramide synthase activity via dimerization (2012), J. Biol. Chem., 287, 21025-21033 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.291

Protein Variants

Protein Variants Comment Organism
H220A/H221A complete loss of activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8N5B7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
palmitoyl-CoA + sphinganine
-
 Homo sapiens CoA + N-palmitoylsphinganine
-
 ?

General Information

General Information Comment Organism
physiological function CerS5 activity is inhibited in a dominant-negative fashion by co-expression with catalytically inactive CerS5, and isoform CerS2 activity is enhanced by co-expression with a catalytically active form of CerS5 or CerS6. In a constitutive heterodimer comprising CerS5 and CerS2, the activity of CerS2 depends on the catalytic activity of CerS5. CerS dimers are formed upon rapid stimulation of ceramide synthesis by curcumin Homo sapiens