Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.24 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 2.3.1.24

Cloned(Commentary)

Cloned (Comment) Organism
gene CERS5, recombinant expression of HA-tagged wild-type enzyme, and point mutants as well as truncated CerS5DELTAC332-392 mutant and chimeric mutant enzyme in HEK-293 cells, recombinant expression of FLAG-tagged CerS5 in HEK-293 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
H220A/H221A site-directed mutagenesis, mutation of the two residues involved in catalytic activity completely abrogates CerS5 activity in a constitutive dimer Homo sapiens
additional information cloning of a chimeric HA-tagged CerS5:CerS2 isozymes heterodimer, insertion of a transmembrane (TM) domain3 between the two monomers of the dimer (CerS5:TM:CerS5-HA). The truncated mutant DELTA332-392 lacking the last putative transmembrane domain is inactive. Chimeric mutant CerS5:TM:CerS2-HA displays slightly more activity using C16-CoA as substrate than CerS5, but remarkably, CerS2 activity measured using C22-CoA is elevated by 3fold. Isozymes CerS5 and CerS6 modulate CerS2 activity upon coexpression. This increase in CerS2 activity is abolished using a noncatalytically active form of CerS5 in the constitutive dimer (CerS5HH:TM:CerS2-HA), demonstrating that optimal CerS2 activity depends on an interaction with a catalytically active form of CerS5 Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8N5B7
-
-

Renatured (Commentary)

Renatured (Comment) Organism
recombinant HA-tagged wild-type CerS5 and HA-tagged chimeric mutant CerS5:TM:CerS2 are reconstituted in 1,2-dioleoyl-sn-glycero-3-phosphocholine liposomes Homo sapiens

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer CerS activity can be modulated by dimer formation. CerS5 activity is inhibited in a dominant-negative fashion by co-expression with catalytically inactive CerS5. CerS dimers are formed rapidly upon stimulation of ceramide synthesis Homo sapiens

Synonyms

Synonyms Comment Organism
ceramide synthase 5
-
 Homo sapiens
CerS5
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Homo sapiens

General Information

General Information Comment Organism
additional information chimeric mutant CerS5:TM:CerS2-HA displays slightly more activity using C16-CoA as substrate than CerS5, but remarkably, CerS2 activity measured using C22-CoA is elevated by 3fold. Isozymes CerS5 and CerS6 modulate CerS2 activity upon co-expression. This increase in CerS2 activity is abolished using a noncatalytically active form of CerS5 in the constitutive dimer (CerS5HH:TM:CerS2-HA), demonstrating that optimal CerS2 activity depends on an interaction with a catalytically active form of CerS5 Homo sapiens