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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.24 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
2.3.1.297 gene CERS2, recombinant expression of C-terminally HA-tagged CerS2 and of chimeric HA-tagged CerS5:CerS2 heterodimer in HEK-293 cells, recombinant expression of FLAG-tagged CerS2 in HEK-293 cells. Isozymes CerS5 and CerS6 modulate CerS2 activity upon coexpression Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.24 H220A/H221A site-directed mutagenesis, mutation of the two residues involved in catalytic activity completely abrogates CerS5 activity in a constitutive dimer Homo sapiens
2.3.1.24 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
2.3.1.291 H220A/H221A complete loss of activity Homo sapiens
2.3.1.297 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). 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

EC Number Metals/Ions Comment Organism Structure
2.3.1.24 Mg2+ activates Homo sapiens
2.3.1.297 Mg2+ activates Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.24 sphinganine + palmitoyl-CoA Homo sapiens
-
 N-palmitoylsphinganine + CoA
-
 ?
2.3.1.297 behenoyl-CoA + dihydrosphingosine Homo sapiens
-
 CoA + N-behenoyldihydrosphingosine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.24 Homo sapiens Q8N5B7
-
-
2.3.1.291 Homo sapiens Q8N5B7
-
-
2.3.1.297 Homo sapiens Q96G23
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.3.1.24 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
2.3.1.297 recombinant HA-tagged chimeric mutant CerS5:TM:CerS2 is reconstituted in 1,2-dioleoyl-sn-glycero-3-phosphocholine liposomes Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.24 sphinganine + palmitoyl-CoA
-
 Homo sapiens N-palmitoylsphinganine + CoA
-
 ?
2.3.1.291 palmitoyl-CoA + sphinganine
-
 Homo sapiens CoA + N-palmitoylsphinganine
-
 ?
2.3.1.297 behenoyl-CoA + dihydrosphingosine
-
 Homo sapiens CoA + N-behenoyldihydrosphingosine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.24 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
2.3.1.297 dimer dimer CerS activity can be modulated by dimer formation. CerS2 activity is enhanced by co-expression with a catalytically active form of CerS5 or CerS6. CerS dimers are formed rapidly upon stimulation of ceramide synthesis Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.3.1.24 ceramide synthase 5
-
 Homo sapiens
2.3.1.24 CerS5
-
 Homo sapiens
2.3.1.297 ceramide synthase 2
-
 Homo sapiens
2.3.1.297 CerS2
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.24 37
-
 assay at Homo sapiens
2.3.1.297 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.24 7.5
-
 assay at Homo sapiens
2.3.1.297 7.5
-
 assay at Homo sapiens

General Information

EC Number General Information Comment Organism
2.3.1.24 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
2.3.1.291 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
2.3.1.297 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