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Literature summary extracted from

  • Malinina, L.; Brown, R.E.
    Catalytic mechanism of eukaryotic neutral ceramidase (2015), Structure, 23, 1371-1372 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.23 purified recombinant N-glycosylated extracellular region of nCDase in complex with phosphate, X-ray diffraction structure determination and analysis at 2.6 A resolution Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.23 Zn2+ required, binding site structure analysis Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.23 ceramide + H2O Homo sapiens
-
 fatty acid + sphingosine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.23 Homo sapiens Q9NR71
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.23 ceramide + H2O
-
 Homo sapiens fatty acid + sphingosine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.23 neutral ceramidase
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
3.5.1.23 metabolism sphingolipid metabolism and interconnected bioactive metabolites derived from ceramide, overview. Ceramide, the essential synthetic building block for sphingomyelin, glycosphingolipids, and ceramide-1-phosphate is hydrolyzed by ceramidase to fatty acid and sphingosine, which then is phosphorylated to sphingosine-1-phosphate (S1P) by sphingosine kinases Homo sapiens
3.5.1.23 additional information analysis of the catalytic mechanism of eukaryotic neutral ceramidase, structurally based explanation for ceramide specificity, comparison to the bacterial neutral ceramidase, overview. A general acid-base catalysis mechanism is proposed for amide bond hydrolysis by nCDase. In this mechanism, the Zn2+ ion functions to activate a water molecule for nucleophilic attack of the amide carbon. His196 serves as a general base for proton extraction from water and subsequently, a general acid to shuttle this proton to the nitrogen of ceramide during amide bond cleavage. The catalytic domain of the human enzyme contains an extra 30-residue subdomain inserted within the loop between beta14 and alpha7. In human nCDase, the 30-residue subdomain insert replacing the 6-residue span of bacterial CDase displays specific mobility. Stabilization of the subdomain conformation is aided by two internal disulfide bridges, formed by four cysteines that are conserved in eukaryotes Homo sapiens
3.5.1.23 physiological function neutral ceramidases are key enzymes of sphingolipid metabolism that hydrolyze the fatty acyl/sphingosine amide linkage of ceramide at neutral pH Homo sapiens