Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.23
Description:Ceramidase.
Alternative Name: Acylsphingosine deacylase.
Cath: 2.60.40.230; 2.60.40.2300;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.23
BRENDA Enzyme Link: BRENDA 3.5.1.23
KEGG Enzyme Link: KEGG3.5.1.23
BioCyc Enzyme Link: BioCyc 3.5.1.23
ExPASy Enzyme Link: ExPASy3.5.1.23
EC2PDB Enzyme Link: EC2PDB 3.5.1.23
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.23
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.23
IntEnz Enzyme Link: IntEnz 3.5.1.23
MEDLINE Enzyme Link: MEDLINE 3.5.1.23
MSA:

3.5.1.23;

Phylogenetic Tree:

3.5.1.23;

Uniprot:
M-CSA:
RHEA:20856 an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[NH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Role of alkaline ceramidases in the generation of sphingosine and its phosphate in erythrocytes.Xu R, Sun W, Jin J, Obeid LM, Mao C2010 Jul20207939
Expression, purification, and characterization of a recombinant neutral ceramidase from Mycobacterium tuberculosis.Okino N, Ikeda R, Ito M201020139604
Purification and characterization of human intestinal neutral ceramidase.Ohlsson L, Palmberg C, Duan RD, Olsson M, Bergman T, Nilsson A2007 Aug17475390
Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides.Mao C, Xu R, Szulc ZM, Bielawski J, Becker KP, Bielawska A, Galadari SH, Hu W, Obeid LM2003 Aug 1512783875