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Literature summary extracted from

  • Ito, M.; Okino, N.; Tani, M.
    New insight into the structure, reaction mechanism, and biological functions of neutral ceramidase (2014), Biochim. Biophys. Acta, 1841, 682-691.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.1.23 cardiolipin phosphatidylglycerol and cardiolipin, which are major lipid components of Staphylococcus aureus, are effective in stimulating the hydrolysis of human skin-type ceramides in the absence of detergents Pseudomonas aeruginosa
3.5.1.23 phosphatidylglycerol phosphatidylglycerol and cardiolipin, which are major lipid components of Staphylococcus aureus, are effective in stimulating the hydrolysis of human skin-type ceramides in the absence of detergents Pseudomonas aeruginosa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.23 DNA and amino acid determination, phylogenetic tree Pseudomonas aeruginosa
3.5.1.23 DNA and amino acid determination, phylogenetic tree Dictyostelium discoideum
3.5.1.23 DNA and amino acid determination, phylogenetic tree Mycobacterium tuberculosis
3.5.1.23 DNA and amino acid determination, phylogenetic tree Oryza sativa
3.5.1.23 DNA and amino acid determination, phylogenetic tree Tribolium castaneum
3.5.1.23 DNA and amino acid determination, phylogenetic tree Drosophila melanogaster
3.5.1.23 DNA and amino acid determination, phylogenetic tree Triticum aestivum
3.5.1.23 DNA and amino acid determination, phylogenetic tree Laodelphax striatellus
3.5.1.23 DNA and amino acid determination, phylogenetic tree Danio rerio
3.5.1.23 DNA and amino acid determination, phylogenetic tree Aspergillus oryzae
3.5.1.23 DNA and amino acid determination, phylogenetic tree Dermatophilus congolensis
3.5.1.23 DNA and amino acid determination, phylogenetic tree, genetic structure Homo sapiens
3.5.1.23 DNA and amino acid determination, phylogenetic tree, genetic structure, the promoter region of mouse brain neutral CDase contains transcriptional response elements for GATA-2, C/EBP, and HNF3beta Mus musculus
3.5.1.23 DNA and amino acid determination, phylogenetic tree, recombinant expression of myc-tagged or GFP-tagged neutral CDase in HEK293 cells. When expressed in HEK293 or CHOP cells, both wild-type and mutant rat neutral CDase with a deleted mucin box are released into the medium Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.23 crystal structure of neutral CDase for the ceramide-free and C2-ceramide-bound forms Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.23 additional information a rat neutral CDase-GFP chimera protein, with GFP fused to the COOH terminus of the enzyme, is distributed in the ER/Golgi compartments and the plasma membrane of HEK293 cells Rattus norvegicus
3.5.1.23 additional information targeted expression of neutral CDase can rescue retinal degeneration in a subset of Drosophila phototransduction mutants Drosophila melanogaster

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.23 endoplasmic reticulum a rat neutral CDase-GFP chimera protein, with GFP fused to the COOH terminus of the enzyme, is distributed in the ER/Golgi compartments and the plasma membrane of HEK293 cells Rattus norvegicus 5783
-
3.5.1.23 extracellular the neutral ceramidase is exclusively secreted into the medium through a vesicular transport system when expressed in S2 cells Drosophila melanogaster
-
-
3.5.1.23 extracellular the neutral ceramidase is secreted Pseudomonas aeruginosa
-
-
3.5.1.23 extracellular the neutral ceramidase is secreted Dictyostelium discoideum
-
-
3.5.1.23 extracellular the neutral ceramidase is secreted Mycobacterium tuberculosis
-
-
3.5.1.23 extracellular the neutral ceramidase is secreted Dermatophilus congolensis
-
-
3.5.1.23 Golgi apparatus a rat neutral CDase-GFP chimera protein, with GFP fused to the COOH terminus of the enzyme, is distributed in the ER/Golgi compartments and the plasma membrane of HEK293 cells Rattus norvegicus 5794
-
3.5.1.23 lysosome of hepatocytes Rattus norvegicus 5764
-
3.5.1.23 membrane membrane topology of rat neutral CDase, overview. A rat neutral CDase-GFP chimera protein, with GFP fused to the COOH terminus of the enzyme, is distributed in the ER/Golgi compartments and the plasma membrane of HEK293 cells Rattus norvegicus 16020
-
3.5.1.23 membrane the neutral ceramidase is membrane-bound, enzyme membrane topology, overview Homo sapiens 16020
-
3.5.1.23 membrane the neutral ceramidase is membrane-bound, enzyme membrane topology, overview Mus musculus 16020
-
3.5.1.23 membrane the neutral ceramidase is membrane-bound, enzyme membrane topology, overview Danio rerio 16020
-
3.5.1.23 additional information the cell-surface expression of CDase is strongly inhibited by brefeldin A or treatment at 5°C, neutral and alkaline enzyme membrane topology, overview Rattus norvegicus
-
-
3.5.1.23 plasma membrane a rat neutral CDase-GFP chimera protein, with GFP fused to the COOH terminus of the enzyme, is distributed in the ER/Golgi compartments and the plasma membrane of HEK293 cells. The CDase is transported to the plasma membrane through the classical ER/Golgi pathway Rattus norvegicus 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.23 Ca2+ a calcium or magnesium ion is presumed to be important for stabilizing the two domains Pseudomonas aeruginosa
3.5.1.23 Mg2+ a calcium or magnesium ion is presumed to be important for stabilizing the two domains Pseudomonas aeruginosa
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Dictyostelium discoideum
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Mycobacterium tuberculosis
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Oryza sativa
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Tribolium castaneum
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Rattus norvegicus
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Homo sapiens
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Drosophila melanogaster
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Mus musculus
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Triticum aestivum
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Laodelphax striatellus
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Danio rerio
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Aspergillus oryzae
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center Dermatophilus congolensis
3.5.1.23 Zn2+ neutral CDase contains a zinc ion in the active site that functions as a catalytic center, the active center of CDase is the zinc ion itself, with the reaction following a similar mechanism as observed for zinc-dependent carboxypeptidase Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.23 additional information Pseudomonas aeruginosa the Pseudomonas neutral CDase can hydrolyze ceramide in intact erythrocytes, leading to hemolysis. The reaction mechanism for ceramide hydrolysis in vivo appears to be the same as that for ceramide hydrolysis in vitro because the mutation of residues surrounding the catabolic zinc ion abolish the hemolytic activity along with ceramide hydrolysis by CDase in intact erythrocytes ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.23 Aspergillus oryzae Q5B5D5
-
-
3.5.1.23 Danio rerio Q5W7F1
-
-
3.5.1.23 Dermatophilus congolensis
-
-
-
3.5.1.23 Dictyostelium discoideum
-
-
-
3.5.1.23 Drosophila melanogaster Q9VA70
-
-
3.5.1.23 Homo sapiens Q9NR71
-
-
3.5.1.23 Laodelphax striatellus R4N4U2
-
-
3.5.1.23 Mus musculus Q9JHE3
-
-
3.5.1.23 Mycobacterium tuberculosis
-
-
-
3.5.1.23 Oryza sativa
-
-
-
3.5.1.23 Pseudomonas aeruginosa
-
-
-
3.5.1.23 Rattus norvegicus Q91XT9
-
-
3.5.1.23 Tribolium castaneum
-
-
-
3.5.1.23 Triticum aestivum A9YFM2
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.1.23 glycoprotein the enzyme contains N-glycan Dictyostelium discoideum
3.5.1.23 glycoprotein the enzyme contains N-glycan Drosophila melanogaster
3.5.1.23 glycoprotein the enzyme contains N-glycan Aspergillus oryzae
3.5.1.23 glycoprotein the enzyme contains N-glycan and O-glycan Rattus norvegicus
3.5.1.23 glycoprotein the enzyme contains N-glycan and O-glycan Homo sapiens
3.5.1.23 glycoprotein the enzyme contains N-glycan and O-glycan Mus musculus
3.5.1.23 glycoprotein the enzyme contains N-glycan and O-glycan, the intestinal enzyme is glycosylated with complex-type N-glycans and O-glycans Danio rerio

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Pseudomonas aeruginosa
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Dictyostelium discoideum
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Mycobacterium tuberculosis
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Oryza sativa
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Tribolium castaneum
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Rattus norvegicus
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Homo sapiens
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Drosophila melanogaster
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Mus musculus
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Triticum aestivum
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Laodelphax striatellus
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Danio rerio
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Aspergillus oryzae
3.5.1.23 a ceramide + H2O = a carboxylate + sphingosine neutral CDase contains a zinc ion in the active site that functions as a catalytic center, and the hydrolysis of the N-acyl linkage in ceramide proceeds through a mechanism that is similar to that described for zinc-dependent carboxypeptidase, reaction mechanism, overview Dermatophilus congolensis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.23 brain high expression level of neutral ceramidase Rattus norvegicus
-
3.5.1.23 brain high expression level of neutral ceramidase Homo sapiens
-
3.5.1.23 endothelial cell
-
Rattus norvegicus
-
3.5.1.23 endothelial cell
-
Mus musculus
-
3.5.1.23 heart high expression level of neutral ceramidase Homo sapiens
-
3.5.1.23 hepatocyte in rat hepatocytes, neutral CDase signals appear as many foci distributed throughout the cytoplasm partially co-localizing with the LPG85 signal, a marker for lysosomes/late endosomes Rattus norvegicus
-
3.5.1.23 intestine a strong signal for neutral CDase is detected in zebrafish intestine at the luminal surface of the villi and microvilli of adsorptive epithelial cells Danio rerio
-
3.5.1.23 kidney high expression level of neutral ceramidase Homo sapiens
-
3.5.1.23 kidney high expression level of neutral ceramidase Mus musculus
-
3.5.1.23 kidney high expression level of neutral ceramidase, at the top of themicrovilli in proximal tubule cells Rattus norvegicus
-
3.5.1.23 liver high expression level of neutral ceramidase Homo sapiens
-
3.5.1.23 liver high expression level of neutral ceramidase Mus musculus
-
3.5.1.23 additional information neutral ceramidase is ubiquitously expressed in various mammalian tissues Rattus norvegicus
-
3.5.1.23 additional information neutral ceramidase is ubiquitously expressed in various mammalian tissues Homo sapiens
-
3.5.1.23 additional information neutral ceramidase is ubiquitously expressed in various mammalian tissues Mus musculus
-
3.5.1.23 pancreas high expression level of neutral ceramidase Homo sapiens
-
3.5.1.23 S2 cell
-
Drosophila melanogaster
-
3.5.1.23 skeletal muscle high expression level of neutral ceramidase Homo sapiens
-
3.5.1.23 small intestine high expression level of neutral ceramidase Rattus norvegicus
-
3.5.1.23 small intestine high expression level of neutral ceramidase Homo sapiens
-
3.5.1.23 small intestine highest expression level of neutral ceramidase, on the epithelial mucosa in the jejunum and ileum, neutral CDase is highly expressed in the small intestine along the brush border Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.23 additional information the Pseudomonas neutral CDase can hydrolyze ceramide in intact erythrocytes, leading to hemolysis. The reaction mechanism for ceramide hydrolysis in vivo appears to be the same as that for ceramide hydrolysis in vitro because the mutation of residues surrounding the catabolic zinc ion abolish the hemolytic activity along with ceramide hydrolysis by CDase in intact erythrocytes Pseudomonas aeruginosa ?
-
?
3.5.1.23 additional information the enzyme can hydrolyze human skin-specific omega-hydroxyacyl ceramides Pseudomonas aeruginosa ?
-
?

Subunits

EC Number Subunits Comment Organism
3.5.1.23 More neutral CDase is composed of two domains: a novel NH2-terminal domain harboring an active site and an immunoglobulin-like COOH-terminal domain. A zinc-binding site is located in the center of the NH2-terminal domain, whereas a calcium/magnesium-binding site is found at the interface between the NH2-terminal and COOH-terminal domains Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
3.5.1.23 CDase
-
Pseudomonas aeruginosa
3.5.1.23 CDase
-
Dictyostelium discoideum
3.5.1.23 CDase
-
Mycobacterium tuberculosis
3.5.1.23 CDase
-
Oryza sativa
3.5.1.23 CDase
-
Tribolium castaneum
3.5.1.23 CDase
-
Rattus norvegicus
3.5.1.23 CDase
-
Homo sapiens
3.5.1.23 CDase
-
Drosophila melanogaster
3.5.1.23 CDase
-
Mus musculus
3.5.1.23 CDase
-
Triticum aestivum
3.5.1.23 CDase
-
Laodelphax striatellus
3.5.1.23 CDase
-
Danio rerio
3.5.1.23 CDase
-
Aspergillus oryzae
3.5.1.23 CDase
-
Dermatophilus congolensis
3.5.1.23 neutral CDase
-
Rattus norvegicus
3.5.1.23 neutral ceramidase
-
Pseudomonas aeruginosa
3.5.1.23 neutral ceramidase
-
Dictyostelium discoideum
3.5.1.23 neutral ceramidase
-
Mycobacterium tuberculosis
3.5.1.23 neutral ceramidase
-
Oryza sativa
3.5.1.23 neutral ceramidase
-
Tribolium castaneum
3.5.1.23 neutral ceramidase
-
Rattus norvegicus
3.5.1.23 neutral ceramidase
-
Homo sapiens
3.5.1.23 neutral ceramidase
-
Drosophila melanogaster
3.5.1.23 neutral ceramidase
-
Mus musculus
3.5.1.23 neutral ceramidase
-
Triticum aestivum
3.5.1.23 neutral ceramidase
-
Laodelphax striatellus
3.5.1.23 neutral ceramidase
-
Danio rerio
3.5.1.23 neutral ceramidase
-
Aspergillus oryzae
3.5.1.23 neutral ceramidase
-
Dermatophilus congolensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.23 3
-
-
Dictyostelium discoideum
3.5.1.23 4 4.5
-
Aspergillus oryzae
3.5.1.23 5 12
-
Tribolium castaneum
3.5.1.23 5.7 6
-
Oryza sativa
3.5.1.23 6 7
-
Rattus norvegicus
3.5.1.23 6.5 7.5
-
Drosophila melanogaster
3.5.1.23 7.5
-
-
Mus musculus
3.5.1.23 7.5
-
-
Danio rerio
3.5.1.23 7.5 8.5
-
Homo sapiens
3.5.1.23 8
-
-
Laodelphax striatellus
3.5.1.23 8 9
-
Pseudomonas aeruginosa
3.5.1.23 8 9
-
Mycobacterium tuberculosis

Expression

EC Number Organism Comment Expression
3.5.1.23 Homo sapiens gemcitabine downregulates the neutral ceramidase down

General Information

EC Number General Information Comment Organism
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Pseudomonas aeruginosa
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Dictyostelium discoideum
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Mycobacterium tuberculosis
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Oryza sativa
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Tribolium castaneum
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Rattus norvegicus
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Homo sapiens
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Drosophila melanogaster
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Mus musculus
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Triticum aestivum
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Laodelphax striatellus
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Danio rerio
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Aspergillus oryzae
3.5.1.23 evolution ceramidases are classified into three distinct groups, acid (Asah1), neutral (Asah2), and alkaline (Asah3) CDases, based on their primary structure and optimum pH. Acid CDase catabolizes ceramide in lysosomes and is found only in vertebrates. In contrast, the distribution of neutral and alkaline CDases is broad, with both being found in species ranging from lower eukaryotes to mammals; however, only neutral CDase is found in prokaryotes, including some pathogenic bacteria. Neutral CDase is thought to have gained a specific domain (mucin box) in the N-terminal region after the vertebrate split, allowing the enzyme to be stably expressed at the plasmamembrane as a type II membrane protein. Molecular evolution of neutral ceramidase acquiring a mucin box, overview Dermatophilus congolensis
3.5.1.23 malfunction knockdown of the zebrafish neutral CDase with an antisense morpholino oligonucleotide led to an increase in the number of zebrafish embryos with severe morphological abnormalities, such as defects in blood circulation, which were possibly caused by abnormal heart formation Danio rerio
3.5.1.23 malfunction KO mice are impaired in the intestinal degradation of sphingolipids Mus musculus
3.5.1.23 additional information enzyme structure-function relationship, homology modeling of the enzymes using Pseudomonas CDase as the template, overview. The enzyme contains a signal/anchor sequence and a mucin box Rattus norvegicus
3.5.1.23 additional information enzyme structure-function relationship, homology modeling of the enzymes using Pseudomonas CDase as the template, overview. The enzyme contains a signal/anchor sequence and a mucin box Homo sapiens
3.5.1.23 additional information enzyme structure-function relationship, homology modeling of the enzymes using Pseudomonas CDase as the template, overview. The enzyme contains a signal/anchor sequence and a mucin box Danio rerio
3.5.1.23 additional information enzyme structure-function relationship, homology modeling of the enzymes using Pseudomonas CDase as the template, overview. The enzyme contains a signal/anchor sequence but no mucin box Drosophila melanogaster
3.5.1.23 additional information enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence and a mucin box Mus musculus
3.5.1.23 additional information enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box Pseudomonas aeruginosa
3.5.1.23 additional information enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box Dictyostelium discoideum
3.5.1.23 additional information enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box Oryza sativa
3.5.1.23 additional information enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box Tribolium castaneum
3.5.1.23 additional information enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box Triticum aestivum
3.5.1.23 additional information enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box Laodelphax striatellus
3.5.1.23 additional information enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box Aspergillus oryzae
3.5.1.23 additional information enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box Dermatophilus congolensis
3.5.1.23 additional information enzyme structure-function relationship, overview. The enzyme contains no signal/anchor sequence and no mucin box Mycobacterium tuberculosis
3.5.1.23 physiological function neutral CDase is expressed in the intestines of humans and plays a major role in ceramide metabolism in the gut Homo sapiens
3.5.1.23 physiological function neutral CDase may be involved in a pathway for the digestion of dietary sphingolipids in mice Mus musculus