Activating Compound | Comment | Organism | Structure |
---|---|---|---|
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 | |
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 (Comment) | Organism |
---|---|
DNA and amino acid determination, phylogenetic tree | Pseudomonas aeruginosa |
DNA and amino acid determination, phylogenetic tree | Dictyostelium discoideum |
DNA and amino acid determination, phylogenetic tree | Mycobacterium tuberculosis |
DNA and amino acid determination, phylogenetic tree | Oryza sativa |
DNA and amino acid determination, phylogenetic tree | Tribolium castaneum |
DNA and amino acid determination, phylogenetic tree | Drosophila melanogaster |
DNA and amino acid determination, phylogenetic tree | Triticum aestivum |
DNA and amino acid determination, phylogenetic tree | Laodelphax striatellus |
DNA and amino acid determination, phylogenetic tree | Danio rerio |
DNA and amino acid determination, phylogenetic tree | Aspergillus oryzae |
DNA and amino acid determination, phylogenetic tree | Dermatophilus congolensis |
DNA and amino acid determination, phylogenetic tree, genetic structure | Homo sapiens |
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 |
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 (Comment) | Organism |
---|---|
crystal structure of neutral CDase for the ceramide-free and C2-ceramide-bound forms | Pseudomonas aeruginosa |
Protein Variants | Comment | Organism |
---|---|---|
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 |
additional information | targeted expression of neutral CDase can rescue retinal degeneration in a subset of Drosophila phototransduction mutants | Drosophila melanogaster |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
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 | - |
extracellular | the neutral ceramidase is exclusively secreted into the medium through a vesicular transport system when expressed in S2 cells | Drosophila melanogaster | - |
- |
extracellular | the neutral ceramidase is secreted | Pseudomonas aeruginosa | - |
- |
extracellular | the neutral ceramidase is secreted | Dictyostelium discoideum | - |
- |
extracellular | the neutral ceramidase is secreted | Mycobacterium tuberculosis | - |
- |
extracellular | the neutral ceramidase is secreted | Dermatophilus congolensis | - |
- |
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 | - |
lysosome | of hepatocytes | Rattus norvegicus | 5764 | - |
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 | - |
membrane | the neutral ceramidase is membrane-bound, enzyme membrane topology, overview | Homo sapiens | 16020 | - |
membrane | the neutral ceramidase is membrane-bound, enzyme membrane topology, overview | Mus musculus | 16020 | - |
membrane | the neutral ceramidase is membrane-bound, enzyme membrane topology, overview | Danio rerio | 16020 | - |
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 | - |
- |
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 | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | a calcium or magnesium ion is presumed to be important for stabilizing the two domains | Pseudomonas aeruginosa | |
Mg2+ | a calcium or magnesium ion is presumed to be important for stabilizing the two domains | Pseudomonas aeruginosa | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Dictyostelium discoideum | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Mycobacterium tuberculosis | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Oryza sativa | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Tribolium castaneum | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Rattus norvegicus | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Homo sapiens | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Drosophila melanogaster | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Mus musculus | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Triticum aestivum | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Laodelphax striatellus | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Danio rerio | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Aspergillus oryzae | |
Zn2+ | neutral CDase contains a zinc ion in the active site that functions as a catalytic center | Dermatophilus congolensis | |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus oryzae | Q5B5D5 | - |
- |
Danio rerio | Q5W7F1 | - |
- |
Dermatophilus congolensis | - |
- |
- |
Dictyostelium discoideum | - |
- |
- |
Drosophila melanogaster | Q9VA70 | - |
- |
Homo sapiens | Q9NR71 | - |
- |
Laodelphax striatellus | R4N4U2 | - |
- |
Mus musculus | Q9JHE3 | - |
- |
Mycobacterium tuberculosis | - |
- |
- |
Oryza sativa | - |
- |
- |
Pseudomonas aeruginosa | - |
- |
- |
Rattus norvegicus | Q91XT9 | - |
- |
Tribolium castaneum | - |
- |
- |
Triticum aestivum | A9YFM2 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | the enzyme contains N-glycan | Dictyostelium discoideum |
glycoprotein | the enzyme contains N-glycan | Drosophila melanogaster |
glycoprotein | the enzyme contains N-glycan | Aspergillus oryzae |
glycoprotein | the enzyme contains N-glycan and O-glycan | Rattus norvegicus |
glycoprotein | the enzyme contains N-glycan and O-glycan | Homo sapiens |
glycoprotein | the enzyme contains N-glycan and O-glycan | Mus musculus |
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 | Comment | Organism | Reaction ID |
---|---|---|---|
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | Comment | Organism | Textmining |
---|---|---|---|
brain | high expression level of neutral ceramidase | Rattus norvegicus | - |
brain | high expression level of neutral ceramidase | Homo sapiens | - |
endothelial cell | - |
Rattus norvegicus | - |
endothelial cell | - |
Mus musculus | - |
heart | high expression level of neutral ceramidase | Homo sapiens | - |
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 | - |
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 | - |
kidney | high expression level of neutral ceramidase | Homo sapiens | - |
kidney | high expression level of neutral ceramidase | Mus musculus | - |
kidney | high expression level of neutral ceramidase, at the top of themicrovilli in proximal tubule cells | Rattus norvegicus | - |
liver | high expression level of neutral ceramidase | Homo sapiens | - |
liver | high expression level of neutral ceramidase | Mus musculus | - |
additional information | neutral ceramidase is ubiquitously expressed in various mammalian tissues | Rattus norvegicus | - |
additional information | neutral ceramidase is ubiquitously expressed in various mammalian tissues | Homo sapiens | - |
additional information | neutral ceramidase is ubiquitously expressed in various mammalian tissues | Mus musculus | - |
pancreas | high expression level of neutral ceramidase | Homo sapiens | - |
S2 cell | - |
Drosophila melanogaster | - |
skeletal muscle | high expression level of neutral ceramidase | Homo sapiens | - |
small intestine | high expression level of neutral ceramidase | Rattus norvegicus | - |
small intestine | high expression level of neutral ceramidase | Homo sapiens | - |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
? | |
additional information | the enzyme can hydrolyze human skin-specific omega-hydroxyacyl ceramides | Pseudomonas aeruginosa | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
CDase | - |
Pseudomonas aeruginosa |
CDase | - |
Dictyostelium discoideum |
CDase | - |
Mycobacterium tuberculosis |
CDase | - |
Oryza sativa |
CDase | - |
Tribolium castaneum |
CDase | - |
Rattus norvegicus |
CDase | - |
Homo sapiens |
CDase | - |
Drosophila melanogaster |
CDase | - |
Mus musculus |
CDase | - |
Triticum aestivum |
CDase | - |
Laodelphax striatellus |
CDase | - |
Danio rerio |
CDase | - |
Aspergillus oryzae |
CDase | - |
Dermatophilus congolensis |
neutral CDase | - |
Rattus norvegicus |
neutral ceramidase | - |
Pseudomonas aeruginosa |
neutral ceramidase | - |
Dictyostelium discoideum |
neutral ceramidase | - |
Mycobacterium tuberculosis |
neutral ceramidase | - |
Oryza sativa |
neutral ceramidase | - |
Tribolium castaneum |
neutral ceramidase | - |
Rattus norvegicus |
neutral ceramidase | - |
Homo sapiens |
neutral ceramidase | - |
Drosophila melanogaster |
neutral ceramidase | - |
Mus musculus |
neutral ceramidase | - |
Triticum aestivum |
neutral ceramidase | - |
Laodelphax striatellus |
neutral ceramidase | - |
Danio rerio |
neutral ceramidase | - |
Aspergillus oryzae |
neutral ceramidase | - |
Dermatophilus congolensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
3 | - |
- |
Dictyostelium discoideum |
4 | 4.5 | - |
Aspergillus oryzae |
5 | 12 | - |
Tribolium castaneum |
5.7 | 6 | - |
Oryza sativa |
6 | 7 | - |
Rattus norvegicus |
6.5 | 7.5 | - |
Drosophila melanogaster |
7.5 | - |
- |
Mus musculus |
7.5 | - |
- |
Danio rerio |
7.5 | 8.5 | - |
Homo sapiens |
8 | - |
- |
Laodelphax striatellus |
8 | 9 | - |
Pseudomonas aeruginosa |
8 | 9 | - |
Mycobacterium tuberculosis |
Organism | Comment | Expression |
---|---|---|
Homo sapiens | gemcitabine downregulates the neutral ceramidase | down |
General Information | Comment | Organism |
---|---|---|
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
malfunction | KO mice are impaired in the intestinal degradation of sphingolipids | Mus musculus |
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 |
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 |
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 |
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 |
additional information | enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence and a mucin box | Mus musculus |
additional information | enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box | Pseudomonas aeruginosa |
additional information | enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box | Dictyostelium discoideum |
additional information | enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box | Oryza sativa |
additional information | enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box | Tribolium castaneum |
additional information | enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box | Triticum aestivum |
additional information | enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box | Laodelphax striatellus |
additional information | enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box | Aspergillus oryzae |
additional information | enzyme structure-function relationship, overview. The enzyme contains a signal/anchor sequence but no mucin box | Dermatophilus congolensis |
additional information | enzyme structure-function relationship, overview. The enzyme contains no signal/anchor sequence and no mucin box | Mycobacterium tuberculosis |
physiological function | neutral CDase is expressed in the intestines of humans and plays a major role in ceramide metabolism in the gut | Homo sapiens |
physiological function | neutral CDase may be involved in a pathway for the digestion of dietary sphingolipids in mice | Mus musculus |