Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.23 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

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(Commentary)

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 (Commentary)

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

Protein Variants

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

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

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/ Products (Substrates)

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

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

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

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

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 and Products (Substrate)

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

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

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

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

Expression

Organism Comment Expression
Homo sapiens gemcitabine downregulates the neutral ceramidase down

General Information

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