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Information on EC 3.5.1.23 - ceramidase and Organism(s) Drosophila melanogaster and UniProt Accession Q9VA70
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3.5.1.23 ceramidaseSpecify your search results
Word Map
- 3.5.1.23
-
adipor1
- sphingolipids
- obesity
-
adipokine
- agonist
- sphingomyelinase
- sphingomyelin
- lysosomal
- farber
-
obese
- leptin
- adipocytes
-
amp-activated
- sphingosine-1-phosphate
- peroxisome
- cardiovascular
-
proliferator-activated
- triglyceride
-
globular
-
insulin-sensitizing
-
high-fat
- tnf
- smases
-
adipocytokine
-
adipocyte-derived
-
monophosphate-activated
-
anti-atherogenic
-
t-cadherin
- steatosis
-
adiposity
- glucosylceramide
- glycosphingolipids
-
obesity-related
-
antidiabetic
- 1-phosphate
-
seven-transmembrane
- gaucher
- dihydrosphingosine
-
p-ampk
- palmitoyltransferase
-
homa-ir
-
sphingoid
- hoarseness
-
ceramide-induced
- sphinganine
-
ceramide-mediated
- dihydroceramide
-
myoclonic
-
adipocyte-secreted
- analysis
- pharmacology
- drug development
- medicine
-
hypoadiponectinemia
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
adipor2, adiponectin receptor, ceramidase, acid ceramidase, asah1, neutral ceramidase, acdase, ncdase, acer2, acer3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acylsphingosine deacylase
-
-
-
-
CDase
-
CDase is the only functional ceramidase present in Drosophila
Dacer
glycosphingolipid ceramide deacylase
-
-
-
-
N-acylsphingosine amidohydrolase
-
-
-
-
PHP32
-
-
-
-
Putative 32 KDA heart protein
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
N-acylsphingosine amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
37289-06-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
C12-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + H2O
?
substrate activity assay
-
-
?
palmitoyl sphingosine + H2O
palmitate + sphingosine
substrate activity assay
-
-
?
ceramide + H2O
sphingosine + fatty acid
ceramidase activity on D-e-C6, D-e-C12, D-e-C16, D-e-C18, and D-e-C24:1-ceramide
-
-
?
additional information
?
-
ceramidases are a group of enzymes that catalyze the hydrolysis of ceramides to generate sphingosine, which is phosphorylated to form sphingosine 1-phosphate
-
-
?
additional information
?
-
-
ceramidases are a group of enzymes that catalyze the hydrolysis of ceramides to generate sphingosine, which is phosphorylated to form sphingosine 1-phosphate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
ceramidases are a group of enzymes that catalyze the hydrolysis of ceramides to generate sphingosine, which is phosphorylated to form sphingosine 1-phosphate
-
-
?
additional information
?
-
-
ceramidases are a group of enzymes that catalyze the hydrolysis of ceramides to generate sphingosine, which is phosphorylated to form sphingosine 1-phosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Bac-Dacer microsomes cause a twofold increase in ceramidase activity on D-e-C6, D-e-C12, D-e-C16, D-e-C18, and D-e-C24:1-ceramide at pH 9.0
-
additional information
-
Bac-Dacer microsomes cause a twofold increase in ceramidase activity on D-e-C6, D-e-C12, D-e-C16, D-e-C18, and D-e-C24:1-ceramide at pH 9.0
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00125
CDase null mutant and CDase null expressing fat body driven CDase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the neutral ceramidase is exclusively secreted into the medium through a vesicular transport system when expressed in S2 cells
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
malfunction
a Dacer-deficient Drosophila melanogaster mutant has higher catalase (CAT) activity and CAT transcription level, leading to higher resistance to oxidative stress induced by paraquat. Altered antioxidative activity in Dacer mutant might be responsible for increased oxidative stress resistance. Quantitative proteomic analysis of wild-type and mutant cells. Three oxidoreductases, including two cytochrome P450 (CG3050, CG9438) and an oxoglutarate/iron-dependent dioxygenase (CG17807), are most significantly upregulated in the Dacer overexpressing mutant
metabolism
Dacer plays a role in fly development and longevity by controlling the metabolism of ceramides
physiological function
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
physiological function
Dacer plays a role in fly development and longevity by controlling the metabolism of ceramides. Dacer inactivation delays Drosophila pre-adult development, while Dacer inactivation increases Drosophila lifespan
physiological function
enzyme Dacer regulates expression of oxidative stress proteins
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NCASE_DROME
704
1
78232
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
targeted expression of neutral CDase can rescue retinal degeneration in a subset of Drosophila phototransduction mutants
additional information
insertional mutagenesis leading to enzyme inactivation, transposon location of the dacer mutant, overview. The mutation increases the levels of ceamides in both the pupal and adult stages, and increases pre-adult development time, lifespan, and anti-oxidative stress capacity, overview
additional information
-
insertional mutagenesis leading to enzyme inactivation, transposon location of the dacer mutant, overview. The mutation increases the levels of ceamides in both the pupal and adult stages, and increases pre-adult development time, lifespan, and anti-oxidative stress capacity, overview
additional information
generation of a Dacer-deficient Drosophila melanogaster mutant, which has higher catalase (CAT) activity and CAT transcription level, leading to higher resistance to oxidative stress induced by paraquat, quantitative proteomic analysis of wild-type and mutant cells. Three oxidoreductases, including two cytochrome P450 (CG3050, CG9438) and an oxoglutarate/iron-dependent dioxygenase (CG17807), are most significantly upregulated in the Dacer overexpressing mutant. Altered antioxidative activity in Dacer mutant might be responsible for increased oxidative stress resistance
additional information
-
generation of a Dacer-deficient Drosophila melanogaster mutant, which has higher catalase (CAT) activity and CAT transcription level, leading to higher resistance to oxidative stress induced by paraquat, quantitative proteomic analysis of wild-type and mutant cells. Three oxidoreductases, including two cytochrome P450 (CG3050, CG9438) and an oxoglutarate/iron-dependent dioxygenase (CG17807), are most significantly upregulated in the Dacer overexpressing mutant. Altered antioxidative activity in Dacer mutant might be responsible for increased oxidative stress resistance
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the Dacer/brainwashing or BWA gene CG13969 localizes to the 38B2-3 region of the left arm of the second chromosome, DNA and amino acid sequence determination and analysis, functional overexpression in High Five insect cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Acharya, J.K.; Dasgupta, U.; Rawat, S.S.; Yuan, C.; Sanxaridis, P.D.; Yonamine, I.; Karim, P.; Nagashima, K.; Brodsky, M.H.; Tsunoda, S.; Acharya, U.
Cell-nonautonomous function of ceramidase in photoreceptor homeostasis
Neuron
57
69-79
2008
Drosophila melanogaster (Q9VA70)
Yang, Q.; Gong, Z.J.; Zhou, Y.; Yuan, J.Q.; Cheng, J.; Tian, L.; Li, S.; Lin, X.D.; Xu, R.; Zhu, Z.R.; Mao, C.
Role of Drosophila alkaline ceramidase (Dacer) in Drosophila development and longevity
Cell. Mol. Life Sci.
67
1477-1490
2010
Drosophila melanogaster (Q9VIP7), Drosophila melanogaster, Drosophila melanogaster BL-18012 (Q9VIP7)
Yuan, C.; Rao, R.P.; Jesmin, N.; Bamba, T.; Nagashima, K.; Pascual, A.; Preat, T.; Fukusaki, E.; Acharya, U.; Acharya, J.K.
CDase is a pan-ceramidase in Drosophila
Mol. Biol. Cell
22
33-43
2011
Drosophila melanogaster
Ito, M.; Okino, N.; Tani, M.
New insight into the structure, reaction mechanism, and biological functions of neutral ceramidase
Biochim. Biophys. Acta
1841
682-691
2014
Dictyostelium discoideum, Mycobacterium tuberculosis, Oryza sativa, Pseudomonas aeruginosa, Tribolium castaneum, Dermatophilus congolensis, Triticum aestivum (A9YFM2), Aspergillus oryzae (Q5B5D5), Danio rerio (Q5W7F1), Rattus norvegicus (Q91XT9), Mus musculus (Q9JHE3), Homo sapiens (Q9NR71), Drosophila melanogaster (Q9VA70), Laodelphax striatellus (R4N4U2)
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