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Information on EC 3.5.1.23 - ceramidase and Organism(s) Danio rerio
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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: Danio rerio
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
-
-
-
-
glycosphingolipid ceramide deacylase
-
-
-
-
N-acylsphingosine amidohydrolase
-
-
-
-
neutral ceramidase
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
4-nitrobenzo-2-oxa-1,3-diazole-C12-ceramide + H2O
4-nitrobenzo-2-oxa-1,3-diazole-dodecanoic acid + ceramide
-
-
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
neutral CDase contains a zinc ion in the active site that functions as a catalytic center
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
a strong signal for neutral CDase is detected in zebrafish intestine at the luminal surface of the villi and microvilli of adsorptive epithelial cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the neutral ceramidase is membrane-bound, enzyme membrane topology, overview
-
type II integral protein with its N-terminal end anchored to the plasma membrane and C-terminal end exposed to the extracellular space
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
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
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
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). ACER1_DANRE
266
7
30908
Swiss-Prot
other Location (Reliability: 4)
ASAH2_DANRE
743
1
82069
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A2R8QL79_DANRE
387
0
44481
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8M1P6A3_DANRE
267
7
30898
TrEMBL
other Location (Reliability: 2)
Q5XJR7_DANRE
390
0
44629
TrEMBL
Secretory Pathway (Reliability: 1)
F1Q7Z4_DANRE
390
0
44717
TrEMBL
Secretory Pathway (Reliability: 1)
A8E524_DANRE
390
0
44751
TrEMBL
Secretory Pathway (Reliability: 1)
Q6PH71_DANRE
395
1
44681
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
-
x * 110000, glycosylated recombinant enzyme, SDS-PAGE, x * 82500, deglycosylated recombinant enzyme, SDS-PAGE
82500
-
x * 110000, glycosylated recombinant enzyme, SDS-PAGE, x * 82500, deglycosylated recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 110000, glycosylated recombinant enzyme, SDS-PAGE, x * 82500, deglycosylated recombinant enzyme, SDS-PAGE
?
x * 44000, about, sequence calculation, x * 50000, about, recombinant glycosylated enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
the zebrafish enzyme is subjected to proteolytic cleavage during maturation, the enzyme has autoproteolytic activity
glycoprotein
-
eight potential N-glycosylation sites, four potential O-glycosylation sites
glycoprotein
the enzyme contains N-glycan and O-glycan, the intestinal enzyme is glycosylated with complex-type N-glycans and O-glycans
glycoprotein
six N-glycosylation sites at amino acid positions 173, 259, 286, 301, 342, and 348, and a single O-glycosylation site at positions 344 present on the beta-subunit are determined in the zebrafish sequence. The alpha-subunit does not have any putative glycosylation site. The recombinant enzyme is glycosylated at the beta-subunit. Deglycosylation by PNGase F
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme knockout, via antisense construct using three different antisense morpholino oligonucleotides (AMOs 1, 2, and 3) that are designed based on sequences at different sites of the 5'-untranslated region, leads to an increase in the number of zebrafish embryos with severe morphological qand cellular abnormalities such as abnormal morphogenesis inhead and tail, pericardiac edema, defect of blood cell circulation, and an increase in apoptotic cells, phenotype, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged enzyme from Pichia pastoris strain GS115 by nickel affinity chromatography, ultrafiltration, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, overexpression of C-terminally myc-tagged enzyme in CHOP cells and zebrafish BRF41 cells in endoplasmic reticulum and Golgi apparatus, as well as in plasma membranes
-
gene asah1b, DNA and amino acid sequence determination and analysis, recombinant overexpression of C-terminally His-tagged enzyme in Pichia pastoris strain GS115, method optimization, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshimura, Y.; Tani, M.; Okino, N.; Iida, H.; Ito, M.
Molecular cloning and functional analysis of zebrafish neutral ceramidase
J. Biol. Chem.
279
44012-44022
2004
Danio rerio
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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