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Information on EC 3.5.1.23 - ceramidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38298

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.23 ceramidase
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P38298 not found.
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkaline ceramidase
-
yeast phyto-ceramidase 1
-
acylsphingosine deacylase
-
-
-
-
alkaline ceramidase
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glycosphingolipid ceramide deacylase
-
-
-
-
N-acylsphingosine amidohydrolase
-
-
-
-
PHP32
-
-
-
-
Putative 32 KDA heart protein
-
-
-
-
yeast dihydroceramidase 1
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
N-acylsphingosine amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37289-06-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acylsphingosine + H2O
carboxylate + sphingosine
show the reaction diagram
N-acylsphingosine + H2O
carboxylate + sphingosine
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acylsphingosine + H2O
carboxylate + sphingosine
show the reaction diagram
the carboxylate is a fatty acid
-
-
r
N-acylsphingosine + H2O
carboxylate + sphingosine
show the reaction diagram
the carboxylate is a fatty acid
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene YPC1
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the N- and C-terminal ends of Ypc1p are oriented towards the lumen and cytosol, respectively, cytosolic or lumenal loops
Manually annotated by BRENDA team
enzyme membrane topology, overview
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the CREST superfamily
malfunction
overexpression of Ypc1p protein significantly increases the levels of free long-chain bases and long-chain base-phosphates and reduces the biosynthetic flow of long-chain bases towards mature sphingolipids, whereas deletion of gene YPC1 causes a significant increase in mature sphingolipids
evolution
the enzyme belongs to the CREST superfamily
malfunction
overexpression of Ydc1p protein significantly increases the levels of free long-chain bases and long-chain base-phosphates and reduces the biosynthetic flow of long-chain bases towards mature sphingolipids
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G124C
site-directed mutagenesis
G235C
site-directed mutagenesis
K157C
site-directed mutagenesis
K67C
site-directed mutagenesis
K91C
site-directed mutagenesis
L65C
site-directed mutagenesis
N123C
site-directed mutagenesis
N158C
site-directed mutagenesis
R93C
site-directed mutagenesis
S197C
site-directed mutagenesis
S293C
site-directed mutagenesis
S297C
site-directed mutagenesis
T181C
site-directed mutagenesis
T98C
site-directed mutagenesis
V185C
site-directed mutagenesis
V236C
site-directed mutagenesis
Y182C
site-directed mutagenesis
Y184C
site-directed mutagenesis
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene YPC, recombinant expression of HA7-tagged enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ramachandra, N.; Conzelmann, A.
Membrane topology of yeast alkaline ceramidase YPC1
Biochem. J.
452
585-594
2013
Saccharomyces cerevisiae (P38298), Saccharomyces cerevisiae (Q02896), Saccharomyces cerevisiae
Manually annotated by BRENDA team