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Information on EC 4.1.2.27 - sphinganine-1-phosphate aldolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q05567

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.27 sphinganine-1-phosphate aldolase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q05567
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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, Archaea, Bacteria
Synonyms
s1p lyase, sgpl1, sphingosine-1-phosphate lyase, s1p-lyase, sphingosine phosphate lyase, sphingosine 1-phosphate lyase, legs2, dpl1p, sphinganine-1-phosphate lyase, sphinganine 1-phosphate lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sphinganine-1-phosphate aldolase
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sphinganine-1-phosphate lyase
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aldolase, dihydrosphingosine 1-phosphate
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Dihydrosphingosine 1-phosphate aldolase
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sphinganine 1-phosphate lyase
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sphinganine-1-phosphate aldolase
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sphinganine-1-phosphate-alkanal-lyase
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sphingosine-1-phosphate lyase
sphingosine-phosphate lyase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde
show the reaction diagram
enzyme is stereospecific for the D-erythro sphingoid base
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
sphinganine-1-phosphate palmitaldehyde-lyase (phosphoethanolamine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
37290-61-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
show the reaction diagram
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ir
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
show the reaction diagram
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D(+)-erythro-dihydrosphingosine-1-phosphate
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?
sphingosine 1-phosphate
phosphoethanolamine + (2E)-hexadecenal
show the reaction diagram
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ir
additional information
?
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enzyme catalyzes a rate-limiting step in sphingolipid catabolism
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?
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
sphinganine 1-phosphate
phosphoethanolamine + palmitaldehyde
show the reaction diagram
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ir
additional information
?
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enzyme catalyzes a rate-limiting step in sphingolipid catabolism
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxydihydrosphingosine 1-phosphonate
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2-acetyl-4-tetrahydroxybutyl-imidazole
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2-acetyl-4-tetrahydroxybutylimidazole
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2-vinyldihydro-sphingosine 1-phosphate
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FTY720
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also called fingolimod
threo-dihydro-sphingosine 1-phosphate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65520
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calculation from sequence of genomic DNA
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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x-ray crystallography
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C344A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
C65L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
C65L/K67L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
C65L/K67L/S70L/N71L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-16
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-31
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-31/C65L/K67L/S70L/N71L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-54
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-57
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
DELTA1-81
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
H268A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
H340A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
K380A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
K386A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
K67L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
K67L/S70L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
N6A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
N71L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
S70L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
S70L/N71L
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
Y554A
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
Y554F
mutant constructed for structure-function analysis of Dpl1p to discover possible modes of regulation
H129A
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the mutation drastically impairs enzyme activity
Y105F
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inactive
Y174F
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the mutant is partially active
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
FLAG-tagged purification is performed
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the plasmids pRS415, pRS416 and pESC are used
expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saba, J.D.; Nara, F.; Bielawska, A.; Garrett, S.; Hannun, Y.A.
The BST1 gene of Saccharomyces cerevisiae is the sphingosine-1-phosphate lyase
J. Biol. Chem.
272
26087-26090
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mukhopadhyay, D.; Howell, K.S.; Riezman, H.; Capitani, G.
Identifying key residues of sphinganine-1-phosphate lyase for function in vivo and in vitro
J. Biol. Chem.
283
20159-20169
2008
Saccharomyces cerevisiae (Q05567)
Manually annotated by BRENDA team
Bourquin, F.; Capitani, G.; Gruetter, M.G.
PLP-dependent enzymes as entry and exit gates of sphingolipid metabolism
Protein Sci.
20
1492-1508
2011
Saccharomyces cerevisiae, Homo sapiens, Myxococcus xanthus, Symbiobacterium thermophilum
Manually annotated by BRENDA team
Bourquin, F.; Riezman, H.; Capitani, G.; Gruetter, M.G.
Structure and function of sphingosine-1-phosphate lyase, a key enzyme of sphingolipid metabolism
Structure
18
1054-1065
2010
Saccharomyces cerevisiae, Homo sapiens (O95470), Homo sapiens, Symbiobacterium thermophilum (Q67PY4), Symbiobacterium thermophilum
Manually annotated by BRENDA team