Information on EC 2.1.1.317 - sphingolipid C9-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.317
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RECOMMENDED NAME
GeneOntology No.
sphingolipid C9-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide = S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:(4E,8E)-sphinga-4,8-dienine ceramide C-methyltransferase
The enzyme, characterized from the fungi Komagataella pastoris and Fusarium graminearum, acts only on ceramides and has no activity with free sphingoid bases or glucosylceramides.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mts1
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Manually annotated by BRENDA team
genes FgMT1 and FgMT2
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Manually annotated by BRENDA team
genes FgMT1 and FgMT2
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Manually annotated by BRENDA team
i.e. Pichia pastoris
Q2QJ12
UniProt
Manually annotated by BRENDA team
i.e. Pichia pastoris
Q2QJ12
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide
S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide
S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, genetic organization and clustering of SAM-dependent methyltransferase sequences, phylogenetic tree, recombinant enzyme functional expression in a Saccharomyces cerevisiae strain that is engineered to produce glucosylceramides suitable as a substrate for C9-methylation. C9-methylated sphingolipids are detected in the transformed strain expressing the candidate from Pichia pastoris, demonstrating its function as a sphingolipid C9-methyltransferase
Q2QJ12
gene mts1, orf19.4831, cloning in Escherichia coli strain DH5alpha
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genes FgMT1 and FgMT2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in and complementation of an enzyme knockout mutant strain C-9-MT-null of Pichia pastoris
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information