2.1.1.317: sphingolipid C9-methyltransferase
This is an abbreviated version!
For detailed information about sphingolipid C9-methyltransferase, go to the full flat file.
Reaction
Synonyms
C9-methyltransferase for sphingolipid 1, MTS1, SMT1, smtA, SmtB
ECTree
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General Information
General Information on EC 2.1.1.317 - sphingolipid C9-methyltransferase
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evolution
malfunction
metabolism
physiological function
additional information
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C-9-methylated glucosylceramides (GlcCers) are sphingolipids unique to fungi
evolution
Q2QJ12
the enzyme belongs to the superfamily of S-adenosylmethionine-dependent methyltransferases and shows highest sequence similarity to plant and bacterial cyclopropane fatty acid synthases, genetic organization and clustering of SAM-dependent methyltransferase sequences, phylogenetic profiling of SAM-dependent methyltransferases, overview
evolution
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the enzyme belongs to the superfamily of S-adenosylmethionine-dependent methyltransferases and shows highest sequence similarity to plant and bacterial cyclopropane fatty acid synthases, genetic organization and clustering of SAM-dependent methyltransferase sequences, phylogenetic profiling of SAM-dependent methyltransferases, overview
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evolution
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C-9-methylated glucosylceramides (GlcCers) are sphingolipids unique to fungi
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Q2QJ12
a Pichia pastoris knock-out strain of the sphingolipid C9-methyltransferase lacks C9-methylated glucosylceramides
malfunction
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the Candida albicans mts1 disruptant had a decreased hyphal growth rate compared to the wild-type strain. The mts1 disruptant grows similarly to wild-type in medium containing SDS or fluconazole. The membrane structure of the mts1 disruptant is not disturbed, mutant phenotype, overview
malfunction
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the DELTAFgmt2 mutant exhibits severe growth defects and produces abnormal conidia, while the DELTAFgmt1 mutant grows like the wild-type strain. The DELTAFgmt2 mutant is less virulent on different host plants tested than the previously characterized DELTAFggcs1 mutant, which lacks GlcCer synthase activity and produces no GlcCer at all. Moreover, the DELTAFgmt1 and DELTAFgmt2 mutants retain sensitivity to the antifungal plant defensins MsDef1 and RsAFP2
malfunction
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DELTAsmt1 mutants lacking the sphingolipid C9 methyltransferase gene (SMT1) are attenuated in virulence and have a growth defect at 37 °C, in neutral/alkaline pH and 5 % CO2 environments
malfunction
increased levels of unmethylated glucosylceramide are observed in smtA mutants. DELTAsmtA and wild-type cells show a similar 9-methyl-glucosylceramide content
malfunction
increased levels of unmethylated glucosylceramide are observed in smtB mutants. DELTAsmtB cells show activity reduced by 50%. The compromised 9-methyl-glucosylceramide production in the DELTAsmtB strain is not accompanied by reduced filamentation or defects in cell polarity
malfunction
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a Pichia pastoris knock-out strain of the sphingolipid C9-methyltransferase lacks C9-methylated glucosylceramides
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malfunction
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the DELTAFgmt2 mutant exhibits severe growth defects and produces abnormal conidia, while the DELTAFgmt1 mutant grows like the wild-type strain. The DELTAFgmt2 mutant is less virulent on different host plants tested than the previously characterized DELTAFggcs1 mutant, which lacks GlcCer synthase activity and produces no GlcCer at all. Moreover, the DELTAFgmt1 and DELTAFgmt2 mutants retain sensitivity to the antifungal plant defensins MsDef1 and RsAFP2
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the enzyme is part of the C-9-methylated glucosylceramides biosynthesis pathway, overview
metabolism
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the enzyme is part of the C-9-methylated glucosylceramides biosynthesis pathway, overview
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C9-methylated glucosylceramide is a fungus-specific sphingolipid. This lipid is a major membrane component in the cell and is thought to play important roles in the growth and virulence of several fungal species. The enzyme is involved in hyphal elongation. The C9-methyl group of a long-chain base in glucosylceramides plays an important role in the hyphal elongation of Candida albicans independent of lipid membrane disruption
physiological function
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sphingolipid C-9 methyltransferases seem to be essential in the organism, they are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum. Isozyme FgMT2 encodes a sphingolipid C-9 methyltransferase that is capable of methylating C-9-methylated glucosylceramides in the absence of the FgMT1-encoded enzyme and that isozyme FgMT2 is the predominant sphingolipid C-9 methyltransferases for methylating C-9-methylated glucosylceramides
physiological function
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the enzyme adds a methyl group to position nine of the sphingosine backbone of ceramide. The sphingolipid glucosylceramide and factors involved in the fungal GlcCer pathways are an integral part of fungal virulence, especially in fungal replication at 37 °C, in neutral/alkaline pH and 5 % CO2 environments (e.g. alveolar spaces)
physiological function
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sphingolipid C-9 methyltransferases seem to be essential in the organism, they are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum. Isozyme FgMT2 encodes a sphingolipid C-9 methyltransferase that is capable of methylating C-9-methylated glucosylceramides in the absence of the FgMT1-encoded enzyme and that isozyme FgMT2 is the predominant sphingolipid C-9 methyltransferases for methylating C-9-methylated glucosylceramides
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Q2QJ12
analysis of the sphingoid base composition of wild-type strains and Saccharomyces cerevisiae strain recombinantly expressing the enzyme
additional information
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analysis of the sphingoid base composition of wild-type strains and Saccharomyces cerevisiae strain recombinantly expressing the enzyme
additional information
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the C-9 methyl group is not a critical structural feature of the GlcCer receptor required for the antifungal action of plant defensins
additional information
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analysis of the sphingoid base composition of wild-type strains and Saccharomyces cerevisiae strain recombinantly expressing the enzyme
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additional information
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the C-9 methyl group is not a critical structural feature of the GlcCer receptor required for the antifungal action of plant defensins
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