Taxonomic group: fungi / Basidiomycota
(Phylum: Basidiomycota)
The structure was elucidated in this paperNCBI PubMed ID: 17850255Publication DOI: 10.1111/j.1365-2958.2007.05941.xJournal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: Bölker M <boelker
staff.uni-marburg.de;>
Institutions: Departments of Biology and Chemistry, Philipps-University Marburg, Marburg, Germany
The phytopathogenic basidiomycetous fungus Ustilago maydis secretes large amounts of the glycolipid biosurfactant ustilagic acid (UA). UA consists of 15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose at its terminal hydroxyl group. In addition, the cellobiose moiety is acetylated and acylated with a short-chain hydroxy fatty acid. We have identified a 58 kb spanning gene cluster that contains 12 open reading frames coding for most, if not all, enzymes needed for UA biosynthesis. Using a combination of genetic and mass spectrometric analysis we were able to assign functional roles to three of the proteins encoded by the gene cluster. This allowed us to propose a biosynthesis route for UA. The Ahd1 protein belongs to the family of non-haem diiron reductases and is required for alpha-hydroxylation of palmitic acid. Two P450 monooxygenases, Cyp1 and Cyp2, catalyse terminal and subterminal hydroxylation of palmitic acid. We could demonstrate that infection of tomato leaves by the plant pathogenic fungus Botrytis cinerea is prevented by co-inoculation with wild-type U. maydis sporidia. U. maydis mutants defective in UA biosynthesis were unable to inhibit B. cinerea infection indicating that UA secretion is critical for antagonistic activity.
biosynthesis, Proteomics, Ustilago, genetic methods
Structure type: oligomer ; 791.4078 [M+Na]+, 807.4028 [M+Na]+, 819.4392 [M+Na]+, 835.4345 [M+Na]+
Location inside paper: Fig. 1(A)
Compound class: glycolipid
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192
Methods: TLC, ESI-MS, biological assays, genetic methods, HPLC, centrifugation, northern analysis
Enzymes that release or process the structure: Cyp1, Cyp2, Ugt1, Uat1, Fas2, Uhd1, Ahd1
Biosynthesis and genetic data: biochemical data, genetic data
Related record ID(s): 48961
NCBI Taxonomy refs (TaxIDs): 559306,
5270
Show glycosyltransferases
There is only one chemically distinct structure:
Taxonomic group: fungi / Basidiomycota
(Phylum: Basidiomycota)
The structure was elucidated in this paperNCBI PubMed ID: 17850255Publication DOI: 10.1111/j.1365-2958.2007.05941.xJournal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: Bölker M <boelker
staff.uni-marburg.de;>
Institutions: Departments of Biology and Chemistry, Philipps-University Marburg, Marburg, Germany
The phytopathogenic basidiomycetous fungus Ustilago maydis secretes large amounts of the glycolipid biosurfactant ustilagic acid (UA). UA consists of 15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose at its terminal hydroxyl group. In addition, the cellobiose moiety is acetylated and acylated with a short-chain hydroxy fatty acid. We have identified a 58 kb spanning gene cluster that contains 12 open reading frames coding for most, if not all, enzymes needed for UA biosynthesis. Using a combination of genetic and mass spectrometric analysis we were able to assign functional roles to three of the proteins encoded by the gene cluster. This allowed us to propose a biosynthesis route for UA. The Ahd1 protein belongs to the family of non-haem diiron reductases and is required for alpha-hydroxylation of palmitic acid. Two P450 monooxygenases, Cyp1 and Cyp2, catalyse terminal and subterminal hydroxylation of palmitic acid. We could demonstrate that infection of tomato leaves by the plant pathogenic fungus Botrytis cinerea is prevented by co-inoculation with wild-type U. maydis sporidia. U. maydis mutants defective in UA biosynthesis were unable to inhibit B. cinerea infection indicating that UA secretion is critical for antagonistic activity.
biosynthesis, Proteomics, Ustilago, genetic methods
Structure type: oligomer ; 791.4111 [M+Na]+, 819.4439 [M+Na]+
C
30H
54O
15, C
30H
54O
16Location inside paper: Fig. 1(A), table 2
Compound class: glycolipid
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192
Methods: TLC, ESI-MS, biological assays, genetic methods, HPLC, centrifugation, northern analysis
Biosynthesis and genetic data: biochemical data, genetic data
Related record ID(s): 48960
NCBI Taxonomy refs (TaxIDs): 559306
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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