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Literature summary for 1.3.5.1 extracted from

  • Avenot, H.F.; Sellam, A.; Karaoglanidis, G.; Michailides, T.J.
    Characterization of mutations in the iron-sulphur subunit of succinate dehydrogenase correlating with Boscalid resistance in Alternaria alternata from California pistachio (2008), Phytopathology, 98, 736-742.
    View publication on PubMed

Application

Application Comment Organism
molecular biology the relevance of modifications in Alternaria alternata AaSdhB sequence in conferring boscalid resistance is discussed Alternaria alternata

Protein Variants

Protein Variants Comment Organism
H277R the molecular basis of boscalid-resistant phenotypes in Alternaria alternata is elucidated. Furthermore, the cross-resistance pattern between boscalid and carboxin in these isolates is investigated. The iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R Alternaria alternata
H277Y the molecular basis of boscalid-resistant phenotypes in Alternaria alternata is elucidated. Furthermore, the cross-resistance pattern between boscalid and carboxin in these isolates is investigated. The iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R Alternaria alternata

Inhibitors

Inhibitors Comment Organism Structure
carboxin
-
Alternaria alternata

Metals/Ions

Metals/Ions Comment Organism Structure
3Fe-4S center the iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R Alternaria alternata

Organism

Organism UniProt Comment Textmining
Alternaria alternata
-
-
-

Synonyms

Synonyms Comment Organism
AaSdhB
-
Alternaria alternata
succinate dehydrogenase
-
Alternaria alternata