کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
4357395 1300056 2011 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Characterisation of the ArmA adenylation domain implies a more diverse secondary metabolism in the genus Armillaria
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک علوم کشاورزی و بیولوژیک (عمومی)
پیش نمایش صفحه اول مقاله
Characterisation of the ArmA adenylation domain implies a more diverse secondary metabolism in the genus Armillaria
چکیده انگلیسی

The armA-gene, encoding a tridomain enzyme reminiscent of nonribosomal peptide synthetases, was identified in the genome of the basidiomycete Armillaria mellea. Heterologously expressed enzyme and the ATP-pyrophosphate exchange assay were used for the in vitro biochemical characterisation of the ArmA adenylation domain. l-leucine was the preferred substrate, while l-threonine, l-valine, l-alanine, and l-isoleucine were turned over at lower rates (83 %, 62 %, 56 %, and 44 %, respectively). Other proteinogenic amino acids, 2-oxo acids, and benzoic acid derivatives were not accepted. As the substrate range of ArmA is incompatible with the secondary metabolites known from the genus Armillaria, our results imply greater natural product diversity in this genus. This is the first biochemical characterisation of a basidiomycete amino acid-adenylating domain, and our results may help refine computer algorithms to predict substrate specificities for basidiomycete nonribosomal peptide synthetases whose genes are discovered through genome sequencing.


► armA encodes a tridomain quinone synthetase-like enzyme in Armillaria mellea.
► ArmA primarily adenylates l-leucine.
► The ArmA signature ‘nonribosomal’ code deviates from known microbial codes.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Fungal Biology - Volume 115, Issue 8, August 2011, Pages 775–781
نویسندگان
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