Examination of Substrate Specificity of the First Adenylation Domain in mcyA Module Involved in Microcystin Biosynthesis

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dc.contributor.authorYaman, Gözde
dc.contributor.authorYılmaz, Mete
dc.date.accessioned2024-10-30T06:25:41Z
dc.date.available2024-10-30T06:25:41Z
dc.date.issued2020
dc.departmentBTÜ
dc.description.abstractThe cyanotoxin microcystin (MC) is a secondary metabolite, synthesized by nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) enzymes. It has many isoforms and the mechanism of its diversity is not well understood. One of the MC synthetase genes, mcyA, codes for the McyA module containing two adenylation (A) domains. The first domain, McyA-A1, generally binds to L-serine (L-ser). Then the N-methyl transferase (NMT) domain converts L-Ser into N-methyldehydroalanine (Mdha), which usually occupies position 7 on the MC molecule. However, various other amino acids (AAs) might also be present at this position. In this study, bioinformatic analyses of selected cyanobacteria were performed to understand whether genetic information in the first adenylation domain of mcyA could explain incorporation of different AAs at position 7 of the MC molecule. Binding pocket signatures of McyA-A1 and putative activated AAs were determined via various bioinformatics tools. Maximum likelihood phylogenetic trees of full length mcyA, mcyA-A1 and 16S rRNA genes were prepared in Mega 6. Phylogenetic analysis of mcyA-A1 nucleotide sequences was in agreement with the predictions of activated AAs by McyA-A1. In comparison with the 16S rRNA and full length mcyA gene trees, mcyA-A1 phylogenetic trees suggested horizontal transfer of the A domain in either Planktothrix agardhii (Gomont) Anagnostidis & Komárek or Planktothrix rubescens (De Candolle ex Gomont) Anagnostidis & Komárek strains. Predictions of activated AAs were generally in agreement with the chemically determined position 7 AAs. However, there were exceptions suggesting the multispecificity of the first A domain of McyA in some cyanobacteria.
dc.identifier10.21448/ijsm.715530
dc.identifier.doi10.21448/ijsm.715530
dc.identifier.endpage285
dc.identifier.issn21486905
dc.identifier.issue4
dc.identifier.scopusqualityQ4
dc.identifier.startpage275
dc.identifier.urihttps://hdl.handle.net/20.500.12885/2676
dc.identifier.volume7
dc.institutionauthorYaman, Gözde
dc.institutionauthorYılmaz, Mete
dc.institutionauthoridhttps://orcid.org/0000-0001-6044-3194
dc.institutionauthoridhttps://orcid.org/0000-0002-0982-727X
dc.language.isoen
dc.publisherPamukkale University
dc.relation.ispartofInternational Journal of Secondary Metabolite
dc.relation.ispartofseriesInternational Journal of Secondary Metabolite
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Öğrenci
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectMicrocystin
dc.subjectNonribosomal Peptides
dc.subjectPolyketide Synthase
dc.subjectAdenylation Domain
dc.subjectBioinformatics
dc.titleExamination of Substrate Specificity of the First Adenylation Domain in mcyA Module Involved in Microcystin Biosynthesis
dc.typeArticle
oaire.citation.issue4
oaire.citation.volume7

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