کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
9951564 1416960 2018 26 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Cloning and characterization of a new delta-specific l-leucine dioxygenase from Anabaena variabilis
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Cloning and characterization of a new delta-specific l-leucine dioxygenase from Anabaena variabilis
چکیده انگلیسی
Optically pure hydroxy amino acids show several bioactivities and are valuable building blocks for the pharmaceutical industry. Fe(II)/α-ketoglutarate dependent dioxygenases catalyze the hydroxylation or sulfoxidation of l-amino acids with high regio- and stereoselectivity. While several β- and γ-specific enzymes have been described, only one δ-specific hydroxylase has been reported so far. Based on its similarity to the known l-leucine 5-hydroxylase from Nostoc punctiforme, an open reading frame from the cyanobacterium Anabaena variabilis was identified as putative l-leucine dioxygenase (AvLDO). Here we report the cloning and characterization of this dioxygenase. The enzyme showed a high preference for acidic conditions and moderate reaction temperatures. AvLDO catalyzed the regio- and stereoselective hydroxylation of several aliphatic amino acids in δ-position. In case of the sulfoxidation of l-methionine, AvLDO produced the opposite diastereomer than isoleucine dioxygenase. AvLDO is thus an interesting addition to the toolbox of Fe(II)/α-ketoglutarate dependent dioxygenases. On the genomic DNA of Anabaena variabilis ATCC 29413, the avldo gene is located on a gene cluster involved (2S,4S)-4-methylproline biosynthesis, which is contained in bioactive peptides often found from cyanobacteria. This fact suggests the metabolic functional role of this amino acid dioxygenase in cyanobacteria.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Biotechnology - Volume 284, 20 October 2018, Pages 68-74
نویسندگان
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