کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
6451156 1361329 2017 12 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Research review paperBreaking the mirror: l-Amino acid deaminase, a novel stereoselective biocatalyst
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Research review paperBreaking the mirror: l-Amino acid deaminase, a novel stereoselective biocatalyst
چکیده انگلیسی


- Enantiomerically pure amino acids (AA) are of increasing interest for the industries.
- d-Amino acid oxidase-catalyzed deracemization of a dl-solution produces the l-AA.
- Isolation of d-AAs was hampered by the lack of a suitable l-amino acid oxidase activity.
- l-Amino acid deaminase represents a suitable alternative.
- Its structure has been recently solved and protein engineering studies performed.

Enantiomerically pure amino acids are of increasing interest for the fine chemical, agrochemicals and pharmaceutical industries. During past years l-amino acids have been produced from deracemization of dl-solution employing the stereoselective flavoenzyme d-amino acid oxidase. On the other hand, the isolation of corresponding d-isomer was hampered by the scarce availability of a suitable l-amino acid oxidase activity. On this side, l-amino acid deaminase (LAAD), only present in the Proteus bacteria, represents a suitable alternative. This FAD-containing enzyme catalyzes the deamination of l-amino acids to the corresponding α-keto acids and ammonia, with no hydrogen peroxide production (a potentially dangerous oxidizing species) since the electrons of the reduced cofactor are transferred to a membrane-bound cytochrome. Very recently the structure of LAAD has been solved: in addition to a FAD-binding domain and to a substrate-binding domain, it also possesses an N-terminal putative transmembrane α-helix (residues 8-27, not present in the crystallized protein variant) and a small α + β subdomain (50-67 amino acids long, named “insertion module”) strictly interconnected to the substrate binding domain. Structural comparison showed that LAAD resembles the structure of several soluble amino acid oxidases, such as l-proline dehydrogenase, glycine oxidase or sarcosine oxidase, while only a limited structural similarity with d- or l-amino acid oxidase is apparent. In this review, we present an overview of the structural and biochemical properties of known LAADs and describe the advances that have been made in their biotechnological application also taking advantage from improved variants generated by protein engineering studies.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biotechnology Advances - Volume 35, Issue 6, 1 November 2017, Pages 657-668
نویسندگان
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