Bacillus anthracis ω-amino acid:pyruvate transaminase employs a different mechanism for dual substrate recognition than other amine transaminases-Reference-Cited by-同舟云学术

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Bacillus anthracis ω-amino acid:pyruvate transaminase employs a different mechanism for dual substrate recognition than other amine transaminases

Published:2016-01-21 Issue:10 Volume:100 Page:4511-4521
ISSN:0175-7598
Container-title:Applied Microbiology and Biotechnology
language:en
Short-container-title:Appl Microbiol Biotechnol

Author:

Steffen-Munsberg Fabian,Matzel Philipp,Sowa Miriam A.,Berglund Per,Bornscheuer Uwe T.,Höhne Matthias

Funder

Fonds der Chemischen Industrie

European Union KBBE-2011-5

Seventh Framework Programme

Publisher

Springer Science and Business Media LLC

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s00253-015-7275-9.pdf

Reference36 articles.

1. Bommer M, Ward JM (2013) A 1-step microplate method for assessing the substrate range of L-α-amino acid aminotransferase. Enzyme Microb Tech 52:218–225. doi: 10.1016/j.enzmictec.2013.02.007

2. Cassimjee KE, Manta B, Himo F (2015) A quantum chemical study of the ω-transaminase reaction mechanism. Org Biomol Chem 13:8453–8464. doi: 10.1039/c5ob00690b

3. Crismaru CG, Wybenga GG, Szymanski W, Wijma HJ, Wu B, Bartsch S, de Wildeman S, Poelarends GJ, Feringa BL, Dijkstra BW, Janssen DB (2013) Biochemical properties and crystal structure of a β-phenylalanine aminotransferase from Variovorax paradoxus. Appl Environ Microbiol 79:185–195. doi: 10.1128/aem.02525-12

4. Davies MT (1959) A universal buffer solution for use in ultra-violet spectrophotometry. Analyst 84:248–251. doi: 10.1039/an9598400248

5. Dey S, Lane JM, Lee RE, Rubin EJ, Sacchettini JC (2010) Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase. Biochemistry 49:6746–6760. doi: 10.1021/bi902097j

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