Revealing the Structural Basis of Promiscuous Amine Transaminase Activity. Issue 1 (8th November 2012)

• Record Type: Journal Article
• Authors: Steffen‐Munsberg, Fabian; Vickers, Clare; Thontowi, Ahmad; Schätzle, Sebastian; Meinhardt, Tina; Svedendahl Humble, Maria; Land, Henrik; Berglund, Per; Bornscheuer, Uwe T.; Höhne, Matthias
• Is Part Of: ChemCatChem. Volume 5:Issue 1(2013:Jan.)
• Page Start: 154
• Page End: 157
• Publication Date: 2012-11-08
• Subjects: Catalysis -- Periodicals; 541.39505
• DOI: 10.1002/cctc.201200545
• Languages: English
• ISSNs: 1867-3880

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>One lock for different keys:</bold> A flexible arginine in the active site allows γ‐aminobutyrate:pyruvate transaminases to bind the chemically different substrates <sc>L</sc>‐alanine and γ‐aminobutyric acid. Moreover, a flexible arginine residue facilitates the promiscuous conversion of (<italic>S</italic>)‐amines and ketones. The degree of promiscuity can be related to distinct key amino acids lying at the surface of the active site.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg36q0s74x" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>