7p3t
Transaminase of gamma-proteobacteriumTransaminase of gamma-proteobacterium
Structural highlights
FunctionPublication Abstract from PubMedDespite the plethora of information on (S)-selective amine transaminases, the (R)-selective ones are still not well-studied; only a few structures are known to date, and their substrate scope is limited, apart from a few stellar works in the field. Herein, the structure of Luminiphilus syltensis (R)-selective amine transaminase is elucidated to facilitate engineering towards variants active on bulkier substrates. The V37A variant exhibited increased activity towards 1-phenylpropylamine and to activity against 1-butylamine. In contrast, the S248 and T249 positions, located on the beta-turn in the P-pocket, seem crucial for maintaining the activity of the enzyme. Rational engineering of Luminiphilus syltensis (R)-selective amine transaminase for the acceptance of bulky substrates.,Konia E, Chatzicharalampous K, Drakonaki A, Muenke C, Ermler U, Tsiotis G, Pavlidis IV Chem Commun (Camb). 2021 Dec 3;57(96):12948-12951. doi: 10.1039/d1cc04664k. PMID:34806715[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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