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The (R)-selective amine transaminase from Aspergillus fumigatus with inhibitor boundThe (R)-selective amine transaminase from Aspergillus fumigatus with inhibitor bound
Structural highlights
FunctionPublication Abstract from PubMedChirale amines are important precursors for the pharmaceutical and fine-chemical industry. Due to this, the demand for enantiopure amines is currently increasing. Amine transaminases (ATA) can produce a large spectrum of chiral amines in (R)- or (S)-configuration depending on their substrate scope and stereo preference by converting a prochiral ketone into the chiral amine while using alanine as amine donor producing pyruvate as alpha-keto acid product. In order to guide protein engineering of transaminases to improve substrate specificity and enantioselectivity, we carried out a crystal structure analysis at 1.6 A resolution of the (R)-ATA from Aspergillus fumigatus with the bound inhibitor gabaculine. This revealed that Arg126 plays an important role for the dual substrate recognition of this enzyme as mutating this residue to alanine reduced substantially the ability of the enzyme to use pyruvate as amino acceptor. This article is protected by copyright. All rights reserved. Structural and biochemical characterization of the dual substrate recognition of the (R)-selective amine transaminase from Aspergillus fumigatus.,Skalden L, Thomsen M, Hohne M, Bornscheuer UT, Hinrichs W FEBS J. 2014 Nov 15. doi: 10.1111/febs.13149. PMID:25400251[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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