4cmd

The (R)-selective transaminase from Nectria haematococca

spinqualitylabelsall models 4cmd, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cmd is a 2 chain structure with sequence from Fusarium vanettenii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.68Å Ligands: MES, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C7YVL8_FUSV7 Publication Abstract from PubMed During the last decade the use of transaminases for the production of pharmaceutical and fine chemical intermediates has attracted a great deal of attention. Transaminases are versatile biocatalysts for the efficient production of amine intermediates and many have (S)-enantiospecificity. Transaminases with (R)-specificity are needed to expand the applications of these enzymes in biocatalysis. In this work we have identified a fungal putative (R)-specific transaminase from the Eurotiomycetes Nectria haematococca, cloned a synthetic version of this gene, demonstrated (R)-selective deamination of several substrates including (R)-alpha-methylbenzylamine, as well as production of (R)-amines, and determined its crystal structure. The crystal structures of the holoenzyme and the complex with an inhibitor gabaculine offer the first detailed insight into the structural basis for substrate specificity and enantioselectivity of the industrially important class of (R)-selective amine:pyruvate transaminases. This article is protected by copyright. All rights reserved. STRUCTURED DIGITAL ABSTRACT: TAm and TAm bind by x-ray crystallography (View interaction). The substrate specificity, enantioselectivity and structure of the (R)-selective amine:pyruvate transaminase from Nectria haematococca.,Sayer C, Martinez-Torres RJ, Richter N, Isupov MN, Hailes HC, Littlechild JA, Ward JM FEBS J. 2014 Mar 11. doi: 10.1111/febs.12778. PMID:24618038 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminotransferase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA