5clo

Crystal structure of a 4-oxalocrotonate tautomerase mutant in complex with nitrostyrene at 2.3 Angstrom

spinqualitylabelsall models 5clo, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5clo is a 18 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NS8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 4OT1_PSEPU Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate. Publication Abstract from PubMed The Michael-type addition reaction is widely used in organic synthesis for carbon-carbon bond formation. However, biocatalytic methodologies for this type of reaction are scarce, which is related to the fact that enzymes naturally catalysing carbon-carbon bond-forming Michael-type additions are rare. A promising template to develop new biocatalysts for carbon-carbon bond formation is the enzyme 4-oxalocrotonate tautomerase, which exhibits promiscuous Michael-type addition activity. Here we present mutability landscapes for the expression, tautomerase and Michael-type addition activities, and enantioselectivity of 4-oxalocrotonate tautomerase. These maps of neutral, beneficial and detrimental amino acids for each residue position and enzyme property provide detailed insight into sequence-function relationships. This offers exciting opportunities for enzyme engineering, which is illustrated by the redesign of 4-oxalocrotonate tautomerase into two enantiocomplementary 'Michaelases'. These 'Michaelases' catalyse the asymmetric addition of acetaldehyde to various nitroolefins, providing access to both enantiomers of gamma-nitroaldehydes, which are important precursors for pharmaceutically active gamma-aminobutyric acid derivatives. Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases.,van der Meer JY, Poddar H, Baas BJ, Miao Y, Rahimi M, Kunzendorf A, van Merkerk R, Tepper PG, Geertsema EM, Thunnissen AM, Quax WJ, Poelarends GJ Nat Commun. 2016 Mar 8;7:10911. doi: 10.1038/ncomms10911. PMID:26952338 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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