5br4

E. coli lactaldehyde reductase (FucO) M185C mutant

spinqualitylabelsall models 5br4, resolution 0.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5br4 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.91Å Ligands: CL, GOL, NAD, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FUCO_ECOLI Publication Abstract from PubMed NAD(P)H-dependent enzymes are ubiquitous in metabolism and cellular processes and are also of great interest for pharmaceutical and industrial applications. Here, we present a structure-guided enzyme engineering strategy for improving catalytic properties of NAD(P)H-dependent enzymes toward native or native-like reactions using mutations to the enzyme's adenine-binding pocket, distal to the site of catalysis. Screening single-site saturation mutagenesis libraries identified mutations that increased catalytic efficiency up to 10-fold in 7 out of 10 enzymes. The enzymes improved in this study represent three different cofactor-binding folds (Rossmann, DHQS-like, and FAD/NAD binding) and utilize both NADH and NADPH. Structural and biochemical analyses show that the improved activities are accompanied by minimal changes in other properties (cooperativity, thermostability, pH optimum, uncoupling), and initial tests on two enzymes (ScADH6 and EcFucO) show improved functionality in Escherichia coli. Mutations in adenine-binding pockets enhance catalytic properties of NAD(P)H-dependent enzymes.,Cahn JK, Baumschlager A, Brinkmann-Chen S, Arnold FH Protein Eng Des Sel. 2016 Jan;29(1):31-8. doi: 10.1093/protein/gzv057. Epub 2015 , Oct 27. PMID:26512129 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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