1026093-55-9Relevant academic research and scientific papers
The substrate spectra of pentaerythritol tetranitrate reductase, morphinone reductase, N-ethylmaleimide reductase and estrogen-binding protein in the asymmetric bioreduction of activated alkenes
Mueller, Nicole J.,Stueckler, Clemens,Hauer, Bernhard,Baudendistel, Nina,Housden, Hazel,Bruce, Neil C.,Faber, Kurt
, p. 387 - 394 (2010)
Four flavoproteins from the old yellow enzyme (OYE) family, pentaerythritol tetranitrate (PETNR) reductase, N-ethylmaleimide reductase (NEMR), morphinone reductase (MorR) and estrogen-binding protein (EBP1), exhibited a broad substrate tolerance by accepting conjugated enals, enones, imides, dicarboxylic acids and esters, as well as a nitroalkene and therefore can be employed for the asymmetric bioreduction of carbon-carbon double (C=C) bonds. In particular, morphinone reductase and estrogen-binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYES.
Two "classical" Old Yellow Enzymes from Chryseobacterium sp. CA49: Broad substrate specificity of Chr-OYE1 and limited activity of Chr-OYE2
Pei, Xiao-Qiong,Xu, Meng-Yu,Wu, Zhong-Liu
, p. 91 - 99 (2016)
Two putative Old Yellow Enzyme (OYE) homologues, Chr-OYE1 and Chr-OYE2, were identified from the genome of Chryseobacterium sp. CA49 as new members of the "classical" subfamily. Chr-OYE1 and Chr-OYE2 were most closely related to the SYE4 from Shewanella oneidensis and NerA from Agrobacterium radiobacter with 41% and 45% identity, respectively. Both enzymes were expressed in Escherichia coli in soluble form, but their catalytic abilities as ene-reductases were quite different. Among the 19 substrate tested, Chr-OYE1 could catalyze the reduction of 18 of them including an ynone with excellent stereoselectivity for several prochiral ones, and its specific activity was roughly 1100-fold high than Chr-OYE2, which only catalyzed 3 of the substrates. After restoring the conserved tyrosine, Chr-OYE2 remained the same substrate spectrum, but showed significantly enhanced activity and stereoselectivity.
A Site-Saturated Mutagenesis Study of Pentaerythritol Tetranitrate Reductase Reveals that Residues 181 and 184 Influence Ligand Binding, Stereochemistry and Reactivity
Toogood, Helen S.,Fryszkowska, Anna,Hulley, Martyn,Sakuma, Michiyo,Mansell, David,Stephens, Gill M.,Gardiner, John M.,Scrutton, Nigel S.
, p. 738 - 749 (2011)
We have conducted a site-specific saturation mutagenesis study of H181 and H184 of flavoprotein pentaerythritol tetranitrate reductase (PETN reductase) to probe the role of these residues in substrate binding and catalysis with a variety of α,β-unsaturated alkenes. Single mutations at these residues were sufficient to dramatically increase the enantiopurity of products formed by reduction of 2-phenyl-1-nitropropene. In addition, many mutants exhibited a switch in reactivity to predominantly catalyse nitro reduction, as opposed to C=C reduction. These mutants showed an enhancement in a minor side reaction and formed 2-phenylpropanal oxime from 2-phenyl-1-nitropropene. The multiple binding conformations of hydroxy substituted nitro-olefins in PETN reductase were examined by using both structural and catalytic techniques. These compounds were found to bind in both active and inhibitory complexes; this highlights the plasticity of the active site and the ability of the H181/H184 couple to coordinate with multiple functional groups. These properties demonstrate the potential to use PETN reductase as a scaffold in the development of industrially useful biocatalysts. Divergent evolution: A site-saturation study of PETN reductase was performed at conserved substrate binding residues H181 and H184. These residues were shown to dramatically alter the ratio of alkene versus nitro-group reduction in favour of oxime by-product formation, as summarised in the picture.
Asymmetric bioreduction of alkenes using ene-reductases YersER and KYE1 and effects of organic solvents
Yanto, Yanto,Winkler, Christoph K.,Lohr, Stephanie,Hall, Melanie,Faber, Kurt,Bommarius, Andreas S.
supporting information; experimental part, p. 2540 - 2543 (2011/06/25)
Asymmetric trans-bioreduction of activated alkenes by KYE1 from Kluyveromyces lactis and Yers-ER from Yersinia bercovieri, two ene-reductases from the Old Yellow Enzyme family, showed a broad substrate spectrum with a moderate to excellent degree of stereoselectivity. Both substrate- and enzyme-based stereocontrols were observed to furnish opposite stereoisomeric products. The effects of organic solvents on enzyme activity and stereoselectivity were outlined in this study, where two-phase systems hexane and toluene are shown to sustain bioreduction efficiency even at high organic solvent content.
