Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 867

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Engineering new catalytic activities in enzymes

Chen, Kai, Arnold, Frances H.·2020·Nature Catalysis
DOI 10.1038/s41929-019-0385-5
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/s41929-019-0385-5

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 2 references

Research works printed but not linked: 128

  1. Hönig, M., Sondermann, P., Carreira, E. M. & Turner, N. Enantioselective chemo- and biocatalysis: partners in retrosynthesis. Angew. Chem. Int. Ed. 56, 8942–8973 (2017). This Review covers many examples of designing retrosynthetic routes with enzymes. · DOI · Paper page
  2. de Souza, R. O. M. A., Miranda, L. S. M. & Bornscheuer, U. T. A retrosynthetic approach for biocatalysis in organic synthesis. Chem. Eur. J. 23, 12040–12063 (2017). · DOI
  3. Turner, N. J. & Humphrey, L. Biocatalysis in Organic Synthesis: The Retrosynthesis Approach (Royal Society of Chemistry, 2018). · DOI
  4. Zanghellini, A. de novo computational enzyme design. Curr. Opin. Chem. Biol. 29, 132–138 (2014).
  5. Khersonsky, O. & Tawfik, D. S. Enzyme promiscuity: a mechanistic and evolutionary perspective. Annu. Rev. Biochem. 79, 471–505 (2010). An in-depth Review of how to recognize and understand enzyme promiscuity. · DOI · Paper page
  6. Tawfik, D. S. Messy biology and the origins of evolutionary innovations. Nat. Chem. Bio. 6, 692–696 (2010). · DOI
  7. Busto, E., Gotor-Fernández, V. & Gotor, V. Hydrolases: catalytically promiscuous enzymes for non-conventional reactions in organic synthesis. Chem. Soc. Rev. 39, 4504–4523 (2010). · DOI
  8. Campos, K. R. et al. The importance of synthetic chemistry in the pharmaceutical industry. Science 363, eaat0805 (2019). · DOI · Paper page
  9. Bornscheuer, U. T. & Kazlauskas, R. J. Catalytic promiscuity in biocatalysis: using old enzymes to form new bonds and follow new pathways. Angew. Chem. Int. Ed. 43, 6032–6040 (2004). · DOI
  10. Branneby, C. et al. Carbon–carbon bonds by hydrolytic enzymes. J. Am. Chem. Soc. 125, 874–875 (2003). · DOI
  11. Mayer, C. et al. The E358S mutant of Agrobacterium sp. β-glucosidase is greatly improved glycosynthase. FEBS Lett. 466, 40–44 (2000). · DOI
  12. Jahn, M. et al. Thioglycoligases: mutant glycosidases for thioglycoside synthesis. Angew. Chem. Int. Ed. 42, 352–354 (2003). · DOI
  13. Schallmey, A. & Schallmey, M. Recent advances on halohydrin dehalogenases—from enzyme identification to novel biocatalytic applications. Appl. Microbiol. Biotechnol. 100, 7827–7839 (2016). · DOI
  14. Fox, R. J. et al. Improving catalytic function by ProSAR-driven enzyme evolution. Nat. Biotechnol. 25, 338–344 (2007). · DOI · Paper page
  15. Syrén, P.-O. et al. Squalene-hopene cyclases—evolution, dynamics and catalytic scope. Curr. Opin. Chem. Biol. 41, 73–82 (2016). · DOI
  16. Seitz, M. et al. Synthesis of heterocyclic terpenoids by promiscuous squalene–hopene cyclases. ChemBioChem 14, 436–439 (2013). · DOI
  17. Hammer, S. C. et al. Squalene hopene cyclases are protonases for stereoselective Brønsted acid catalysis. Nat. Chem. Bio. 11, 121–126 (2015). · DOI
  18. Mangas-Sanchez, J. et al. Imine reductases (IREDs). Curr. Opin. Chem. Biol. 37, 19–25 (2017). · DOI
  19. Sharma, M. et al. A mechanism for reductive amination catalyzed by fungal reductive aminases. ACS Catal. 8, 11534–11541 (2018). · DOI
  20. Aleku, G. A. et al. A reductive aminase from Aspergillus oryzae. Nat. Chem. 9, 961–969 (2017). · DOI · Paper page
  21. Emmanuel, M. A., Greenberg, N. R., Oblinsky, D. G. & Hyster, T. K. Accessing non-natural reactivity by irradiating nicotinamide-dependent enzymes with light. Nature 540, 414–417 (2016). This ground-breaking example of photo-induced enzyme promiscuity using the excited states of biological cofactors opens a whole new route to accessing non-natural enzyme activities. · DOI · Paper page
  22. Biegasiewicz, K. F. et al. Catalytic promiscuity enabled by photoredox catalysis in nicotinamide-dependent oxidoreductases. Nat. Chem. 10, 770–775 (2018). · DOI
  23. Dockrey, S. A. B. & Narayan, A. R. H. Flavin-dependent biocatalysts in synthesis. Tetrahedron 75, 1115–1121 (2019). · DOI
  24. Sandoval, B. A., Meichan, A. J. & Hyster, T. K. Enantioselective hydrogen atom transfer: discovery of catalytic promiscuity in flavin-dependent ‘ene’-reductases. J. Am. Chem. Soc. 139, 11313–11316 (2017). · DOI
  25. Sandoval, B. A. et al. Photoenzymatic catalysis enables radical-mediated ketone reduction in ene-reductases. Angew. Chem. Int. Ed. 58, 8714–8718 (2019). · DOI
  26. Biegasiewicz, K. F. et al. Photoexcitation of flavoenzymes enables a stereoselective radical cyclization. Science 364, 1166–1169 (2019). · DOI · Paper page
  27. Sorigué, D. et al. An algal photoenzyme converts fatty acids to hydrocarbons. Science 357, 903–907 (2017). · DOI · Paper page
  28. Zhang, W. et al. Hydrocarbon synthesis via photoenzymatic decarboxylation of carboxylic acids. J. Am. Chem. Soc. 141, 3116–3120 (2019). · DOI
  29. Meyer, D., Neumann, P., Ficner, R. & Tittmann, K. Observation of a stable carbene at the active site of a thiamin enzyme. Nat. Chem. Bio. 9, 488–490 (2013). · DOI
  30. Breslow, R. On the mechanism of thiamine action. IV.1 Evidence from studies on model systems. J. Am. Chem. Soc. 80, 3719–3726 (1958). · DOI
  31. Loschonsky, S. et al. Catalytic scope of the thiamine-dependent multifunctional enzyme cyclohexane-1,2-dione hydrolase. ChemBioChem 15, 389–392 (2014). · DOI
  32. Loschonsky, S. et al. Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: From C–C bond cleavage to C–C bond ligation. Angew. Chem. Int. Ed. 53, 14402–14406 (2014). · DOI
  33. Bernacchia, G. et al. Enzymatic chemoselective aldehyde–ketone cross-couplings through the polarity reversal of methylacetoin. Angew. Chem. Int. Ed. 54, 7171–7175 (2015). · DOI
  34. Demir, A. S. et al. Enantioselective synthesis of α-hydroxy ketones via benzaldehyde lyase-catalyzed C–C bond formation reaction. Adv. Synth. Catal. 344, 96–103 (2002). · DOI
  35. Dünkelmann, P. et al. Development of a donor–acceptor concept for enzymatic cross-coupling reactions of aldehydes: the first asymmetric cross-benzoin condensation. J. Am. Chem. Soc. 124, 12084–12085 (2002). Excellent example of how enzyme catalysis can solve long-standing chemoselectivity problems in synthetic methodologies. · DOI
  36. Dresen, C. et al. The enzymatic asymmetric conjugate umpolung reaction. Angew. Chem. Int. Ed. 49, 6600–6603 (2010). · DOI
  37. Tai, C.-H. & Cook, P. F. Pyridoxal 5′-phosphate-dependent α, β-elimination reactions: mechanism of O-acetylserine sulfhydrylase. Acc. Chem. Res. 34, 49–59 (2001). · DOI
  38. Maier, T. H. P. Semisynthetic production of unnatural l-α-amino acids by metabolic engineering of the cysteine-biosynthetic pathway. Nat. Biotechnol. 21, 422–427 (2003). · DOI
  39. Phillips, R. S. Synthetic applications of tryptophan synthase. Tetrahedron.: Asymmetry 15, 2787–2792 (2004). · DOI
  40. Buller, A. R. et al. Directed evolution of the tryptophan synthase β-subunit for stand-alone function recapitulates allosteric activation. Proc. Natl. Acad. Sci. USA 112, 14599–14604 (2015). · DOI
  41. Romney, D. K. et al. Unlocking reactivity of TrpB: a general biocatalytic platform for synthesis of tryptophan analogues. J. Am. Chem. Soc. 139, 10769–10776 (2017). · DOI
  42. Boville, C. E. et al. Engineered biosynthesis of β-alkyl tryptophan analogs. Angew. Chem. Int. Ed. 57, 14764–14768 (2018). · DOI
  43. Herger, M. et al. Synthesis of β-branched tryptophan analogues using an engineered subunit of tryptophan synthase. J. Am. Chem. Soc. 138, 8388–8391 (2016). · DOI
  44. Romney, D. K., Sarai, N. S. & Arnold, F. H. Nitroalkanes as versatile nucleophiles for enzymatic synthesis of noncanonical amino acids. ACS Catal. 9, 8726–8730 (2019). · DOI
  45. Heberling, M. M., Wu, B., Bartsch, S. & Janssen, D. B. Priming ammonia lyases and aminomutases for industrial and therapeutic applications. Curr. Opin. Chem. Biol. 17, 250–260 (2013). · DOI
  46. Marshall, S. A., Payne, K. A. P. & Leys, D. The UbiX–UbiD system: the biosynthesis and use of prenylated flavin (prFMN). Arch. Biochem. Biophys. 632, 209–221 (2017). · DOI
  47. Vaillancourt, F. H., Yin, J. & Walsh, C. T. SyrB2 in syringomycin E biosynthesis is a nonheme FeII α-ketoglutarate- and O2-dependent halogenase. Proc. Natl. Acad. Sci. USA 102, 10111–10116 (2005). · DOI · Paper page
  48. Wong, S. D. et al. Elucidation of the iron(iv)–oxo intermediate in the non-haem iron halogenase SyrB2. Nature 499, 320–323 (2013). · DOI · Paper page
  49. Matthews, M. L. et al. Direct nitration and azidation of aliphatic carbons by an iron-dependent halogenase. Nat. Chem. Bio. 10, 209–215 (2014). · DOI
  50. Neugebauer, M. E. et al. A family of radical halogenases for the engineering of amino-acid-based products. Nat. Chem. Bio. 10, 209–215 (2014). · DOI
  51. de Visser, S. P., Kumar, D. & Shaik, S. How do aldehyde side products occur during alkene epoxidation by cytochrome P450? Theory reveals a state-specific multi-state scenario where the high-spin component leads to all side products. J. Inorg. Biochem. 98, 1183–1193 (2004). · DOI
  52. Hammer, S. C. et al. Anti-Markovnikov alkene oxidation by metal-oxo-mediated enzyme catalysis. Science 358, 215–218 (2017). This study demonstrates how a new enzyme activity can be obtained by promoting an alternative reaction pathway. · DOI
  53. Prier, C. K. & Arnold, F. H. Chemomimetic biocatalysis: exploiting the synthetic potential of cofactor-dependent enzymes to create new catalysts. J. Am. Chem. Soc. 137, 13992–14006 (2015). · DOI
  54. Che, C.-M. & Huang, J.-S. Metalloporphyrin-based oxidation systems: from biomimetic reactions to application in organic synthesis. Chem. Commun. 3996–4015 (2009). · DOI
  55. Lu, H. & Zhang, X. P. Catalytic C–H functionalization by metalloporphyrins: recent developments and future directions. Chem. Soc. Rev. 40, 1899–1909 (2011). · DOI
  56. Che, C.-M., Lo, V. K.-Y., Zhou, C.-Y. & Huang, J.-S. Selective functionalisation of saturated C–H bonds with metalloporphyrin catalysts. Chem. Soc. Rev. 40, 1950–1975 (2011). · DOI · Paper page
  57. Maxwell, J. L., Brown, K. C., Bartley, D. W. & Kodadek, T. Mechanism of the rhodium porphyrin-catalyzed cyclopropanation of alkenes. Science 256, 1544–1547 (1992). · DOI
  58. Wolf, J. R. et al. Shape and stereoselective cyclopropanation of alkenes catalyzed by iron porphyrins. J. Am. Chem. Soc. 117, 9194–9199 (1995). · DOI
  59. Coelho, P. S., Brustad, E. M., Kannan, A. & Arnold, F. H. Olefin cyclopropanation via carbene transfer catalyzed by engineered cytochrome P450 enzymes. Science 339, 307–310 (2013). This report of a non-natural carbene-transfer reaction with an engineered haem enzyme laid the foundation for development of novel carbene and nitrene transferases. · DOI · Paper page
  60. Coelho, P. S. et al. A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo. Nat. Chem. Biol. 9, 485–487 (2013). · DOI
  61. Brandenberg, O. F. et al. Stereoselective enzymatic synthesis of heteroatom-substituted cyclopropanes. ACS Catal. 8, 2629–2634 (2018). · DOI
  62. Wang, Z. J. et al. Improved cyclopropanation activity of histidine-ligated cytochrome P450 enables the enantioselective formal synthesis of levomilnacipran. Angew. Chem. Int. Ed. 53, 6810–6813 (2014). · DOI
  63. Knight, A. M. et al. Diverse engineered heme proteins enable stereodivergent cyclopropanation of unactivated alkenes. ACS Cent. Sci. 4, 372–377 (2018). · DOI
  64. Bordeaux, M., Tyagi, V. & Fasan, R. Highly diastereoselective and enantioselective olefin cyclopropanation using engineered myoglobin-based catalysts. Angew. Chem. Int. Ed. 54, 1744–1748 (2015). · DOI
  65. Chen, K. et al. Enzymatic construction of highly strained carbocycles. Science 360, 71–75 (2018). · DOI
  66. Farwell, C. C. et al. Enantioselective enzyme-catalyzed aziridination enabled by active-site evolution of a cytochrome P450. ACS Cent. Sci. 1, 89–93 (2015). · DOI
  67. Tsutsumi, H. et al. Unprecedented cyclization catalyzed by a cytochrome P450 in benzastatin biosynthesis. J. Am. Chem. Soc. 140, 6631–6639 (2018). · DOI
  68. Cho, I. et al. Enantioselective aminohydroxylation of styrenyl olefins catalyzed by an engineered hemoprotein. Angew. Chem. Int. Ed. 58, 3138–3142 (2019). · DOI
  69. Svastits, E., Dawson, J. H., Breslow, R. & Gellman, S. H. Functionalized nitrogen atom transfer catalyzed by cytochrome P-450. J. Am. Chem. Soc. 107, 6427–6428 (1985). · DOI
  70. McIntosh, J. A. et al. Enantioselective intramolecular C–H amination catalyzed by engineered cytochrome P450 enzymes in vitro and in vivo. Angew. Chem. Int. Ed. 52, 9309–9312 (2013). · DOI · Paper page
  71. Yang, Y. et al. An enzymatic platform for the asymmetric amination of primary, secondary and tertiary C(sp 3)–H bonds. Nat. Chem. 11, 987–993 (2019). · DOI
  72. Singh, R., Bordeaux, M. & Fasan, R. P450-catalyzed intramolecular sp 3 C–H amination with arylsulfonyl azide substrates. ACS Catal. 4, 546–552 (2014). · DOI
  73. Bordeaux, M., Singh, R. & Fasan, R. Intramolecular C(sp 3)–H amination of arylsulfonyl azides with engineered and artificial myoglobin-based catalysts. Bioorg. Med. Chem. 22, 5697–5704 (2014). · DOI
  74. Singh, R., Kolev, J. N., Sutera, P. A. & Fasan, R. Enzymatic C(sp 3)–H amination: P450-catalyzed conversion of carbonazidates into oxazolidinones. ACS Catal. 5, 1685–1691 (2015). · DOI
  75. Hyster, T. K. et al. Enzyme-controlled nitrogen-atom transfer enables regiodivergent C–H amination. J. Am. Chem. Soc. 136, 15505–15508 (2014). · DOI
  76. Prier, C. K. et al. Enantioselective, intermolecular benzylic C–H amination catalysed by an engineered iron–haem enzyme. Nat. Chem. 9, 629–634 (2017). · DOI
  77. Zhang, R. K. et al. Enzymatic assembly of carbon–carbon bonds via iron-catalysed sp 3 C–H functionalization. Nature 565, 67–72 (2019). This work highlights the immense potential of natural metalloproteins in addressing important problems in synthetic chemistry, especially those considered to be challenging for earth-abundant transition metal catalysis. · DOI · Paper page
  78. Zhang, J., Huang, X., Zhang, R. K. & Arnold, F. H. Enantiodivergent α-amino C–H fluoroalkylation catalyzed by engineered cytochrome P450s. J. Am. Chem. Soc. 141, 9798–9802 (2019). · DOI
  79. Farwell, C. C. et al. Enantioselective imidation of sulfides via enzyme-catalyzed intermolecular nitrogen-atom transfer. J. Am. Chem. Soc. 136, 8766–8771 (2014). · DOI
  80. Tyagi, V. et al. Biocatalytic synthesis of allylic and allenyl sulfides through a myoglobin-catalyzed Doyle–Kirmse reaction. Angew. Chem. Int. Ed. 55, 13562–13566 (2016). · DOI
  81. Prier, C. K. et al. Asymmetric enzymatic synthesis of allylic amines: a sigmatropic rearrangement strategy. Angew. Chem. Int. Ed. 55, 4711–4715 (2016). · DOI
  82. Wang, Z. J., Peck, N. E., Renata, H. & Arnold, F. H. Cytochrome P450-catalyzed insertion of carbenoids into N–H bonds. Chem. Sci. 5, 598–601 (2014). · DOI
  83. Sreenilayam, G. & Fasan, R. Myoglobin-catalyzed intermolecular carbene N–H insertion with arylamine substrates. Chem. Commun. 51, 1532–1534 (2015). · DOI
  84. Tyagi, V., Bonn, R. B. & Fasan, R. Intermolecular carbene S–H insertion catalysed by engineered myoglobin-based catalysts. Chem. Sci. 6, 2488–2494 (2015). · DOI
  85. Chen, K. et al. Alternate heme ligation steers activity and selectivity in engineered cytochrome P450-catalyzed carbene-transfer reactions. J. Am. Chem. Soc. 140, 16402–16407 (2018). · DOI
  86. Kan, S. B. J., Lewis, R. D., Chen, K. & Arnold, F. H. Directed evolution of cytochrome c for carbon–silicon bond formation: bringing silicon to life. Science 354, 1048–1051 (2016). · DOI · Paper page
  87. Kan, S. B. J. et al. Genetically programmed chiral organoborane synthesis. Nature 552, 132–136 (2017). · DOI
  88. Huang, X. et al. A biocatalytic platform for synthesis of chiral α-trifluoromethylated organoborons. ACS Cent. Sci. 5, 270–276 (2019). · DOI
  89. Chen, K. et al. Engineered cytochrome c-catalyzed lactone-carbene B–H insertion. Synlett 30, 378–382 (2019). · DOI
  90. Lewis, R. D. et al. Catalytic iron–carbene intermediate revealed in a cytochrome c carbene transferase. Proc. Natl. Acad. Sci. USA 115, 7308–7313 (2018). This report describes the first iron-carbene intermediate captured in a protein structure and is among the very few examples of a carbene intermediate bound to any type of iron complex. · DOI
  91. Hayashi, T. et al. Capture and characterization of a reactive haem–carbenoid complex in an artificial metalloenzyme. Nat. Catal. 1, 578–584 (2018). · DOI
  92. Wilson, M. E. & Whitesides, G. M. Conversion of a protein to a homogeneous asymmetric hydrogenation catalyst by site-specific modification with a diphosphinerhodium(i) moiety. J. Am. Chem. Soc. 100, 306–307 (1978). · DOI
  93. Schwizer, F. et al. Artificial metalloenzymes: reaction scope and optimization strategies. Chem. Rev. 118, 142–231 (2018). · DOI · Paper page
  94. Chatterjee, A. et al. An enantioselective artificial Suzukiase based on the biotin–streptavidin technology. Chem. Sci. 7, 673–677 (2016). · DOI
  95. Pierron, J. et al. Artificial metalloenzymes for asymmetric allylic alkylation on the basis of the biotin–avidin technology. Angew. Chem. Int. Ed. 47, 701–705 (2008). · DOI · Paper page
  96. Hyster, T. K., Knörr, L., Ward, T. R. & Rovis, T. Biotinylated Rh(III) complexes in engineered streptavidin for accelerated asymmetric C–H activation. Science 338, 500–503 (2012). · DOI · Paper page
  97. Lo, C. et al. Artificial metalloenzymes for olefin metathesis based on the biotin-(strept)avidin technology. Chem. Commun. 47, 12065–12067 (2011). · DOI
  98. Jeschek, M. et al. Directed evolution of artificial metalloenzymes for in vivo metathesis. Nature 537, 661–665 (2016). This study describes a platform for in vivo artificial metalloenzyme assembly and is one of the rare examples of directed evolution of ArMs. · DOI
  99. Hassan, I. S. et al. Asymmetric δ-lactam synthesis with a monomeric streptavidin artificial metalloenzyme. J. Am. Chem. Soc. 141, 4815–4819 (2019). · DOI
  100. Dürrenberger, M. et al. Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines. Angew. Chem. Int. Ed. 50, 3026–3029 (2011). · DOI
  101. Wu, S. et al. Breaking symmetry: engineering single-chain dimeric streptavidin as host for artificial metalloenzymes. J. Am. Chem. Soc. 15869–15878 (2019). · DOI
  102. Raines, D. J. et al. Redox-switchable siderophore anchor enables reversible artificial metalloenzyme assembly. Nat. Catal. 1, 680–688 (2018). · DOI
  103. Eda, S. et al. Biocompatibility and therapeutic potential of glycosylated albumin artificial metalloenzymes. Nat. Catal. 2, 780–792 (2019). · DOI
  104. Mayer, C., Gillingham, D. G., Ward, T. R. & Hilvert, D. An artificial metalloenzyme for olefin metathesis. Chem. Commun. 47, 12068–12070 (2011). · DOI
  105. Jarvis, A. G. et al. Enzyme activity by design: an artificial rhodium hydroformylase for linear aldehydes. Angew. Chem. Int. Ed. 56, 13596–13600 (2017). · DOI
  106. Yang, H., Srivastava, P., Zhang, C. & Lewis, J. C. A general method for artificial metalloenzyme formation through strain-promoted azide–alkyne cycloaddition. ChemBioChem 15, 223–227 (2014). · DOI
  107. Srivastava, P., Yang, H., Ellis-Guardiola, K. & Lewis, J. C. Engineering a dirhodium artificial metalloenzyme for selective olefin cyclopropanation. Nat. Commun. 6, 7789 (2015). · DOI
  108. Yang, H. et al. Evolving artificial metalloenzymes via random mutagenesis. Nat. Chem. 10, 318–324 (2018). · DOI
  109. Abe, S. et al. Control of the coordination structure of organometallic palladium complexes in an apo-ferritin cage. J. Am. Chem. Soc. 130, 10512–10514 (2008). · DOI
  110. Jing, Q. & Kazlauskas, R. J. Regioselective hydroformylation of styrene using rhodium-substituted carbonic anhydrase. ChemCatChem 2, 953–957 (2010). · DOI
  111. Drienovská, I., Rioz-Martínez, A., Draksharapu, A. & Roelfes, G. Novel artificial metalloenzymes by in vivo incorporation of metal-binding unnatural amino acids. Chem. Sci. 6, 770–776 (2015). · DOI
  112. Drienovská, I. et al. Design of an enantioselective artificial metallohydratase enzyme containing an unnatural metal-binding amino acid. Chem. Sci. 8, 7228–7235 (2017). · DOI
  113. Key, H. M., Dydio, P., Clark, D. S. & Hartwig, J. F. Abiological catalysis by artificial haem proteins containing noble metals in place of iron. Nature 534, 534–537 (2016). · DOI
  114. Dydio, P. et al. An artificial metalloenzyme with the kinetics of native enzymes. Science 354, 102–106 (2016). · DOI · Paper page
  115. Key, H. M. et al. Beyond iron: iridium-containing P450 enzymes for selective cyclopropanations of structurally diverse alkenes. ACS Cent. Sci. 3, 302–308 (2017). · DOI
  116. Dydio, P. et al. Chemoselective, enzymatic C‒H bond amination catalyzed by a cytochrome P450 containing an Ir(Me)–PIX cofactor. J. Am. Chem. Soc. 139, 1750–1753 (2017). · DOI
  117. Agostini, F. et al. Biocatalysis with unnatural amino acids: enzymology meets xenobiology. Angew. Chem. Int. Ed. 56, 9680–9703 (2017). · DOI
  118. Drienovská, I., Mayer, C., Dulson, C. & Roelfes, G. A designer enzyme for hydrazone and oxime formation featuring an unnatural catalytic aniline residue. Nat. Chem. 10, 946–952 (2018). · DOI
  119. Mayer, C. et al. Directed evolution of a designer enzyme featuring an unnatural catalytic amino acid. Angew. Chem. Int. Ed. 58, 2083–2087 (2019). · DOI
  120. Burke, A. J. et al. Design and evolution of an enzyme with a non-canonical organocatalytic mechanism. Nature 570, 219–223 (2019). This artificial enzyme with a novel mechanism from organocatalysis will inspire further development of new enzymes with catalytically functional non-canonical amino acids. · DOI
  121. Bornscheuer, U. T. et al. Engineering the third wave of biocatalysis. Nature 485, 185–194 (2012). · DOI · Paper page
  122. Hughes, G. & Lewis, J. C. Introduction: biocatalysis in industry. Chem. Rev. 118, 1–3 (2018). · DOI
  123. Bornscheuer, U. T. The fourth wave of biocatalysis is approaching. Philos. Trans. R. Soc. A 376, 20170063 (2017). · DOI
  124. Bornscheuer, U. T. Biocatalysis: successfully crossing boundaries. Angew. Chem. Int. Ed. 55, 4372–4373 (2016). · DOI
  125. Wu., Z. et al. Machine-learning-assisted directed protein evolution with combinatorial libraries. Proc. Natl. Acad. Sci. USA 116, 8852–8858 (2019). Machine learning-guided directed evolution of a haem protein for a non-native function facilitated exploration of sequence space. · DOI
  126. O’Hagan, D. & Deng, H. Enzymatic fluorination and biotechnological developments of the fluorinase. Chem. Rev. 115, 634–649 (2015). · DOI · Paper page
  127. Jeon, B., Wang, S.-A., Ruszczycky, M. W. & Liu, H. Natural [4+2]-cyclases. Chem. Rev. 117, 5367–5388 (2017). · DOI
  128. Kelly, S. A. et al. Application of ω-transaminases in the pharmaceutical industry. Chem. Rev. 118, 349–367 (2018). · DOI

Cited by

See all 867

Metadata

Authors
Chen, K., & Arnold, F. H.
Venue
Nature Catalysis
Publisher
Springer Science and Business Media LLC
Published
2020-01-20
Volume
3
Issue
3
Pages
203-213
ISSN
2520-1158 (ISSN-L)
DOI
10.1038/s41929-019-0385-5
OpenAlex
W3002774878
Cited by
867
References
2
FWCI
32.36
Type
journal article
Language
en
Open access
closed
Licence
Funders
  • United States Department of Defense | United States Army | U.S. Army Research, Development and Engineering Command | Army Research Office (W911NF-19-2-0026, W911NF-19-D-0001)
  • Resnick Sustainability Institute for Science, Energy and Sustainability, California Institute of Technology

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Engineering new catalytic activities in enzymes. https://app.cochat.ai/papers/10.1038/s41929-019-0385-5
The paper
Chen, K., & Arnold, F. H. (2020). Engineering new catalytic activities in enzymes. Nature Catalysis. https://doi.org/10.1038/s41929-019-0385-5

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.