Engineering transketolase to accept both unnatural donor and acceptor substrates and produce α-hydroxyketones.
docking
protein engineering
rational design
transketolase
two substrates specificity
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
05 2020
05 2020
Historique:
received:
09
08
2019
revised:
26
09
2019
accepted:
23
10
2019
pubmed:
28
10
2019
medline:
20
1
2021
entrez:
25
10
2019
Statut:
ppublish
Résumé
A narrow substrate range is a major limitation in exploiting enzymes more widely as catalysts in synthetic organic chemistry. For enzymes using two substrates, the simultaneous optimisation of both substrate specificities is also required for the rapid expansion of accepted substrates. Transketolase (TK) catalyses the reversible transfer of a C
Substances chimiques
Ketones
0
Transketolase
EC 2.2.1.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1758-1776Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/N01877X/1
Pays : United Kingdom
Informations de copyright
© 2019 Federation of European Biochemical Societies.
Références
Reetz MT, Bocola M, Carballeira JD, Zha D & Vogel A (2005) Expanding the range of substrate acceptance of enzymes: combinatorial active-site saturation test. Angew Chem Int Ed Engl 44, 4192-4196.
Sprenger GA, Schorken U, Sprenger G & Sahm H (1995) Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains. Eur J Biochem 230, 525-532.
Draths KM, Pompliano DL, Conley DL, Frost JW, Berry A, Disbrow GL, Staversky RJ & Lievense JC (1992) Biocatalytic synthesis of aromatics from D-Glucose - the role of transketolase. J Am Chem Soc 114, 3956-3962.
Demuynck C, Bolte J, Hecquet L & Dalmas V (1991) Enzyme-Catalyzed synthesis of carbohydrates - synthetic potential of transketolase. Tetrahedron Lett 32, 5085-5088.
Toone EJ & Whitesides GM (1991) Enzymes as catalysts in carbohydrate synthesis. Acs Sym Ser 466, 1-22.
Morris KG, Smith MEB, Turner NJ, Lilly MD, Mitra RK & Woodley JM (1996) Transketolase from Escherichia coli: a practical procedure for using the biocatalyst for asymmetric carbon-carbon bond synthesis. Tetrahedron-Asymmetr 7, 2185-2188.
Wohlgemuth R, Smith MEB, Dalby PA & Woodley JM (2010) Transketolases. In Encyclopedia of Industrial Biotechnology: Bioprocess, Bioseparation and Cell Technology, (Flickinger MC, ed), Vol. 7, pp. 4746-4752. John Wiley and Sons Inc, Hoboken.
Turner NJ (2000) Applications of transketolases in organic synthesis. Curr Opin Biotechnol 11, 527-531.
Kobori Y, Myles DC & Whitesides GM (1992) Substrate-specificity and carbohydrate synthesis using transketolase. J Org Chem 57, 5899-5907.
Schenk G, Duggleby RG & Nixon PF (1998) Properties and functions of the thiamin diphosphate dependent enzyme transketolase. Int J Biochem Cell Biol 30, 1297-1318.
Smith MEB, Hibbert EG, Jones AB, Dalby PA & Hailes HC (2008) Enhancing and reversing the stereoselectivity of Escherichia coli transketolaseviasingle-point mutations. Adv Synth Catal 350, 2631-2638.
Hibbert EG, Senussi T, Costelloe SJ, Lei W, Smith ME, Ward JM, Hailes HC & Dalby PA (2007) Directed evolution of transketolase activity on non-phosphorylated substrates. J Biotechnol 131, 425-432.
Hibbert EG, Senussi T, Smith ME, Costelloe SJ, Ward JM, Hailes HC & Dalby PA (2008) Directed evolution of transketolase substrate specificity towards an aliphatic aldehyde. J Biotechnol 134, 240-245.
Galman JL, Steadman D, Bacon S, Morris P, Smith ME, Ward JM, Dalby PA & Hailes HC (2010) α, α'-Dihydroxyketone formation using aromatic and heteroaromatic aldehydes with evolved transketolase enzymes. Chem Commun (Camb) 46, 7608-7610.
Cazares A, Galman JL, Crago LG, Smith ME, Strafford J, Rios-Solis L, Lye GJ, Dalby PA & Hailes HC (2010) Non-alpha-hydroxylated aldehydes with evolved transketolase enzymes. Org Biomol Chem 8, 1301-1309.
Payongsri P, Steadman D, Strafford J, MacMurray A, Hailes HC & Dalby PA (2012) Rational substrate and enzyme engineering of transketolase for aromatics. Org Biomol Chem 10, 9021-9029.
Payongsri P, Steadman D, Hailes HC & Dalby PA (2015) Second generation engineering of transketolase for polar aromatic aldehyde substrates. Enzyme Microb Technol 71, 45-52.
Zhou C, Saravanan T, Lorilliere M, Wei D, Charmantray F, Hecquet L, Fessner WD & Yi D (2017) Second-generation engineering of a Thermostable Transketolase (TKGst ) for aliphatic aldehyde acceptors with either improved or reversed stereoselectivity. ChemBioChem 18, 455-459.
Zabar JA, Lorilliere M, Yi D, Thangavelu S, Devamani T, Nauton L, Charmantray F, Helaine V, Fessner WD & Hecquet L (2015) Engineering a thermostable transketolase for unnatural conversion of (2S)-hydroxyaldehydes. Adv Synth Catal 357, 1715-1720.
Yi D, Saravanan T, Devamani T, Charmantray F, Hecquet L & Fessner WD (2015) A thermostable transketolase evolved for aliphatic aldehyde acceptors. Chem Commun (Camb) 51, 480-483.
Saravanan T, Reif ML, Yi D, Lorilliere M, Charmantray F, Hecquet L & Fessner WD (2017) Engineering a thermostable transketolase for arylated substrates. Green Chem 19, 481-489.
Fiedler E, Golbik R, Schneider G, Tittmann K, Neef H, König S & Hübner G (2001) Examination of donor substrate conversion in yeast transketolase. J Biol Chem 276, 16051-16058.
Sprenger GA & Pohl M (1999) Synthetic potential of thiamin diphosphate-dependent enzymes. J Mol Catal B-Enzym 6, 145-159.
Esakova OA, Meshalkina LE, Kochetov GA & Golbik R (2009) Halogenated pyruvate derivatives as substrates of transketolase from Saccharomyces cerevisiae. Biochemistry (Mosc) 74, 1234-1238.
Saravanan T, Junker S, Kickstein M, Hein S, Link MK, Ranglack J, Witt S, Lorilliere M, Hecquet L & Fessner WD (2017) Donor promiscuity of a thermostable transketolase by directed evolution: efficient complementation of 1-Deoxy-d-xylulose-5-phosphate synthase activity. Angew Chem Int Ed Engl 56, 5358-5362.
Widmann M, Radloff R & Pleiss J (2010) The thiamine diphosphate dependent enzyme engineering database: a tool for the systematic analysis of sequence and structure relations. BMC Biochem 11, 9.
Hailes HC, Rother D, Muller M, Westphal R, Ward JM, Pleiss J, Vogel C & Pohl M (2013) Engineering stereoselectivity of ThDP-dependent enzymes. FEBS J 280, 6374-6394.
Sandford V, Breuer M, Hauer B, Rogers P & Rosche B (2005) (R)-phenylacetylcarbinol production in aqueous/organic two-phase systems using partially purified pyruvate decarboxylase from Candida utilis. Biotechnol Bioeng 91, 190-198.
Meyer D, Walter L, Kolter G, Pohl M, Muller M & Tittmann K (2011) Conversion of pyruvate decarboxylase into an enantioselective carboligase with biosynthetic potential. J Am Chem Soc 133, 3609-3616.
Asztalos P, Parthier C, Golbik R, Kleinschmidt M, Hubner G, Weiss MS, Friedemann R, Wille G & Tittmann K (2007) Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate. Biochemistry 46, 12037-12052.
Wang J, Dong H, Li S & He H (2005) Theoretical study toward understanding the catalytic mechanism of pyruvate decarboxylase. J Phys Chem B 109, 18664-18672.
Pohl M, Siegert P, Mesch K, Bruhn H & Grotzinger J (1998) Active site mutants of pyruvate decarboxylase from Zymomonas mobilis-a site-directed mutagenesis study of L112, I472, I476, E473, and N482. Eur J Biochem 257, 538-546.
Wikner C, Meshalkina L, Nilsson U, Backstrom S, Lindqvist Y & Schneider G (1995) His103 in yeast transketolase is required for substrate recognition and catalysis. Eur J Biochem 233, 750-755.
Strafford J, Payongsri P, Hibbert EG, Morris P, Batth SS, Steadman D, Smith ME, Ward JM, Hailes HC & Dalby PA (2012) Directed evolution to re-adapt a co-evolved network within an enzyme. J Biotechnol 157, 237-245.
Sevostyanova IA, Solovjeva ON & Kochetov GA (2004) A hitherto unknown transketolase-catalyzed reaction. Biochem Biophys Res Commun 313, 771-774.
Steinmetz A, Vyazmensky M, Meyer D, Barak ZE, Golbik R, Chipman DM & Tittmann K (2010) Valine 375 and phenylalanine 109 confer affinity and specificity for pyruvate as donor substrate in acetohydroxy acid synthase isozyme II from Escherichia coli. Biochemistry 49, 5188-5199.
Wille G, Meyer D, Steinmetz A, Hinze E, Golbik R & Tittmann K (2006) The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Nat Chem Biol 2, 324-328.
Yi D, Devamani T, Abdoul-Zabar J, Charmantray F, Helaine V, Hecquet L & Fessner WD (2012) A pH-based high-throughput assay for transketolase: fingerprinting of substrate tolerance and quantitative kinetics. ChemBioChem 13, 2290-2300.
Pechal M, Cvengrosova Z, Holotik S, Malik L & Hrusovsky M (1981) Identification and determination of alpha-hydroxyketones in a reaction mixture. J Chromatogr 206, 541-547.
Shi X, Leal WS & Meinwald J (1996) Assignment of absolute stereochemistry to an insect pheromone by chiral amplification. Bioorg Med Chem 4, 297-303.
Bloom JD, Labthavikul ST, Otey CR & Arnold FH (2006) Protein stability promotes evolvability. Proc Natl Acad Sci USA 103, 5869-5874.
Yu H & Dalby PA (2018) Coupled molecular dynamics mediate long- and short-range epistasis between mutations that affect stability and aggregation kinetics. Proc Natl Acad Sci USA 115, E11043-E11052.
Yu H & Dalby PA (2018) Exploiting correlated molecular-dynamics networks to counteract enzyme activity-stability trade-off. Proc Natl Acad Sci USA 115, E12192-E12200.
Trott O & Olson AJ (2010) AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31, 455-461.
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
Smith ME, Kaulmann U, Ward JM & Hailes HC (2006) A colorimetric assay for screening transketolase activity. Bioorg Med Chem 14, 7062-7065.
Martinez-Torres RJ, Aucamp JP, George R & Dalby PA (2007) Structural stability of E. coli transketolase to urea denaturation. Enzyme Microb Technol 41, 653-662.
Sippl MJ & Wiederstein M (2008) A note on difficult structure alignment problems. Bioinformatics 24, 426-427.
Sippl MJ & Wiederstein M (2012) Detection of spatial correlations in protein structures and molecular complexes. Structure 20, 718-728.
Waterhouse A, Bertoni M, Bienert S, Studer G, Tauriello G, Gumienny R, Heer FT, de Beer TAP, Rempfer C, Bordoli L et al. (2018) SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Res 46, W296-W303.
Forli S, Huey R, Pique ME, Sanner MF, Goodsell DS & Olson AJ (2016) Computational protein-ligand docking and virtual drug screening with the AutoDock suite. Nat Protoc 11, 905-919.
Subrizi F, Cárdenas-Fernández M, Lye GJ, Ward JM, Dalby PA, Sheppard TD & Hailes HC (2016) Transketolase catalysed upgrading of l-arabinose: the one-step stereoselective synthesis of l-gluco-heptulose. Green Chem 18, 3158-3165.