메뉴 건너뛰기




Volumn 100, Issue 6, 2016, Pages 2579-2590

Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities

Author keywords

Aldol reactions; Biocatalysis; Enzyme engineering; Screening; Threonine aldolase

Indexed keywords

AMINO ACIDS; BIOCHEMICAL ENGINEERING; CATALYST ACTIVITY; CHEMICAL REACTIONS; CONDENSATION REACTIONS; CRYSTAL STRUCTURE; KETONES; SCREENING;

EID: 84955283333     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-015-7218-5     Document Type: Review
Times cited : (71)

References (44)
  • 1
    • 79751490852 scopus 로고    scopus 로고
    • Expanding the application range of aldolases: novel asymmetric syntheses of α-methylated β-hydroxy α-amino acids and β-amino alcohols
    • COI: 1:CAS:528:DC%2BC3cXpslCgur8%3D
    • Baer K, Dückers N, Hummel W, Gröger H (2010) Expanding the application range of aldolases: novel asymmetric syntheses of α-methylated β-hydroxy α-amino acids and β-amino alcohols. ChemCatChem 2:939–942
    • (2010) ChemCatChem , vol.2 , pp. 939-942
    • Baer, K.1    Dückers, N.2    Hummel, W.3    Gröger, H.4
  • 2
    • 79960953596 scopus 로고    scopus 로고
    • A study towards efficient L-​threonine aldolase-​catalyzed enantio- and diastereoselective aldol reactions of glycine with substituted benzaldehydes: biocatalyst production and process development
    • Baer K, Dückers N, Rosenbaum T, Leggewie C, Simon S, Krausser M, Osswald S, Hummel W, Groeger H (2011) A study towards efficient L-​threonine aldolase-​catalyzed enantio- and diastereoselective aldol reactions of glycine with substituted benzaldehydes: biocatalyst production and process development. Tetrahedron: Asymmetry 22:925–928
    • (2011) Tetrahedron: Asymmetry , vol.22 , pp. 925-928
    • Baer, K.1    Dückers, N.2    Rosenbaum, T.3    Leggewie, C.4    Simon, S.5    Krausser, M.6    Osswald, S.7    Hummel, W.8    Groeger, H.9
  • 3
    • 34250186111 scopus 로고    scopus 로고
    • Synthesis of L-threo-3, 4-dihydroxyphenylserine (L-threo-DOPS) with thermostabilized low-specific L-threonine aldolase from Streptomyces coelicolor A3(2)
    • COI: 1:CAS:528:DC%2BD2sXnsVSgsLw%3D
    • Baik SH, Yoshioka H, Yukawa H, Harayama S (2007) Synthesis of L-threo-3, 4-dihydroxyphenylserine (L-threo-DOPS) with thermostabilized low-specific L-threonine aldolase from Streptomyces coelicolor A3(2). J Microbiol Biotechnol 17:721–727
    • (2007) J Microbiol Biotechnol , vol.17 , pp. 721-727
    • Baik, S.H.1    Yoshioka, H.2    Yukawa, H.3    Harayama, S.4
  • 4
    • 84899875378 scopus 로고    scopus 로고
    • Dry entrapment of enzymes by epoxy or polyester resins hardened on different solid supports
    • COI: 1:CAS:528:DC%2BC2cXotVars7o%3D
    • Barig S, Funke A, Merseburg A, Schnitzlein K, Stahmann KP (2014) Dry entrapment of enzymes by epoxy or polyester resins hardened on different solid supports. Enzym Microb Technol 60:47–55
    • (2014) Enzym Microb Technol , vol.60 , pp. 47-55
    • Barig, S.1    Funke, A.2    Merseburg, A.3    Schnitzlein, K.4    Stahmann, K.P.5
  • 5
    • 84932196579 scopus 로고    scopus 로고
    • Development of a growth-dependent selection system for identification of L-threonine aldolases
    • COI: 1:CAS:528:DC%2BC2MXhsFSjsrw%3D, PID: 25616526
    • Bulut D, Gröger H, Hummel W (2015) Development of a growth-dependent selection system for identification of L-threonine aldolases. Appl Microbiol Biotechnol 99:5875–5883
    • (2015) Appl Microbiol Biotechnol , vol.99 , pp. 5875-5883
    • Bulut, D.1    Gröger, H.2    Hummel, W.3
  • 6
    • 84876732154 scopus 로고    scopus 로고
    • Strategies for the discovery and engineering of enzymes for biocatalysis
    • COI: 1:CAS:528:DC%2BC3sXksFOlu78%3D
    • Davids T, Schmidt M, Böttcher D, Bornscheuer UT (2013) Strategies for the discovery and engineering of enzymes for biocatalysis. Curr Opin Chem Bio 17:215–220
    • (2013) Curr Opin Chem Bio , vol.17 , pp. 215-220
    • Davids, T.1    Schmidt, M.2    Böttcher, D.3    Bornscheuer, U.T.4
  • 7
    • 77956227979 scopus 로고    scopus 로고
    • Threonine aldolases-screening, properties and applications in the synthesis of non-proteinogenic β-hydroxy-α-amino acids
    • PID: 20683718
    • Dückers N, Baer K, Simon S, Gröger H, Hummel W (2010) Threonine aldolases-screening, properties and applications in the synthesis of non-proteinogenic β-hydroxy-α-amino acids. Appl Microbiol Biotechnol 88:409–424
    • (2010) Appl Microbiol Biotechnol , vol.88 , pp. 409-424
    • Dückers, N.1    Baer, K.2    Simon, S.3    Gröger, H.4    Hummel, W.5
  • 8
    • 41549124663 scopus 로고    scopus 로고
    • Four types of threonine aldolases: similarities and differences in kinetics/thermodynamics
    • COI: 1:CAS:528:DC%2BD1cXksVanur4%3D
    • Fesko K, Reisinger C, Steinreiber J, Weber H, Schürmann M, Griengl H (2008) Four types of threonine aldolases: similarities and differences in kinetics/thermodynamics. J Mol Cat B Enzym 52-53:19–26
    • (2008) J Mol Cat B Enzym , vol.52-53 , pp. 19-26
    • Fesko, K.1    Reisinger, C.2    Steinreiber, J.3    Weber, H.4    Schürmann, M.5    Griengl, H.6
  • 9
    • 73349122320 scopus 로고    scopus 로고
    • Biocatalytic access to α,α-dialkyl-α-amino acids by a mechanism-based approach
    • COI: 1:CAS:528:DC%2BD1MXhs1WltL%2FL
    • Fesko K, Uhl M, Steinreiber J, Gruber K, Griengl H (2010) Biocatalytic access to α,α-dialkyl-α-amino acids by a mechanism-based approach. Angew Chem Int Ed 49:121–124
    • (2010) Angew Chem Int Ed , vol.49 , pp. 121-124
    • Fesko, K.1    Uhl, M.2    Steinreiber, J.3    Gruber, K.4    Griengl, H.5
  • 10
    • 84878484080 scopus 로고    scopus 로고
    • Biocatalytic methods for C-C bond formation
    • COI: 1:CAS:528:DC%2BC3sXivVKjurk%3D
    • Fesko K, Gruber M (2013) Biocatalytic methods for C-C bond formation. ChemCatChem 5:1248
    • (2013) ChemCatChem , vol.5 , pp. 1248
    • Fesko, K.1    Gruber, M.2
  • 11
    • 84946485729 scopus 로고    scopus 로고
    • Expanding the threonine aldolase toolbox for the asymmetric synthesis of tertiary α-amino acids
    • PID: 26189018
    • Fesko K, Strohmeier GA, Breinbauer R (2015) Expanding the threonine aldolase toolbox for the asymmetric synthesis of tertiary α-amino acids. Appl Microbiol Biotechnol. doi:10.1007/s00253-015-6803-y
    • (2015) Appl Microbiol Biotechnol
    • Fesko, K.1    Strohmeier, G.A.2    Breinbauer, R.3
  • 12
    • 84899130825 scopus 로고    scopus 로고
    • Threonine aldolases
    • COI: 1:CAS:528:DC%2BC2cXhsVOit7jJ, PID: 24767426
    • Franz SE, Stewart JD (2014) Threonine aldolases. Adv Appl Microbiol 88:57–101
    • (2014) Adv Appl Microbiol , vol.88 , pp. 57-101
    • Franz, S.E.1    Stewart, J.D.2
  • 14
    • 84864490929 scopus 로고    scopus 로고
    • A novel genetic selection system for PLP-dependent threonine aldolases
    • COI: 1:CAS:528:DC%2BC38Xpt1SgtLs%3D
    • Giger L, Toscano MD, Bouzon M, Marlièred P, Hilvert D (2012) A novel genetic selection system for PLP-dependent threonine aldolases. Tetrahedron 68:7549–7557
    • (2012) Tetrahedron , vol.68 , pp. 7549-7557
    • Giger, L.1    Toscano, M.D.2    Bouzon, M.3    Marlièred, P.4    Hilvert, D.5
  • 16
    • 53849112321 scopus 로고    scopus 로고
    • Serine hydroxymethyl transferase from Streptococcus thermophilus and L-​threonine aldolase from Escherichia coli as stereocomplementary biocatalysts for the synthesis of β-​hydroxy-​α,​ω-​diamino acid derivatives
    • COI: 1:CAS:528:DC%2BD1cXmsl2js78%3D, PID: 18384024
    • Gutierrez ML, Garrabou X, Agosta E, Servi S, Parella T, Joglar J, Clapes P (2008) Serine hydroxymethyl transferase from Streptococcus thermophilus and L-​threonine aldolase from Escherichia coli as stereocomplementary biocatalysts for the synthesis of β-​hydroxy-​α,​ω-​diamino acid derivatives. Chem Eur J 14:4647–4656
    • (2008) Chem Eur J , vol.14 , pp. 4647-4656
    • Gutierrez, M.L.1    Garrabou, X.2    Agosta, E.3    Servi, S.4    Parella, T.5    Joglar, J.6    Clapes, P.7
  • 17
    • 72249087573 scopus 로고    scopus 로고
    • Diastereoselective synthesis of L-threo-3, 4-dihydroxyphenylserine by low-specific L-threonine aldolase mutants
    • COI: 1:CAS:528:DC%2BD1MXhsFaqtrfO, PID: 19760118
    • Gwon HJ, Baik SH (2010) Diastereoselective synthesis of L-threo-3, 4-dihydroxyphenylserine by low-specific L-threonine aldolase mutants. Biotechnol Lett 32:143–149
    • (2010) Biotechnol Lett , vol.32 , pp. 143-149
    • Gwon, H.J.1    Baik, S.H.2
  • 18
    • 84859197751 scopus 로고    scopus 로고
    • Optimal production of L-threo-2, 3-dihydroxyphenylserine (L-threo-DOPS) on a large scale by diastereoselectivity-enhanced variant of l-threonine aldolase expressed in Escherichia coli
    • COI: 1:CAS:528:DC%2BC38XjvVSntb0%3D
    • Gwon HJ, Yoshioka H, Song NE, Kim JH, Song YR, Jeong DY, Baik SH (2012) Optimal production of L-threo-2, 3-dihydroxyphenylserine (L-threo-DOPS) on a large scale by diastereoselectivity-enhanced variant of l-threonine aldolase expressed in Escherichia coli. Preparative Biochem Biotechnol 42:143–154
    • (2012) Preparative Biochem Biotechnol , vol.42 , pp. 143-154
    • Gwon, H.J.1    Yoshioka, H.2    Song, N.E.3    Kim, J.H.4    Song, Y.R.5    Jeong, D.Y.6    Baik, S.H.7
  • 20
    • 0036785348 scopus 로고    scopus 로고
    • X-ray structures of threonine aldolase complexes: structural basis of substrate recognition
    • COI: 1:CAS:528:DC%2BD38Xms1Cgtro%3D
    • Kielkopf CL, Burley SK (2002) X-ray structures of threonine aldolase complexes: structural basis of substrate recognition. Biochem 41:11711–11720
    • (2002) Biochem , vol.41 , pp. 11711-11720
    • Kielkopf, C.L.1    Burley, S.K.2
  • 21
    • 78649857195 scopus 로고    scopus 로고
    • Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5′-phosphate synthesis
    • COI: 1:CAS:528:DC%2BC3MXhs1Gmt70%3D, PID: 21119630
    • Kim J, Kershner JP, Novikov Y, Shoemaker RK, Copley SD (2010) Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5′-phosphate synthesis. Mol Syst Biol 6:436
    • (2010) Mol Syst Biol , vol.6 , pp. 436
    • Kim, J.1    Kershner, J.P.2    Novikov, Y.3    Shoemaker, R.K.4    Copley, S.D.5
  • 22
    • 84899647395 scopus 로고    scopus 로고
    • Production and properties of threonine aldolase immobilisates
    • COI: 1:CAS:528:DC%2BC2cXjtlSrsLY%3D
    • Kurjatschij S, Katzberg M, Bertau M (2014) Production and properties of threonine aldolase immobilisates. J Mol Cat B Enzym 103:3–9
    • (2014) J Mol Cat B Enzym , vol.103 , pp. 3-9
    • Kurjatschij, S.1    Katzberg, M.2    Bertau, M.3
  • 23
    • 0242659239 scopus 로고    scopus 로고
    • High-throughput screening methods for selecting L-​threonine aldolases with improved activity
    • COI: 1:CAS:528:DC%2BD3sXptVWntbw%3D
    • Lee SJ, Kang HY, Lee Y (2003) High-throughput screening methods for selecting L-​threonine aldolases with improved activity. J Mol Catal B Enzym 26:265–272
    • (2003) J Mol Catal B Enzym , vol.26 , pp. 265-272
    • Lee, S.J.1    Kang, H.Y.2    Lee, Y.3
  • 24
    • 0032479296 scopus 로고    scopus 로고
    • A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. strain DK-38. Molecular cloning and cofactor characterization
    • COI: 1:CAS:528:DyaK1cXkt12itLw%3D, PID: 9642221
    • Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (1998) A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. strain DK-38. Molecular cloning and cofactor characterization. J Biol Chem 273:16678–16685
    • (1998) J Biol Chem , vol.273 , pp. 16678-16685
    • Liu, J.Q.1    Dairi, T.2    Itoh, N.3    Kataoka, M.4    Shimizu, S.5    Yamada, H.6
  • 25
    • 0034605589 scopus 로고    scopus 로고
    • Diversity of microbial threonine aldolases and their application
    • COI: 1:CAS:528:DC%2BD3cXltVGqsro%3D
    • Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (2000) Diversity of microbial threonine aldolases and their application. J Mol Cat B Enzym 10:107–115
    • (2000) J Mol Cat B Enzym , vol.10 , pp. 107-115
    • Liu, J.Q.1    Dairi, T.2    Itoh, N.3    Kataoka, M.4    Shimizu, S.5    Yamada, H.6
  • 26
    • 84923493444 scopus 로고    scopus 로고
    • A fast and sensitive coupled enzyme assay for the measurement of L-threonine and application to high-throughput screening of threonine-overproducing strains
    • COI: 1:CAS:528:DC%2BC2cXhsVGnsLzO
    • Liu Y, Li F, Zhang X, Cao G, Jiang W, Sun Y, Zheng P, Zhang D (2014) A fast and sensitive coupled enzyme assay for the measurement of L-threonine and application to high-throughput screening of threonine-overproducing strains. Enzym Microb Technol 67:1–7
    • (2014) Enzym Microb Technol , vol.67 , pp. 1-7
    • Liu, Y.1    Li, F.2    Zhang, X.3    Cao, G.4    Jiang, W.5    Sun, Y.6    Zheng, P.7    Zhang, D.8
  • 27
    • 84925492025 scopus 로고    scopus 로고
    • Evolution of threonine aldolases, a diverse family involved in the second pathway of glycine biosynthesis
    • COI: 1:CAS:528:DC%2BC2MXitVCqs7g%3D, PID: 25644973
    • Liu G, Zhang M, Chen X, Zhang W, Ding W, Zhang Q (2015) Evolution of threonine aldolases, a diverse family involved in the second pathway of glycine biosynthesis. J Mol Evol 80:102–107
    • (2015) J Mol Evol , vol.80 , pp. 102-107
    • Liu, G.1    Zhang, M.2    Chen, X.3    Zhang, W.4    Ding, W.5    Zhang, Q.6
  • 28
    • 35148814896 scopus 로고    scopus 로고
    • A simple selection strategy for evolving highly efficient enzymes
    • COI: 1:CAS:528:DC%2BD2sXhtFagt7rN, PID: 17873865
    • Neuenschwander M, Butz M, Heintz C, Kast P, Hilvert D (2007) A simple selection strategy for evolving highly efficient enzymes. Nat Biotechnol 25:1145–1147
    • (2007) Nat Biotechnol , vol.25 , pp. 1145-1147
    • Neuenschwander, M.1    Butz, M.2    Heintz, C.3    Kast, P.4    Hilvert, D.5
  • 31
    • 35348890863 scopus 로고    scopus 로고
    • An efficient plasmid vector for expression cloning of large numbers of PCR fragments in Escherichia coli
    • COI: 1:CAS:528:DC%2BD2sXhtFGgs7nP, PID: 17786428
    • Reisinger C, Kern A, Fesko K, Schwab H (2007) An efficient plasmid vector for expression cloning of large numbers of PCR fragments in Escherichia coli. Appl Microbiol Biotechnol 77:241–244
    • (2007) Appl Microbiol Biotechnol , vol.77 , pp. 241-244
    • Reisinger, C.1    Kern, A.2    Fesko, K.3    Schwab, H.4
  • 33
    • 84855287864 scopus 로고    scopus 로고
    • Investigation on the chemoenzymatic synthesis of threo- and erythro-β-hydroxy-L-glutamic acid derivatives
    • COI: 1:CAS:528:DC%2BC38Xptlei
    • Sagui F, De Micheli C, Roda G, Magrone P, Pizzoli R, Riva S (2012) Investigation on the chemoenzymatic synthesis of threo- and erythro-β-hydroxy-L-glutamic acid derivatives. J Mol Catal B Enzym 75:27–34
    • (2012) J Mol Catal B Enzym , vol.75 , pp. 27-34
    • Sagui, F.1    De Micheli, C.2    Roda, G.3    Magrone, P.4    Pizzoli, R.5    Riva, S.6
  • 36
    • 84941073138 scopus 로고    scopus 로고
    • Sequential biocatalytic aldol reactions in multistep asymmetric synthesis: pipecolic acid, piperidine and pyrrolidine (homo)iminocyclitol derivatives from achiral building blocks
    • COI: 1:CAS:528:DC%2BC2cXhsFamtL3F
    • Soler A, Garrabou X, Hernandez K, Gutierrez ML, Busto E, Bujons J, Parella T, Joglar J, Clapes P (2014) Sequential biocatalytic aldol reactions in multistep asymmetric synthesis: pipecolic acid, piperidine and pyrrolidine (homo)iminocyclitol derivatives from achiral building blocks. Adv Synth Catal 356:3007–3024
    • (2014) Adv Synth Catal , vol.356 , pp. 3007-3024
    • Soler, A.1    Garrabou, X.2    Hernandez, K.3    Gutierrez, M.L.4    Busto, E.5    Bujons, J.6    Parella, T.7    Joglar, J.8    Clapes, P.9
  • 37
    • 34447285545 scopus 로고    scopus 로고
    • Synthesis of γ-halogenated and long-chain β-hydroxy-α-amino acids and 2-amino-1, 3-diols using threonine aldolases
    • COI: 1:CAS:528:DC%2BD2sXnslKmtrc%3D
    • Steinreiber J, Fesko K, Reisinger C, Schürmann M, Assema F, Griengl H (2007a) Synthesis of γ-halogenated and long-chain β-hydroxy-α-amino acids and 2-amino-1, 3-diols using threonine aldolases. Tetrahedron 63:8088–8093
    • (2007) Tetrahedron , vol.63 , pp. 8088-8093
    • Steinreiber, J.1    Fesko, K.2    Reisinger, C.3    Schürmann, M.4    Assema, F.5    Griengl, H.6
  • 39
    • 84886771050 scopus 로고    scopus 로고
    • Flow synthesis of phenylserine using threonine aldolase immobilized on Eupergit support
    • PID: 24204429
    • Tibhe JD, Fu H, Noël T, Wang Q, Meuldijk J, Hessel V (2013) Flow synthesis of phenylserine using threonine aldolase immobilized on Eupergit support. Beilstein J Org Chem 9:2168–2179
    • (2013) Beilstein J Org Chem , vol.9 , pp. 2168-2179
    • Tibhe, J.D.1    Fu, H.2    Noël, T.3    Wang, Q.4    Meuldijk, J.5    Hessel, V.6
  • 40
    • 84929501327 scopus 로고    scopus 로고
    • The crystal structure of D-threonine aldolase from Alcaligenes xylosoxidans provides insight into a metal ion assisted PLP-dependent mechanism
    • PID: 25884707
    • Uhl MK, Oberdorfer G, Steinkellner G, Riegler-Berket L, Mink D, van Assema F, Schürmann M, Gruber K (2015) The crystal structure of D-threonine aldolase from Alcaligenes xylosoxidans provides insight into a metal ion assisted PLP-dependent mechanism. PLoS One 10:e0124056
    • (2015) PLoS One , vol.10 , pp. 0124056
    • Uhl, M.K.1    Oberdorfer, G.2    Steinkellner, G.3    Riegler-Berket, L.4    Mink, D.5    van Assema, F.6    Schürmann, M.7    Gruber, K.8
  • 41
    • 27644456596 scopus 로고    scopus 로고
    • Recombinant production of serine hydroxymethyl transferase from Streptococcus thermophilus and its preliminary evaluation as a biocatalyst
    • COI: 1:CAS:528:DC%2BD2MXhtFansL7J, PID: 15726349
    • Vidal L, Calveras J, Clapés P, Ferrer P, Caminal G (2005) Recombinant production of serine hydroxymethyl transferase from Streptococcus thermophilus and its preliminary evaluation as a biocatalyst. Appl Microbiol Biotechnol 68:489–497
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 489-497
    • Vidal, L.1    Calveras, J.2    Clapés, P.3    Ferrer, P.4    Caminal, G.5
  • 42
    • 84924054475 scopus 로고    scopus 로고
    • Improving thermal stability of thermophilic L-threonine aldolase from Thermatoga maritima
    • COI: 1:CAS:528:DC%2BC2MXjt1aqsL8%3D, PID: 25701680
    • Wieteska L, Ionov M, Szemraj J, Feller C, Kolinski A, Gront D (2015) Improving thermal stability of thermophilic L-threonine aldolase from Thermatoga maritima. J Biotechnol 199:69–76
    • (2015) J Biotechnol , vol.199 , pp. 69-76
    • Wieteska, L.1    Ionov, M.2    Szemraj, J.3    Feller, C.4    Kolinski, A.5    Gront, D.6
  • 44
    • 78751575964 scopus 로고    scopus 로고
    • Preparation of optically active β-hydroxy-α-amino acid by immobilized Escherichia coli cells with serine hydroxymethyltransferase activity
    • COI: 1:CAS:528:DC%2BC3MXntVWr, PID: 20514546
    • Zhao GH, Li H, Liu W, Zhang WG, Zhang F, Liu Q, Jiao QC (2011) Preparation of optically active β-hydroxy-α-amino acid by immobilized Escherichia coli cells with serine hydroxymethyltransferase activity. Amino Acids 40:215–220
    • (2011) Amino Acids , vol.40 , pp. 215-220
    • Zhao, G.H.1    Li, H.2    Liu, W.3    Zhang, W.G.4    Zhang, F.5    Liu, Q.6    Jiao, Q.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.