Full Paper
[
[
[
7] L. Dalla-Vechia, B. Reichart, T. Glasnov, L. S. Miranda, C. O. Kappe, R. O.
de Souza, Org. Biomol. Chem. 2013, 11, 6806–6813.
8] A. Schulz, P. Taggeselle, D. Tripier, K. Bartsch, Appl. Environ. Microbiol.
here. Although further work is needed to investigate a wider
range of substrates, perhaps even including ketones, this artifi-
cial biocatalytic system will expand the toolkit for biocatalytic
asymmetric synthesis by forming a conversion pathway be-
tween mineral and organic nitrogen sources.
1990, 56, 1–6.
9] J. Meiwes, M. Schudok, G. Kretzschmar, Tetrahedron: Asymmetry 1997, 8,
527–536.
[
10] J. Krapcho, C. Turk, D. W. Cushman, J. R. Powell, J. M. DeForrest, E. R.
Spitzmiller, D. S. Karanewsky, M. Duggan, G. Rovnyak, J. Schwartzet, J.
Med. Chem. 1988, 31, 1148–60.
Experimental Section
[
[
[
11] R. J. Anderson, K. G. Adams, C. A. Henrick, J. Agric. Food Chem. 1985, 33,
5
08–514.
The assay solution for TA activity measurements contained Tris-HCl
12] R. Giavazzi, A. Garofalo, C. Ferri, V. Lucchini, E. A. Bone, S. Chiari, P. D.
Brown, M. I. Nicoletti, G. Taraboletti, Clin. Cancer Res. 1998, 4, 985–992.
13] H. Shinkai, M. Nishikawa, Y. Sato, K. Toi, I. Kumashiro, Y. Seto, M. Fukuma,
K. Dan, S. Toyoshima, J. Med. Chem. 1989, 32, 1436–1441.
buffer (100 m
amino donor (100 m
acid (20 m , adjusted to pH 9.0 with NaOH). The reaction was initi-
M
, pH 9.0), pyridoxal 5′-phosphate (PLP) (0.1 m
M),
M
, adjusted to pH 9.0 with NaOH), and α-keto
M
ated by adding TA enzyme solution and allowed to react for 10 min
at 35 °C. The enzymatic reaction was then quenched by adding 1 M
HCl and the amount of product was detected by HPLC, as described
in the supporting information. The TA activity was defined as the
amount of enzyme that catalyzed the formation of 1 μmol of prod-
uct per minute.
[14] R. Romero, B. M. Sibai, L. Sanchez-Ramos, G. J. Valenzuela, J. C. Veille, B.
Tabor, K. G. Perry, M. Varner, T. M. Goodwin, R. Lane, J. Smith, G. Shan-
gold, G. W. Creasy, Am. J. Obstet. Gynecol. 2000, 182, 1173–1183.
[
15] B. Weiner, W. Szymanski, D. B. Janssen, A. J. Minnaard, B. L. Feringa, Chem.
Soc. Rev. 2010, 39, 1656–1691.
[
16] S. J. Zuend, M. P. Coughlin, M. P. Lalonde, E. N. Jacobsen, Nature 2009,
4
61, 968–970.
AADH and ADH activity were determined at 35 °C by monitoring at
[17] J. D. Stewart, Curr. Opin. Chem. Biol. 2001, 5, 120–129.
[18] Y. P. Xue, C. H. Cao, Y. G. Zheng, Chem. Soc. Rev. 2018, 47, 1516–1561.
3
40 nm with a TU-1810PC recording spectrophotometer equipped
[
[
19] D. M. Zhu, L. Hua, Biotechnol. J. 2009, 4, 1420–1431.
20] P. P. Taylor, D. P. Pantaleone, R. F. Senkpeil, I. G. Fotheringham, Trends
Biotechnol. 1998, 16, 412–418.
with a thermostatted cell compartment (Beijing Puhua General In-
strument Co., Ltd., China). The reaction mixtures for AADH assay
contained Tris-HCl buffer (100 m
α-keto acid (20 m , adjusted to pH 8.0 with ammonia), and 25 μL
of enzyme solution in a total volume of 1 mL. The reaction mixtures
M, pH 8.0), NAD(P)H (0.25 mM), and
[21] F. Guo, P. Berglund, Green Chem. 2017, 19, 333–360.
[22] M. Xian, S. Alaux, E. Sagot, T. Gefflaut, J. Org. Chem. 2007, 72, 7560–7566.
[23] A. Iwasaki, Y. Yamada, N. Kizaki, Y. Ikenaka, J. Hasegawa, Appl. Microbiol.
Biotechnol. 2006, 69, 499–505.
M
+
for ADH assay contained Tris-HCl buffer (100 mM, pH 8.0), NAD(P)
(
0.25 m ), and 2-propanol (100 m ), and also 25 μL of enzyme
M
M
[
24] I. Slabu, J. L. Galman, R. C. Lloyd, N. J. Turner, ACS Catal. 2017, 7, 8263–
solution in a total volume of 1 mL. Nonenzymatic reaction rates
served as controls, which were subtracted from the reaction rate in
the presence of the enzyme. One unit of enzyme activity was de-
fined as the amount of enzyme that catalyzed generation or degra-
dation of 1 μmol of NAD(P)H per min with a molar absorption coef-
8
284.
[
25] R. J. Meier, M. T. Gundersen, J. M. Woodley, M. Schürmann, ChemCatChem
2015, 7, 2594–2597.
[26] P. C. Engel, K. Dalziel, Biochem. J. 1967, 105, 691–695.
[27] A. Yoshisa, E. Freese, Biochem. Biophys. Acta 1965, 96, 248–262.
[28] B. D. Sanwal, M. W. Zink, Arch. Biochem. Biophys. 1961, 94, 799–802.
29] Y. Asano, A. Nakazawa, K. Endo, J. Biol. Chem. 1987, 262, 10346–10354.
30] A. Galkin, L. Kulakova, T. Yoshimura, K. Soda, N. Esaki, Appl. Environ.
Microbiol. 1997, 63, 4651–4656.
–1
–1
ficient of 6.22 m
M
cm , under the above experimental conditions.
[
[
The tri-enzymatic reactions were performed in 10-mL EP tubes in a
thermostatic water bath under magnetic stirring at 35 °C, and each
enzyme (purified protein) dosage was 0.1 mg/mL. The reaction mix-
[
31] S. Y. K. Seah in Industrial Enzymes (Eds.: J. Polaina, A. P. MacCabe),
Springer, 2007, pp. 489–504.
[32] B. K. Cho, J. H. Seo, T. W. Kang, B. G. Kim, Biotechnol. Bioeng. 2003, 83,
ture contained NH -NH Cl buffer (100 m
M
, pH 8.0), PLP (0.1 m
, adjusted to pH 8.0 with ammonia before-
), 2-propanol (15 m ), and α-keto acid sub-
M),
3
4
amino donor (0.1 m
M
+
hand), NAD(P) (0.1 m
M
M
226–234.
[
33] S. Hanzawa, S. Oe, K. Tokuhisa, K. Kawano, T. Kobayashi, T. Kudo, H. Kaki-
dani, Biotechnol. Lett. 2001, 23, 589–591.
strate (10 mM, adjusted to pH 8.0 with ammonia; Scheme 1).
[
34] H. Yun, B. G. Kim, Biosci. Biotechnol. Biochem. 2008, 72, 3030–3033.
Acknowledgments
[35] J. S. Shin, B. G. Kim, Biotechnol. Biochem. 1999, 65, 206–211.
[
36] M. Höhne, S. Kuhl, K. Robins, U. T. Bornscheuer, ChemBioChem 2008, 9,
This work was financially supported by the National Natural
Science Foundation of China (No. 21476199, 21676240).
363–365.
[37] K. Bartsch, R. Schneider, A. Schulz, Appl. Environ. Microbiol. 1996, 62,
794–3799.
3
[
38] T. Li, A. B. Kootstra, I. G. Fotheringham, Org. Process Res. Dev. 2002, 6,
Keywords: Asymmetric synthesis · Enzyme catalysis ·
Transamination · Unnatural amino acid
533–538.
[39] J. M. Xu, F. T. Fu, H. F. Hu, Y. G. Zheng, Anal. Biochem. 2016, 495, 29–31.
[
[
[
40] J. M. Xu, F. Cheng, F. T. Fu, H. F. Hu, Y. G. Zheng, Appl. Biochem. Biotechnol.
017, 182, 898–909.
41] A. Galkin, L. Kulakova, T. Ohshima, N. Esaki, K. Soda, Protein Eng. 1997,
0, 687–690.
42] K. Kataoka, K. Tanizawa, J. Mol. Catal. B 2003, 23, 299–309.
2
[
[
1] E. A. Bell, A. A. Watson, R. J. Nash, Nat. Prod. Commun. 2008, 3, 93–110.
2] R. P. Hicks, A. L. Russell in Unnatural Amino Acids (Eds.: L. Pollegioni,
S. Servi), Springer, 2012, pp. 135–167.
3] R. Patel, Biomolecules 2013, 3, 741–777.
4] M. H. Yasuda, M. Ueda, K. Okano, H. Mihara, N. Esaki, ACS Symp., Ser.
1
[
[
[43] X. J. Yin, Y. Y. Liu, L. J. Meng, H. S. Zhou, J. P. Wu, L. R. Yang, Adv. Synth.
Catal. 2019, 361, 803–812.
2
009, 1009, 357–374.
5] F. Khorsand, C. D. Murphy, A. J. Whitehead, P. C. Engel, Green Chem. 2017,
9, 503–510.
[44] H. Li, J. C. Liao, ACS Synth. Biol. 2014, 3, 13–20.
[45] K. Vedha-Peters, M. Gunawardana, J. D. Rozzell, S. J. Novick, J. Am. Chem.
Soc. 2006, 128, 10923–10929.
[46] D. Koszelewski, I. Lavandera, D. Clay, G. M. Guebitz, D. Rozzell, W. Kroutil,
Angew. Chem. Int. Ed. 2008, 47, 9337–9340; Angew. Chem. 2008, 120,
9477.
[
[
1
6] M. Vincent, B. Marchand, G. Rémond, S. Jaguelin-Guinamant, G. Damien,
B. Portevin, J. Y. Baumal, J. P. Volland, J. P. Bouchet, P. H. Lambertet, Drug
Des. Discovery 1992, 9, 11–28.
Eur. J. Org. Chem. 2019, 6470–6477
www.eurjoc.org
6476
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim