Truncation of N-terminal regions of Digitalis lanata progesterone 5β-reductase alters catalytic efficiency and substrate preference

Biochimie

Volumn 101, Issue 1, 2014, Pages 31-38

  Rudolph, Kristin ^a   Bauer, Peter ^a   Schmid, Benedikt ^a   Mueller Uri, Frieder ^a   Kreis, Wolfgang ^a  

^a UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

Author keywords

Digitalis lanata; His tag; Progesterone 5 reductase; Substrate affinity; Truncation mutation

Indexed keywords

DIGITALIS; OXIDOREDUCTASE; PROGESTERONE; PROGESTERONE 5 BETA-REDUCTASE; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; GENE DELETION; GENETICS; KINETICS; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; DIGITALIS; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; OXIDOREDUCTASES; PLANT PROTEINS; PROGESTERONE; SEQUENCE DELETION; SUBSTRATE SPECIFICITY;

EID: 84899427362     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2013.12.010     Document Type: Article

References (37)

1. J. Arnau, C. Lauritzen, G.E. Petersen, and J. Pedersen Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins Prot. Expr. Purif. 48 2006 1 13
2. L. Qin, C. Hiser, A. Mulichak, R.M. Garavito, and S. Ferguson-Miller Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase Proc. Natl. Acad. Sci. U. S. A. 103 2006 16117 16122
3. M.H. Bucher, A.G. Evdokimov, and D.S. Waugh Differential effects of short affinity tags on the crystallization of Pyrococcus furiosus maltodextrin-binding protein Acta Crystallogr. D Biol. Crystallogr. 58 2001 392 397
4. M. Carson, D.H. Johnson, H. McDonald, C. Brouillette, and L.J. DeLucas His-tag impact on structure Acta Crystallogr. D Biol. Crystallogr. 63 2007 295 301
5. A. Chaikuad, N. Shafqat, R. Al-Mokhtar, G. Cameron, A.R. Clarke, R.L. Brady, U. Oppermann, J. Frayne, and W.W. Yue Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS Biochem. J. 435 2011 401 409
6. D. Busso, R. Kim, and S.H. Kim Expression of soluble recombinant proteins in a cell-free system using a 96-well format J. Biochem. Biophys. Methods 55 2003 233 240
7. A.B. Mason, Q.Y. He, P.J. Halbrooks, S.J. Everse, D.R. Gumerov, I.A. Kaltashov, V.C. Smith, J. Hewitt, and R.T.A. MacGillivray Differential effect of a His-tag at the N- and C-termini: functional studies with recombinant human serum transferrin Biochemistry 41 2002 9448 9454
8. S. Yano, W. Suyotha, A. Honda, K. Takagi, N. Rattanakit-Chandet, M. Wakayama, and T. Tachiki N-terminal region of chitinase I of Bacillus circulans KA-304 contained new chitin-biding domain Biosci. Biotechnol. Biochem. 75 2011 299 304
9. D.C. Williams, D.J. McGarvey, E.J. Katahira, and R. Croteau Truncation of limonene synthase preprotein provides a fully active 'pseudomature' form of this monoterpene cyclase and reveals the function of the amino-terminal arginine pair Biochemistry 37 1998 12213 12220
10. H. Horchani, L. Sabrina, L. Régine, A. Sayari, Y. Gargouri, and R. Verger Heterologous expression and N-terminal His-tagging processes affect the catalytic properties of staphylococcal lipases: a monolayer study J. Colloid. Interface Sci. 350 2010 586 594
11. A. Sayari, H. Mosbah, R. Verger, and Y. Gargouri The N-terminal His-tag affects the enantioselectivity of staphylococcal lipases: a monolayer study J. Colloid. Interface Sci. 313 2007 261 267
12. B. Persson, Y. Kallberg, J.E. Bray, E. Bruford, S.L. Dellaporta, A.D. Favia, R.G. Duarte, H. Jörnvall, K.L. Kavanagh, N. Kedishvili, M. Kisiela, E. Maser, R. Mindnich, S. Orchard, T.M. Penning, J.M. Thornton, J. Adamski, and U. Oppermann The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative Chem. Biol. Interact. 178 2009 94 98
13. D.E. Gärtner, W. Keilholz, and H.U. Seitz Purification, characterization and partial peptide microsequencing of progesterone 5β-Reductase from shoot cultures of Digitalis purpurea Eur. J. Biochem. 225 1994 1125 1132
14. P. Perez-Bermudez, A.A. Moya Garcia, I. Tunon, and I. Gavidia Digitalis purpurea P5βR2, encoding steroid 5β-reductase, is a novel defense-related gene involved in cardenolide biosynthesis New Phytol. 185 2010 687 700
15. V. Herl, G. Fischer, F. Müller-Uri, and W. Kreis Molecular cloning and heterologous expression of progesterone 5β-reductase from Digitalis lanata Ehrh Phytochemistry 67 2006 225 231
16. D.E. Gärtner, and H.U. Seitz Enzyme activities in cardenolide-accumulating, mixotrophic shot culture of Digitalis purpurea L. Plant Physiol. 141 1993 269 275
17. V. Herl, G. Fischer, F. Müller-Uri, and W. Kreis Molecular cloning and expression of progesterone 5β-reductase (5β-POR) from Isoplexis canariensis Planta Med. 72 2006 1163 1165
18. V. Herl, D.C. Albach, F. Müller-Uri, C. Bräuchler, G. Heubl, and W. Kreis Using progesterone 5β-reductase, a gene encoding a key enzyme in the cardenolide biosynthesis, to infer the phylogeny of the genus Digitalis Plant Sys. Evol. 271 2008 65 78
19. 4,5-steroid 5β-reductases as biocatalysts for the reduction of activated C]C double bonds in acyclic and monocyclic molecules Adv. Synth. Catal. 351 2009 2787 2790
20. J. Munkert, P. Bauer, E. Burda, F. Müller-Uri, and W. Kreis Progesterone 5β-reductase of Erysimum crepidifolium: cDNA cloning, expression in E. coli, and reduction of enones with the recombinant protein Phytochemistry 72 2011 1710 1717
21. P. Bauer, J. Munkert, M. Brydziun, E. Burda, F. Müller-Uri, H. Gröger, Y.A. Muller, and W. Kreis Highly conserved progesterone 5β-reductase genes (P5βR) from 5β-cardenolide-free and 5β-cardenolide-producing angiosperms Phytochemistry 71 2010 1495 1505
22. M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 252
23. U. Stuhlemmer, and W. Kreis Cardenolide formation and activity of pregnane-modifying enzymes in cellsuspension cultures, shoot cultures ad leaves of Digitalis lanata Plant Physiol. Biochem. 34 1996 85 91
24. P. Bauer, L. Rudolph, F. Müller-Uri, and W. Kreis Vein patterning 1-encoded progesterone 5β-reductase: activity-guided improvement of catalytic efficiency Phytochemistry 77 2012 53 59
25. M. Michaelis, and M.L. Menten The kinetics of invertin action Biochem. Z. 49 1913 333 369
26. U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
27. R. Tarrio, F.J. Ayala, and F. Rodriguez-Trelles The vein patterning 1 (VEP1) gene family laterally spread through an ecological network PLoS One 6 2011 22279
28. A. Thorn, C. Egerer-Sieber, C.M. Jäger, V. Herl, F. Müller-Uri, W. Kreis, and Y.A. Muller The crystal structure of progesterone 5β-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases J. Biol. Chem. 283 2008 17260 17269
29. B. Persson, Y. Kallberg, U. Oppermann, and H. Jörnvall Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs) Chem. Biol. Interact. 143-144 2003 271 278
30. P. Zerbe, A. Chiang, and J. Bohlmann Mutational analysis of white spruce (Picea glauca) ent-kaurene synthase (PgKS) reveals common and distinct mechanisms of conifer diterpene synthases of general and specialized metabolism Phytochemistry 74 2012 30 39
31. G.B. Sala-Newby, and A.K. Campbell Stepwise removal of the C-terminal 12 amino acids of firefly luciferase results in graded loss of activity Biochim. Biophys. Acta 1206 1994 155 160
32. E.C. Ralph, L. Xiang, J.R. Cashman, and J. Zhang His-tag truncated butyrylcholinesterase as a useful construct for in vitro characterization of wild-type and variant butyrylcholinesterases Protein Expr. Purif. 80 2011 22 27
33. A.F. Hengeveld, S.E. Schoustra, A.H. Westphal, and A. de Kok Pyruvate dehydrogenase from Azotobacter vinelandii. Properties of the N-terminally truncated enzyme Eur. J. Biochem. 265 1999 1098 1107
34. A.C. Freydank, W. Brandt, and B. Dräger Protein structure modeling indicates hexahistidine-tag interference with enzyme activity Proteins 72 2008 173 183
35. R. Stuermer, B. Hauer, M. Hall, and K. Faber Assymmetric bioreduction of activated C]C bonds using enoate reductases from the old yellow enzyme family Curr. Opin. Chem. Biol. 11 2007 203 211
36. B.M. Nestl, B.A. Nebel, and B. Hauer Recent progress in industrial biocatalysis Curr. Opin. Chem. Biol. 15 2010 1 7
37. K. Durchschein, S. Wallner, P. Macheroux, W. Schwab, T. Winkler, W. Kreis, and K. Faber Nicotineamide- dependent Ene reductases as alternative biocatalysts for the reduction of activated alkenes Eur. J. Org. Chem. 2012 2012 4963 4968