1.Arnold, F.H. 1998. Design by directed evolution. Acc. Cashem. Res., 31, 125-131

2.Bajorath, J., Stenkamp, R. and Aruffo, A. 1994. Knowledge-based model building of proteins: Concepts and examples. Protein Sci., 2, 1798-1810.

3.Blundell, T.L., Sibanda, B.L., Sternberg, M.J.E. and Thornton, J.M. 1987. Knowledge-based prediction of protein structure and the design of novel molecules. Nature, 326, 347-352.

4.Bowie, J.U., Lüthy, R. and Eisenberg, D. 1991. A method to identify protein sequences that fold into a known three-dimensional structure. Science, 253, 164-170.

5.Chang, Y.Y. and Cronan, J.E., Jr. 1995. Detection by site-specific disulfide cross-linking of a conformational change in binding of Escherschia coli pyruvate oxidase to lipid bilayers. J. Bio. Chem. 270, 7896-7901

6.Goffin, P., Muscariello, L., Lorquet, F., Stukkens, A., Prozzi, D., Sacco, M., Kleerebezem, M. and Hols, P. 2006. Involvement of pyruvate oxidase activity and acetate production in the survival of Lactobacillus plantarum during the stationary phase of aerobic growth. Appl. Environ. Microbiol., 72, 7933-7940

7.Johnson, M.S. and Overigton, J.P. 1993. A structural basis for sequence comparisons: An evaluation of scoring methodologies. J. Mol. Biol., 233, 716-738.

8.Johnson, M.S., Srinivasan, N., Sowdhamini, R. and Blundell, T.L. 1994. Knowledge-based protein modelling. Crit. Rev. Biochem. Mol. Biol., 29, 1-68.

9.Jones, D.T. 1999. GenTHREADER: An efficient and reliable protein folds recognition method for genomic sequences. J. Mol. Biol., 287, 797-815

10.Juan, E.C.M., Hoque, M.M., Hossain, M.T., Yamamoto, T., Imamura, S., Suzuki, K., Sekiguchi, T. and Takénaka, A. 2007. The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 63, 900-907.

11.Kleywegt, G.J. and Jones, T.A. 1998. Phi/psi-chology: Ramachandran revisited. Structure, 4, 1395-1400.

12.Lako, J.D.W., Yengkopiong, J.P., Stafford, W.H.L., Tuffin, M. and Cowan, D.A. 2018. Cloning, expression and characterization of thermostable YdaP from Bacillus licheniformis 9A. Acta Biochim. Pol., 65, 59-66

13.Leichert, L.I.O., Scharf, C. and Hecker, M. 2003. Global characterization of disulfide stress in Bacillus subtilis. J. Bacteriol., 185, 1967-1975.

14.Lorquet, F., Goffin, P., Muscariello, L., Baudry, J.B., Ladero, V., Sacco, M., Kleerebezem, M. and Hols, P. 2004. Characterization and functional analysis of the poxB gene, which encodes pyruvate oxidase in Lactobacillus plantarum. J. Bacteriol., 186, 3749-3759.

15.Lovell, S.C., Davis, J.W., Arendall, W.B. 3rd., de Bakker, P.I., Word, J.M., Richardson, M.G. and Richardson, J.S. 2001. Structure validation by Calpha geometry phi, psi and Cbeta deviation. Proteins, 50, 437-450.

16.Martin, A.C.R., MacArthur, M.W. and Thorton, J.M. 1997. Assessment of comparative modeling in CASP2. Proteins, 1, 14-28.

17.Mather, M., Schopfer, L.M., Massey, V. and Gennis, R.B. 1982. Studies of the flavin adenine dinucleotide binding region in Escherichia coli pyruvate oxidase. J. Biol. Chem., 257, 12887-12892.

18.Muller, Y.A. and Schulz, G.E. 1993. Structure of thiamine and flavindependent enzyme pyruvate oxidase. Science, 259, 965-967.

19.Muller, Y.A., Schumacher, G., Rudolph, R. and Schulz, G.E. 1994. The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum. J. Mol. Biol., 237, 315-335.

20.Neumann, P., Weidner, A., Pech, A., Stubbs, M.T. and Tittmann, K. 2008. Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli. Proc. Nat. Acad. Sci., 105, 17390-17395

21.Patton, T.G., Rice, K.C., Foster, M.K. and Bayles, K.W. 2005. The Staphylococcus aureus cidC gene encodes a pyruvate oxidase that affects acetate metabolism and cell death in stationary phase. Mol. Microbiol, 56, 1664-1674

22.Rapp, C.S. and Friesner, R.A. 1999. Prediction of loop geometries using a generalized Born model of solvation effect. Proteins, 35, 173-183

23.Šali, A. and Blundell, T.L. 1993. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol., 234, 779-815.

24.Šali, A. and Overington, J.P. 1994. Derivation of rules for comparative protein modeling from a database of protein structure alignments. Protein Sci., 3, 1582-1596.

25.Šali, A., Potterton, L., Yuan, F., Vlijmen, H. and Karplus, M. 1995. Evaluation of comparative protein structure modeling by MODELLER. Proteins, 23, 318-326

26.Sánchez, R. and Šali, A. 1997. Advances in comparative proteinstructure modeling. Curr. Opin. Struct. Biol., 7, 206-214.

27.S?nchez, R., Ya, B.A., Feyfant, E. and Šali, A. 1997. Homology protein structure modeling. Trans. Am. Cryst. Assoc., 32, 81-91.

28.Schreiner, M.E. and Eikmanns, B.J. 2005. Pyruvate: Quinone oxidoreductase from Corynebacterium glutamicum: Purification and biochemical characterization. J. Bacteriol., 187, 862-871.

29.Sedewitz, B., Schleifer, K.H. and Gotz, F. 1984. Purification and biochemical characterization of pyruvate oxidase from Lactobacillus plantarum. J. Bacteriol., 160, 273-278.

30.Shi, J., Blundell, T.L. and Mizuguchi, K. 2001. Sequence structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol., 310, 243-257

31.Sutcliffe, M.J., Hanseef, I., Carney, D. and Blundell, T.L. 1987. Knowledge based modelling of homologue proteins. Part I. Three dimensional frameworks derived from the simultaneous superposition of multiple structures. Protein Eng., 1, 377-384

32.Tittmann, K., Wille, G., Golbik, R., Weidner, A., Ghisla, S. and Hübner, G. 2005. Radical phosphate transfer mechanism for the thiamin diphosphate and FAD-dependent pyruvate oxidase from Lactobacillus plantarum. Kinetics coupling of intercofactor electron transfer with phosphate transfer to acetyl-thiamin diphosphate via a transient FAD semiquinone/hydroxyethyl- ThDP radical pair. Biochemistry, 44, 13291-13303.

33.Tomar, A., Eiteman, M.A. and Atman, E. 2003. The effect of acetate pathway mutations on the production of pyruvate in Escherichia coli. Appl. Microbiol. Biotechnol., 62, 76-82.

34.Wille, G., Meyer, D., Steinmetz, A., Hinze, E., Golbik, R. and Tittmann, K. 2006. The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Nat. Chem. Biol., 2, 324-328.

35.Zhang, X., Kenneth, W. and Bayles, S.L. 2017. Staphylococcus aureus CidC is a pyruvate: Menaquinone oxidoreductase. Biochemistry, 56, 4819-4829.