| 1 |
Extended substrate range of thiamine diphosphate-dependent MenD enzyme by coupling of two C-C-bonding reactions
Schapfl M, Baier S, Fries A, Ferlaino S, Waltzer S, Muller M, Sprenger GA
Applied Microbiology and Biotechnology, 102(19), 8359, 2018 |
| 2 |
Simultaneous Identification of Reaction and Inactivation Kinetics of an Enzyme-catalyzed Carboligation
Ohs R, Leipnitz M, Schopping M, Spiess AC
Biotechnology Progress, 34(5), 1081, 2018 |
| 3 |
Structural and functional significance of the highly-conserved residues in Mycobacterium tuberculosis acetohydroxyacid synthase
Baig IA, Moon JY, Kim MS, Koo BS, Yoon MY
Enzyme and Microbial Technology, 58-59, 52, 2014 |
| 4 |
Characterization of recombinant FAD-independent catabolic acetolactate synthase from Enterococcus faecalis V583
Lee SC, Kim J, La IJ, Kim SK, Yoon MY
Enzyme and Microbial Technology, 52(1), 54, 2013 |
| 5 |
Role of a highly conserved proline-126 in ThDP binding of Mycobacterium tuberculosis acetohydroxyacid synthase
Baig IA, Gedi V, Lee SC, Koh SH, Yoon MY
Enzyme and Microbial Technology, 53(4), 243, 2013 |
| 6 |
Structural insights of the MenD from Escherichia coli reveal ThDP affinity
Amit P, Saleem Y, Nam KH, Kim KS, Park SY, Kim EE, Hwang KY
Biochemical and Biophysical Research Communications, 380(4), 797, 2009 |
| 7 |
Structural and functional analysis of Vitamin K-2 synthesis protein MenD
Priyadarshi A, Kim EE, Hwang KY
Biochemical and Biophysical Research Communications, 388(4), 748, 2009 |
| 8 |
Derivation and identification of a mechanistic model for a branched enzyme-catalyzed carboligation
Ohs R, Fischer K, Schopping M, Spiess AC
Biotechnology Progress |
