Unexpected tautomeric equilibria of the carbanionenamine intermediate in pyruvate oxidase highlight unrecognized chemical versatility of thiamin

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 27, 2012, Pages 10867-10872

  Meyer, Danilo ^a   Neumann, Piotr ^b   Koers, Eline ^a   Sjuts, Hanno ^a   Lüdtke, Stefan ^a   Sheldrick, George M ^c   Ficner, Ralf ^b   Tittmann, Kai ^a  

^a University of Göttingen   (Germany)

^b Institute for Microbiology and Genetics   (Germany)

^c UNIVERSITY OF GÖTTINGEN   (Germany)

Author keywords

Crystallography; Enzyme mechanism; Tautomerization

Indexed keywords

AMINE; CARBANIONENAMINE; CARBON; HETEROCYCLIC COMPOUND; PYRUVATE OXIDASE; QUERCETIN; THIAMINE; UNCLASSIFIED DRUG;

ARTICLE; ATOM; CHEMICAL STRUCTURE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ELECTRON; ELECTROPHILICITY; ENZYME MECHANISM; LACTOBACILLUS PLANTARUM; MOLECULAR MECHANICS; NUCLEOPHILICITY; OSCILLATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; TAUTOMER; TAUTOMERIZATION;

AMINOPYRIDINES; BACTERIAL PROTEINS; BIPHENYL COMPOUNDS; COENZYMES; CRYSTALLOGRAPHY; ENZYME ACTIVATION; FLAVIN-ADENINE DINUCLEOTIDE; IMIDAZOLES; LACTOBACILLUS PLANTARUM; MODELS, CHEMICAL; PROTEIN STRUCTURE, TERTIARY; PYRUVATE OXIDASE; THIAMINE PYROPHOSPHATE;

EID: 84863588054     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1201280109     Document Type: Article

References (25)

1. Schowen RL (1998) Thiamin-dependent enzymes. Comprehensive Biological Catalysis, ed ML Sinnott (Academic Press, London), Vol 2, pp 217-266.
2. Breslow R (1957) The mechanism of thiamine action. 2. Rapid deuterium exchange in thiazolium salts. J Am Chem Soc 79:1762-1763.
3. Kluger R, Tittmann K (2008) Thiamin diphosphate catalysis: Enzymic and nonenzymic covalent intermediates. Chem Rev 108:1797-1833.
4. Jordan F (2003) Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions. Nat Prod Rep 20:184-201.
5. Fiedler E, et al. (2002) Snapshot of a key intermediate in enzymatic thiamin catalysis: Crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae. Proc Natl Acad Sc USA 99:591-595. (Pubitemid 34106556)
6. Wille G, et al. (2006) The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Nat Chem Biol 2:324-328. (Pubitemid 43787214)
7. Machius M, et al. (2006) A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase. Structure 14:287-298. (Pubitemid 43202018)
8. Berthold CL, et al. (2007) Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases. Structure 15:853-861. (Pubitemid 47042431)
9. Suzuki R, et al. (2010) Crystal structures of phosphoketolase: Thiamine diphosphate-dependent dehydration mechanism. J Biol Chem 285:34279-34287.
10. Tittmann K, et al. (2005) Radical phosphate transfer mechanism for the thiamin diphosphate- and FAD-dependent pyruvate oxidase from Lactobacillus plantarum. Kinetic 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. (Pubitemid 41429454)
11. Chabriere E, et al. (2001) Crystal structure of the free radical intermediate of pyruvate: Ferredoxin oxidoreductase. Science 294(5551):2559-2563. (Pubitemid 34027298)
12. Mansoorabadi SO, et al. (2006) EPR spectroscopic and computational characterization of the hydroxyethylidene-thiamine pyrophosphate radical intermediate of pyruvate: Ferredoxin oxidoreductase. Biochemistry 45:7122-7131. (Pubitemid 43877400)
13. Kern D, et al. (1997) How thiamine diphosphate is activated in enzymes. Science 275:67-70. (Pubitemid 27020308)
14. Schellenberger A (1998) Sixty years of thiamin diphosphate biochemistry. Biochim Biophys Acta 1385:177-186.
15. Nemeria N, et al. (2007) The 1′,4′-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes. Proc Natl Acad Sci USA 104:78-82. (Pubitemid 46067987)
16. Nemeria NS, Chakraborty S, Balakrishnan A, Jordan F (2009) Reaction mechanisms of thiamin diphosphate enzymes: Defining states of ionization and tautomerization of the cofactor at individual steps. FEBS J 276:2432-2446.
17. Tittmann K, et al. (2003) NMR analysis of covalent intermediates in thiamin diphosphate enzymes. Biochemistry 42:7885-7891. (Pubitemid 36807705)
18. Vazquez S, Camps P (2005) Chemistry of pyramidalized alkenes. Tetrahedron 61:5147-5208. (Pubitemid 40703904)
19. Chen YT, Barletta GL, Haghjoo K, Cheng JT, Jordan F (1994) Reactions of benzaldehyde with thiazolium salts in Me(2)So - Evidence for initial formation of 2-(alpha-hydroxybenzyl) thiazolium by nucleophilic-addition and for dramatic solvent effects on benzoin formation. J Org Chem 59:7714-7722.
20. Cleland WW, Frey PA, Gerlt JA (1998) The low barrier hydrogen bond in enzymatic catalysis. J Biol Chem 273:25529-25532. (Pubitemid 28475766)
21. Tittmann K (2009) Reaction mechanisms of thiamin diphosphate enzymes: Redox reactions. FEBS J 276:2454-2468.
22. Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26:795-800.
23. Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr Sect D Biol Crystallogr 60:2126-2132. (Pubitemid 41742764)
24. Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr Sect D Biol Crystallogr 58:1948-1954. (Pubitemid 35337293)
25. Sheldrick GM (2008) A short history of SHELX. Acta Crystallogr Sect A 64:112-122.