Structural and mechanistic studies on N2-(2-carboxyethyl)arginine synthase

Biochemical and Biophysical Research Communications

Volumn 385, Issue 4, 2009, Pages 512-517

  Caines, Matthew E C ^a   Sorensen, John L ^a   Schofield, Christopher J ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Lactam; Antibiotic; Clavulanic acid biosynthesis; N2 (2 Carboxyethyl)arginine synthase; Penicillin resistance; Thiamin diphosphate

Indexed keywords

ARGININE; GLYCERALDEHYDE 3 PHOSPHATE; N 2 (2 CARBOXYETHYL)ARGININE SYNTHASE; SYNTHETASE; TARTARIC ACID; UNCLASSIFIED DRUG; VALERIC ACID DERIVATIVE;

ARTICLE; BINDING SITE; CHEMICAL REACTION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; MICHAEL ADDITION; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

ARGININE; ARGININOSUCCINATE LYASE; ARGININOSUCCINATE SYNTHASE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; MULTIENZYME COMPLEXES; PROTEIN CONFORMATION; PROTEIN ENGINEERING; STREPTOMYCES; TARTRATES; VALERATES;

STREPTOMYCES CLAVULIGERUS;

EID: 67349086911     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.05.095     Document Type: Article

References (25)

1. Jordan F. Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions. Nat. Prod. Rep. 20 (2003) 184-201
2. Breslow R. On the mechanism of thiamine action. IV. Evidence from studies on model systems. J. Am. Chem. Soc. 80 (1958) 3719-3726
3. Kern D., Kern G., Neef H., Tittmann K., Killenberg-Jabs M., Wikner C., Schneider G., and Hübner G. How thiamin diphosphate is activated in enzymes. Science 275 (1997) 67-70
4. Khaleeli N., Li R., and Townsend C.A. Origin of the β-lactam carbons in clavulanic acid from an unusual thiamine pyrophosphate-mediated reaction. J. Am. Chem. Soc. 121 (1999) 9223-9224
5. 2-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway. J. Biol. Chem. 279 (2004) 5685-5692
6. Merski M., and Townsend C.A. Observation of an acryloyl-thiamin diphosphate adduct in the first step of clavulanic acid biosynthesis. J. Am. Chem. Soc. 129 (2007) 15750-15751
7. 3H]acetyl phosphate. Eur. J. Biochem. 120 (1981) 593-597
8. Thomas G., Diefenbach R., and Duggleby R.G. Inactivation of pyruvate decarboxylase by 3-hydroxypyruvate. Biochem. J. 266 (1990) 305-308
9. Duggleby R.G. Suicide inhibition of acetohydroxyacid synthase by hydroxypyruvate. J. Enzyme Inhib. Med. Chem. 20 (2005) 1-4
10. Apfel M.A., Ikeda B.H., Speckhard D.C., and Frey P.A. Escherichia coli pyruvate dehydrogenase complex. Thiamin pyrophosphate-dependent inactivation by 3-bromopyruvate. J. Biol. Chem. 259 (1984) 2905-2909
11. Kershaw N.J., Caines M.E.C., Sleeman M.C., and Schofield C.J. The enzymology of clavam and carbapenem biosynthesis. Chem. Commun. (2005) 4251-4263
12. Dyda F., Furey W., Swaminathan S., Sax M., Farrenkopf B., and Jordan F. Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4 Å resolution. Biochemistry 32 (1993) 6165-6170
13. Muller Y.A., and Schulz G.E. Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. Science 259 (1993) 965-967
14. Arjunan P., Umland T., Dyda F., Swaminathan S., Furey W., Sax M., Farrenkopf B., Gao Y., Zhang D., and Jordan F. Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 Å resolution. J. Mol. Biol. 256 (1996) 590-600
15. Leslie A.G.W. Integration of macromolecular diffraction data. Acta Crystallogr. Sect. D: Biol. Crystallogr. 55 (1999) 1696-1702
16. Collaborative Computational Project Number 4. The CCP 4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D: Biol. Crystallogr. 50 (1994) 760-763
17. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Method. Enzymol. 276 (1997) 307-326
18. Murshudov G.N., Vagin A.A., Lebedev A., Wilson K.S., and Dodson E.J. Efficient anisotropic refinement of macromolecular structures using FFT. Acta Crystallogr. Sect. D: Biol. Crystallogr. 55 (1999) 247-255
19. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D: Biol. Crystallogr. 60 (2004) 2126-2132
20. Schüttelkopf A.W., and van Aalten D.M.F. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. Sect. D: Biol. Crystallogr. 60 (2004) 1355-1363
21. DeLano W.L. The PyMOL Molecular Graphics System (2008), DeLano Scientific LLC, Palo Alto, CA, USA
22. Schreuder H.A., Groengijk H., van der Laan J.M., and Wierenga R.K. The transfer of protein crystals from their original mother liquor to a solution with a completely different precipitant. J. Appl. Crystallogr. 21 (1988) 426-429
23. Harding M.M. Metal-ligand geometry relevant to proteins and in proteins: sodium and potassium. Acta Crystallogr. Sect. D: Biol. Crystallogr. 58 (2002) 872-874
24. Frank R.A.W., Titman C.M., Pratap J.V., Luisi B.F., and Perham R.N. A molecular switch and proton wire synchronize the active sites in thiamine enzymes. Science 306 (2004) 872-876
25. Dobritzsch D., König S., Schneider G., and Lu G. High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases. J. Biol. Chem. 273 (1998) 20196-20204