Inhibition of Escherichia coli porphobilinogen synthase using analogs of postulated intermediates

Chemistry and Biology

Volumn 7, Issue 3, 2000, Pages 185-196

  Jarret, Caroline ^a   Stauffer, Frédéric ^a   Henz, Matthias E ^a   Marty, Maurus ^a   Lüönd, Rainer M ^a   Bobálová, Janette ^a   Schürmann, Peter ^a   Neier, Reinhard ^a  

^a UNIVERSITY OF NEUCHÂTEL   (Switzerland)

Author keywords

Analogs of intermediates; Inhibition studies; Porphobilinogen synthase

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034055234     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(00)00089-2     Document Type: Article

References (57)

1. Battersby A.R., Fookes C.J.R., Matcham G.W.J., McDonald E. Biosynthesis of the pigments of life: formation of the macrocycle. Nature. 285:1980;17-21
2. Shemin D. δ-Aminolevulinic acid dehydratase (Rhodopseudomas spheroides). Methods Enzymol. 1970;205-211. XVII Part A
3. Cheh A.M., Neilands J.B. The δ-aminolevulinate dehydratases: molecular and environmental properties. Bonding and Structure. 1976;123-169 Springer-Verlag, Berlin
4. 12. Nat. Prod. Rep. 6:1989;171-203
5. Jordan P.M. The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphyrinogen III. Jordan P.M. Biosynthesis of Tetrapyrroles. 1991;1-66 Elsevier, Amsterdam
6. Franck B., Stratmann H. Condensation products of the porphyrin precursor 5-aminolevulinic acid. Heterocycles. 15:1981;919-923
7. 12. Trans. N.Y. Acad. Science 35:1973;72-79
8. Butler A.R., George S. The nonenzymatic cyclic dimerisation of 5-aminolevulinic acid. Tetrahedron. 48:1992;7879-7886
9. Neier R. Chemical synthesis of porphobilinogen and studies of its biosynthesis. Moody C.J. Advances in Nitrogen Heterocycles. 1996;35-146 JAI Press Inc, Greenwich, Connecticut
10. Nandi D.L., Shemin D. δ-Aminolevulinic acid dehydratase of Rhodopseudomonas spheroides. II. Association to polymers and dissociation to subunits. J. Biol. Chem. 243:1968;1231-1235
11. Echelard Y., Dymetryszyn J., Drolet M., Sasarman A. Nucleotide sequence of the hemB gene of Escherchia coli K12. Mol. Gen. Genet. 214:1988;503-508
12. Jaffe E.K. Porphobilinogen synthase, the first source of heme's asymmetry. J. Bioenerg. Biomembr. 27:1995;169-179
13. Gibbs P.N.B., Jordan P.M. Identification of lysine at the active site of human 5-aminolaevulinate dehydratase. Biochem. J. 236:1986;447-451
14. Nandi D.L., Shemin D. δ-Aminolevulinic acid dehydratase of Rhodopseudomonas spheroides, III. Mechanism of porphobilinogen synthesis. J. Biol. Chem. 243:1968;1236-1242
15. Mitchell L.W., Jaffe E.K. Porphobilinogen synthase from Escherichia coli is a Zn(II) metalloenzyme stimulated by Mg(II). Arch. Biochem. Biophys. 300:1993;169-177
16. Petrovich R.M., Litwin S., Jaffe E.K. Bradyrhizobium japonicum porphobilinogen synthase uses two Mg(II) and monovalent cations. J. Biol. Chem. 271:1996;8692-8699
17. Erskine P.T., Cooper J.B.et al. X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase. Nat. Struct. Biol. 4:1997;1025-1031
18. Erskine P.T., Cooper J.B.et al. The Schiff base complex of yeast 5-aminolaevulinic acid dehydratase with laevulinic acid. Protein Science 8:1999;1250-1256
19. Erskine P.T., Shoolingin-Jordan P.M.et al. X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 Å resolution. Biochemistry. 38:1999;4266-4276
20. 2+ dependent porphobilinogen synthase. J. Mol. Biol. 289:1999;591-602
21. Sundberg R.J. Pyrroles and their benzo derivatives: synthesis. Katritzky A.R., Rees C.W., Scriven E.F. Comprehensive Heterocyclic Chemistry. 1996;275-321 Elsevier Science Ltd, Oxford, UK
22. Abeles, R.H., Frey, P.A. & Jencks, W.P. Nitrogen metabolism: amino acids, urea, and heme. In Biochemistry. (pp.714-717), Jones and Bartlett Publishers, Boston
23. Jordan P.M., Seehra J.S. Mechanism of action of 5-aminolevulinic acid dehydratase: stepwise order of addition of the two molecules of 5-aminolevulinic acid in the enzymic synthesis of porphobilinogen. J. Chem. Soc. Chem. Commun. 1980;240-242
24. Granick S., Mauzerall D. Porphyrin biosynthesis in erythrocytes. II. Enzymes converting δ-aminolevulinic acid to coproporphyrinogen. J. Biol. Chem. 232:1958;1119-1140
25. Lüönd R.M., Walker J., Neier R.W. Assessment of the active-site requirements of 5-aminolaevulinic acid dehydratase: Evaluation of substrate and product analogues as competitive inhibitors. J. Org. Chem. 57:1992;5005-5013
26. Senior N.M., Warren M.J.et al. Comparative studies on the 5-aminoleavulinic acid dehydratases from Pisum sativum, Escherichia coli and Saccharomyces cerevisiae. Biochem. J. 320:1996;401-412
27. Cheung K-M., Spencer P., Timko M.P., Shoolingin-Jordan P.M. Characterization of a recombinant pea 5-aminolevulinic acid dehydratase and comparative Inhibition studies with the Escherichia coli dehydratase. Biochemistry. 36:1997;1148-1156
28. Appleton D., Duguid A.B., Lee S-K., Ha Y-J., Ha H-J., Leeper F.J. Synthesis of analogues of 5-aminolaevulinic acid and inhibition of 5-aminolaevulinic acid dehydratase. J. Chem. Soc. Perkin. Trans. 1:1998;89-101
29. Cornish-Bowden A., Wharton C.W. Reactions of two substrates. Rickwood D., Male D. Enzyme Kinetics. 1990;25-33 IRL Press Limited, Oxford
30. Michaelis M., Menten M.L. Die kinetik der invertinwirkung. Kinetics of the action of invertine. Biochem. Z. 49:1913;333-369. [Kinetics of the action of invertine]
31. Neuhaus F.C. The enzymatic synthesis of D-alanyl-D-alanine. J. Biol. Chem. 237:1962;3128-3135
32. Zawadzke L.E., Bugg T.D.H., Walsh C.T. Existence of two D-alanine:D-alanine ligases in Escherichia coli: cloning and sequencing of the ddlA gene and purification and characterization of the DdlA and DdlB enzymes. Biochemistry. 30:1991;1673-1682
33. Tschudy D.P., Hess R.A., Frykholm B.C. Inhibition of δ-aminolevulinic acid dehydrase by 4, 6-dioxoheptanoic acid. J. Biol. Chem. 256:1981;9915-9923
34. Henz M. Inhibitionsstudien zum mechanismus der porphobilinogen synthase isoliert aus Escherichia coli CR 261. 1996;University of Neuchâtel. [Inhibition studies of porphobilinigen synthase isolated from Escherichia coli 261 in view of elucidating the mechanism of PBGS] [PhD thesis]
35. Jarret C. Etude de la porphobilinogène synthase d'Escherichia coli: inhibition sélectives des deux sites actifs. 1999;University of Neuchâtel. [Studies of Escherichia coli porphobilinogen synthase: directed site selective inhibition] [PhD thesis]
36. Hünig S., Lücke E. Kettenverlängerung von dicarbonsäuren um 6 und 12 C-atome. Chem. Ber. 92:1959;652-662. [Chain elongation of dicarboxylic acids by 6 and 12 C-atoms.]
37. Zürcher A., Hesse M. Die oxidation von 3-(1-nitro-2-oxocycloalkyl)propanal. Helv. Chim. Acta. 70:1987;1937-1943. [Oxidation of 3-(1-nitro-2-oxocycloalkyl)propanal]
38. Diels O., Alder K. Synthesen in der hydroaromatischen reihe; 'dien-synthesen' mit pyrrol und seinen homologen. Justus Liebigs Ann. Chem. 486:1931;211-225. [Synthesis in the field of hydrogenated aromoatic rings; 'diene-synthesis' using pyrol and its homologs]
39. Feuer H., Bachman G.B., White E.H. The reaction of succinic anhydride with hydrazine hydrate. J. Am. Chem. Soc. 73:1951;4716-4719
40. Neuberger A., Scott J.J. The synthesis of δ-succinamidolævulic acid and related compounds. J. Chem. Soc. 1954;1820-1825
41. Heller J., Yogev A., Dreiding A.S. Bishomochinon. Helv. Chim. Acta. 55:1972;1003-1025. [Bishomoquinone.]
42. Kostova K., Hesse M. γ-Nitro-γ-butyrolacton. Helv. Chim. Acta. 67:1984;1725-1728. [γ-Nitro-γ-butyrolactone]
43. Rieke R.D., Wehmeyer R.M., Wu T.C., Ebert G.W. New organocopper reagents prepared utilizing highly reactive copper. Tetrahedron. 45:1989;443-454
44. Zhu L., Wehmeyer R.M., Rieke R.D. The direct formation of functionalized alkyl(aryl)zink halides by oxidative addition of highly reactive zinc with organic halides and their reactions with acid chlorides, α, β-unsaturated ketones, and allylic, aryl and vinyl halides. J. Org. Chem. 56:1991;1445-1453
45. Guijarro D., Rosenberg D.M., Rieke R.D. The reaction of active zinc with organic bromides. J. Am. Chem. Soc. 121:1999;4155-4167
46. Finch N., Fitt J.J., Hsu I.H.C. Cyclopentenone synthesis by directed cyclization. J. Org. Chem. 36:1971;3191-3196
47. Serebryakov E.P., Simolin A.V., Kucherov V.F., Rozynov B.V. New metabolites of Fusarium moniliform. Tetrahedron. 26:1970;5215-5223
48. Sharma K.K., Torssell K.B.G. New routes to γ-ketoesters, β-hydroxy-δ-ketoesters, α, β-unsaturated γ-ketoaldehydes and acetals. Synthesis of cyclopentenones. Tetrahedron. 40:1984;1085-1089
49. Naora H., Ohnuki T., Nakamura A. An improved synthesis of methyl 7-(2-hydroxy-5-oxo-1-cyclopentenyl)heptanoate. Bull. Chem. Soc. Jpn. 61:1988;993-994
50. Bertschy H., Meunier A., Neier R. A new pyrrole synthesis. Angew. Chem. Int. Ed. Engl. 29:1990;777-778
51. Mukaiyama T. The directed aldol reaction. Org. React. 28:1982;203-331
52. Meister C., Scharf H.D. Synthese von (1s)-(-)-frontalin. Liebigs Ann. Chem. 1983;913-921. [Synthesis of (1s)-(-)-frontaline]
53. Johnson R.A., Sharpless K.B. Addition reactions with formation of carbon-oxygen bonds: (ii) Asymmetric methods of epoxidation. Trost B.M. Comprehensive Organic Synthesis. Vol. 7 Oxidation. 1991;389-436 Pergamon Press, Oxford, UK
54. Carlier P.R., Mungall W.S., Schröder G., Sharpless K.B. Enhanced kinetic resolution and enzyme-like shape selectivity. J. Am. Chem. Soc. 110:1988;2978-2979
55. Marty M. Synthese von enantiomerenreinen analoga eines möglichen zwischenproduktes der PBG biosynthese. 1995;University of Neuchâtel. [Chain elongation of dicarboxylic acids by 6 and 12 C-atoms] [PhD thesis]
56. Mauzerall D., Granick S. The occurence and determination fo δ-aminolevulinic acid and porphobilinogen in urine. J. Biol. Chem. 219:1956;435-446
57. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1977;248-254