Novel cofactors via post-translational mocifications of enzyme active sites

Chemistry and Biology

Volumn 7, Issue 7, 2000, Pages

  Okeley, Nicole M ^a   Van Der Donk, Wilfred A ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0033942582     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(00)00140-X     Document Type: Review

References (79)

1. van Poelje P.D., Snell E.E. Pyruvoyl-dependent enzymes. Annu. Rev. Biochem. 59:1990;29-59.
2. Kabisch U.C., Gräntzdörffer A., Schierhorn A., Rücknagel K.P., Andreesen J.R., Pich A. Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein. J. Biol. Chem. 274:1999;8445-8454.
3. Wagner M., Sonntag D., Grimm R., Pich A., Eckerskorn C. Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum - biochemical and molecular analysis. Eur. J. Biochem. 260:1999;38-49.
4. Klinman J.P., Mu D. Quinoenzymes in biology. Annu. Rev. Biochem. 63:1994;299-344.
5. Janes S.M., Klinman J.P.et al. A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase. Science. 248:1990;981-987.
6. McIntire W.S., Wemmer D.E., Chistoserdov A., Lidstrom M.E. A new cofactor in a prokaryotic enzyme. tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase Science. 252:1991;817-824.
7. Wang S.X., Klinman J.P.et al. A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains. Science. 273:1996;1078-1084.
8. Wilmot C.M., Phillips S.E.et al. Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction. Biochemistry. 36:1997;1608-1620.
9. Wilce M.C., Yamaguchi H.et al. Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. Biochemistry. 36:1997;16116-16133.
10. Li R., Klinman J.P., Mathews F.S. Copper amine oxidase from Hansenula polymorpha. the crystal structure determined at 2.4 A resolution reveals the active conformation Structure. 6:1998;293-307.
11. Chen L., Hol W.G.J.et al. Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase. FEBS Lett. 287:1991;163-166.
12. Su Q., Klinman J.P. Probing the mechanism of proton coupled electron transfer to dioxygen. the oxidative half-reaction of bovine serum amine oxidase Biochemistry. 37:1998;12513-12525.
13. Mure M., Klinman J.P. Model studies of topaquinone-dependent amine oxidases 1. Oxidation of benzylamine by topaquinone analogs. J. Am. Chem. Soc. 117:1995;8698-8706.
14. 2+. Biochem. J. 330:1998;383-387.
15. Wilmot C.M., Hajdu J., McPherson M.J., Knowles P.F., Phillips S.E. Visualization of dioxygen bound to copper during enzyme catalysis. Science. 286:1999;1724-1728.
16. Matsuzaki R., Fukui T., Sato H., Ozaki Y., Tanizawa K. Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue. FEBS Lett. 351:1994;360-364.
17. Cai D., Klinman J.P. Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase. J. Biol. Chem. 269:1994;32039-32042.
18. Ruggiero C.E., Dooley D.M. Stoichiometry of the topa quinone biogenesis reaction in copper amine oxidases. Biochemistry. 38:1999;2892-2898.
19. Dooley D.M. Structure and biogenesis of topaquinone and related cofactors. J. Biol. Inorg. Chem. 4:1999;1-11.
20. Dove J.E., Smith A.J., Kuchar J., Brown D.E., Dooley D.M., Klinman J.P. Identification of the quinone cofactor in a lysyl oxidase from Pichia pastoris. FEBS Lett. 398:1996;231-234.
21. Frebort I., Adachi O. Two amine oxidases from Aspergillus niger AKU 3302 contain topa quinone as the cofactor: unusual cofactor link to the glutamyl residue occurs only at one of the enzymes. Biochim. Biophys. Acta. 1295:1996;59-72.
22. Chen L., Durley R.C., Mathews F.S., Davidson V.L. Structure of an electron transfer complex. methylamine dehydrogenase, amicyanin, and cytochrome c551i Science. 264:1994;86-90.
23. Stubbe J., van der Donk W.A. Protein radicals in enzyme catalysis. Chem. Rev. 98:1998;705-762.
24. Whittaker J.W., Whittaker M.M. Radical copper oxidases, one electron at a time. Pure Appl. Chem. 70:1998;903-910.
25. Whittaker M.M., Whittaker J.W. The active site of galactose oxidase. J. Biol. Chem. 263:1988;6074-6080.
26. Whittaker M.M., Whittaker J.W. A tyrosine-derived free radical in apogalactose oxidase. J. Biol. Chem. 265:1990;9610-9613.
27. Ito N., Knowles P.F.et al. Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase. Nature. 350:1991;87-90.
28. Johnson J.M., Halsall H.B., Heineman W.R. Redox activation of galactose oxidase. thin layer electrochemical study Biochemistry. 24:1985;1579-1585.
29. Itoh S., Fukuzumi S.et al. Active site models for galactose oxidase - electronic effect of the thioether group in the novel organic cofactor. Inorg. Chem. 36:1997;1407-1416.
30. Ferguson-Miller S., Babcock G.T. Heme/copper terminal oxidases. Chem. Rev. 96:1996;2889-2907.
31. Gennis R.B. Multiple proton-conducting pathways in cytochrome oxidase and a proposed role for the active-site tyrosine. Biochim. Biophys. Acta. 1365:1998;241-248.
32. Michel H. Cytochrome c oxidase. catalytic cycle and mechanisms of proton pumping- a discussion Biochemistry. 38:1999;15129-15140. reply by Wikstrom, M. ibid, (2000) 3515-3519.
33. Yoshikawa S., Tsukihara T.et al. Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science. 280:1998;1723-1729.
34. Ostermeier C., Harrenga A., Ermler U., Michel H. Structure at 2. 7 A resolution of the Paracoccus denitrificans two-subunit cytochrome C oxidase complexed with an antibody F-V fragment. Proc. Natl Acad. Sci. USA. 94:1997;10547-10553.
35. Proshlyakov D.A., Pressler M.A., Babcock G.T. Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase. Proc. Natl Acad. Sci. USA. 95:1998;8020-8025.
36. McCauley K.M., Vrtis J.M., Dupont J., van der Donk W.A. Insights into the functional role of the tyrosine-histidine linkage in cytochrome c oxidase. J. Am. Chem. Soc. 122:2000;2403-2404.
37. Verkhovsky M.I., Jasaitis A., Verkhovskaya M.L., Morgan J.E., Wikstrom M. Proton translocation by cytochrome c oxidase. Nature. 400:1999;480-483.
38. Bravo J., Loewen P.C.et al. Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli. Protein Sci. 6:1997;1016-1023.
39. Buzy A., Hudry-Clergeon G. Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site. J. Protein Chem. 14:1995;59-72.
40. Lerch K. Primary structure of tyrosinase from Neurospora crassa. II. Complete amino acid sequence and chemical structure of a tripeptide containing an unusual thioether. J. Biol. Chem. 257:1982;6414-6419.
41. Gielens C., De Geest N., Xin X.Q., Devreese B., Van Beeumen J., Preaux G. Evidence for a cysteine-histidine thioether bridge in functional units of molluscan haemocyanins and location of the disulfide bridges in functional units δ and γ of the βC-haemocyanin of Helix pomatia. Eur. J. Biochem. 248:1997;879-888.
42. Klabunde T., Eicken C., Sacchettini J.C., Krebs B. Crystal structure of a plant catechol oxidase containing a dicopper center. Nat. Struct. Biol. 5:1998;1084-1090.
43. Cuff M.E., Miller K.I., van Holde K.E., Hendrickson W.A. Crystal structure of a functional unit from Octopus hemocyanin. J. Mol. Biol. 278:1998;855-870.
44. Schmidt B., Selmer T., Igendoh A., von Figura K. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 82:1995;271-278.
45. Miech C., Dierks T., Selmer T., von Figura K., Schmidt B. Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. J. Biol. Chem. 273:1998;4835-4837.
46. Bond C.S., Guss J.M.et al. Structure of a human lysosomal sulfatase. Structure. 5:1997;277-289.
47. Lukatela G., Saenger W.et al. Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry. 37:1998;3654-3664.
48. Dierks T., Schmidt B., von Figura K. Conversion of cysteine to formylglycine. a protein modification in the endoplasmic reticulum Proc. Natl Acad. Sci. USA. 94:1997;11963-11968.
49. Dierks T., Lecca M.R., Schlotterhose P., Schmidt B., von Figura K. Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases. EMBO J. 18:1999;2084-2091.
50. Szameit C., Miech C., Balleininger M., Schmidt B., von Figura K., Dierks T. The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase. J. Biol. Chem. 274:1999;15375-15381.
51. Hernandez D., Stroh J.G., Phillips A.T. Identification of Ser143 as the site of modification in the active site of histidine ammonia-lyase. Arch. Biochem. Biophys. 307:1993;126-132.
52. Taylor R.G., McInnes R.R. Site-directed mutagenesis of conserved serines in rat histidase. Identification of serine 254 as an essential active site residue. J. Biol. Chem. 269:1994;27473-27477.
53. Schuster B., Rétey J. Serine-202 is the putative precursor of the active site dehydroalanine of phenylalanine ammonia lyase. Site-directed mutagenesis studies on the enzyme from parsley (Petroselinum crispum L.). FEBS Lett. 349:1994;252-254.
54. Schwede T.F., Rétey J., Schulz G.E. Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. Biochemistry. 38:1999;5355-5361.
55. Heim R., Prasher D.C., Tsien R.Y. Wavelength mutations and posttranslational autoxidation of green fluorescent protein. Proc. Natl Acad. Sci. USA. 91:1994;12501-12504.
56. Rétey J. Enzymatic catalysis by Friedel-Crafts-type reactions. Naturwissenschaften. 83:1996;439-447.
57. Cleland W.W., Andrews T.J., Gutteridge S., Hartman F.C., Lorimer G.H. Mechanism of rubisco - the carbamate as general base. Chem. Rev. 98:1998;549-561.
58. Taylor T.C., Andersson I. The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate. J. Mol. Biol. 265:1997;432-444.
59. Portis A.R. Jr. Rubisco activase. Biochim. Biophys. Acta. 1015:1990;15-28.
60. Jabri E., Carr M.B., Hausinger R.P., Karplus P.A. The crystal structure of urease from Klebsiella aerogenes. Science. 268:1995;998-1004.
61. Benning M.M., Kuo J.M., Raushel F.M., Holden H.M. Three-dimensional structure of the binuclear metal center of phosphotriesterase. Biochemistry. 34:1995;7973-7978.
62. Kuo J.M., Chae M.Y., Raushel F.M. Perturbations to the active site of phosphotriesterase. Biochemistry. 36:1997;1982-1988.
63. Pearson M.A., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P. Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand. Biochemistry. 37:1998;6214-6220.
64. Kobayashi M., Shimizu S. Metalloenzyme nitrile hydratase. structure, regulation, and application to biotechnology Nat. Biotechnol. 16:1998;733-736.
65. Nagashima S., Endo I.et al. Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms. Nat. Struct. Biol. 5:1998;347-351.
66. Claiborne A., Parsonage D.et al. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry. 38:1999;15407-15416.
67. Yeh J.I., Claiborne A., Hol W.G. Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution. Biochemistry. 35:1996;9951-9957.
68. Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R.K. Crystal structure of methyl coenzyme M reductase - the key enzyme of biological methaneformation. Science. 278:1997;1457-1462.
69. Selmer T., Thauer R.K.et al. The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase. J. Biol. Chem. 275:2000;3755-3760.
70. Thauer R.K. Biochemistry of methanogenesis - a tribute to Stephenson, Marjory. Microbiology. 144:1998;2377-2406.
71. Kelleher N.L. From primary structure to function. biological insights from large-molecule mass spectra Chem. Biol. 7:2000;R37-R45.
72. Gallagher T., Rozwarski D.A., Ernst S.R., Hackert M.L. Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a. J. Mol. Biol. 230:1993;516-528.
73. Dooley D.M., McGuirl M.A., Brown D.E., Turowski P.N., McIntire W.S., Knowles P.F. A Cu(I)-semiquinone state in substrate-reduced amine oxidases. Nature. 349:1991;262-264.
74. Medda R., Padiglia A., Bellelli A., Pedersen J.Z., Agro A.F., Floris G. Cu(I)-semiquinone radical species in plant copper-amine oxidases. FEBS Lett. 453:1999;1-5.
75. Chen L., Mathews F.S.et al. Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution. J. Mol. Biol. 276:1998;131-149.
76. Zhu Z., Davidson V.L. Identification of a new reaction intermediate in the oxidation of methylamine dehydrogenase by amicyanin. Biochemistry. 38:1999;4862-4867.
77. Wachter R.M., Branchaud B.P. Construction and analysis of a semi-quantitative energy profile for the reaction catalyzed by the radical enzyme galactose oxidase. Biochim. Biophys. Acta. 1384:1998;43-54.
78. Fabian M., Wong W.W., Gennis R.B., Palmer G. Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase. Proc. Natl Acad. Sci. USA. 96:1999;13114-13117.
79. Waldow A., Schmidt B., Dierks T., von Bülow R., von Figura K. Amino acid residues forming the active site of arylsulfatase A: role in catalytic activity and substrate binding. J. Biol. Chem. 274:1999;12284-12288.