Catalytic promiscuity and the evolution of new enzymatic activities

Chemistry and Biology

Volumn 6, Issue 4, 1999, Pages

  O'Brien, Patrick J ^a   Herschlag, Daniel ^a  

^a STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0033117461     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(99)80033-7     Document Type: Review

References (144)

1. Lewis, E.B. (1951). Pseudoallelism and gene evolution. Cold Spring Harbor Symp. Quant. Biol. 16, 159-163.
2. Ohno, S. (1970). Evolution by Gene Duplication. George Allen and Unwin, London.
3. Jensen, R.A. (1976). Enzyme recruitment in evolution of new function. Annu. Rev. Microbiol. 30, 409-425.
4. Rossman, M.G., Liljas, A., Branden, C.-I. & Banaszak, L.J. (1975). Evolutionary and structural relationships among dehydrogenases. In The Enzymes. (Boyer, P.D., ed.), pp. 61-102, Academic Press, New York.
5. Wilmanns, M., Hyde, C.C., Davies, D.R., Kirschner, K. & Jansonius, J.N. (1991). Structural conservation in parallel β/α-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis. Biochemistry 30, 9161-9169.
6. Babbitt, P.C., et al., & Gerlt, J.A. (1995). A functionally diverse enzyme superfamily that abstracts the α protons of carboxylic acids. Science 267, 1159-1161.
7. Babbitt, P., et al., & Gerlt, J.A. (1996). The enolase superfamily: A general strategy for enzyme-catalyzed abstration of the α-protons of carboxylic acids. Biochemistry 35, 16489-16501.
8. Babbitt, P.C. & Gerlt, J.A. (1997). Understanding enzyme superfamilies. J. Biol. Chem. 272, 30591-30594.
9. Holm, L. & Sander, C. (1997). An evolutionary treasure: Unification of a broad set of amidohyrolases related to urease. Proteins 28, 72-82.
10. Ollis, D.L., et al., & Goldman, A. (1992). The α/β hydrolase fold. Protein Eng. 5, 197-211.
11. Bernat, B.A., Laughlin, L.T. & Armstrong, R.N. (1997). Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases. Biochemistry 36, 3050-3055.
12. Gerlt, J.A. & Babbitt, P.C. (1998). Mechanistically diverse enzyme superfamilies: The importance of chemistry in the evolution of catalysis. Cur. Opin. Chem. Biol. 2, 607-612.
13. Armstrong, R.N. (1998). Mechanistic imperatives for the evolution of glutathione transferases. Cur. Opin. Chem. Biol. 2, 618-623.
14. Alexander, F.W., Sandmeier, E., Mehta, P.K. & Christen, P. (1994). Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes: Regio-specific α, β and γ families. Eur. J. Biochem. 219, 953-960.
15. Aravind, L. & Koonin, E.V. (1998). A novel family of predicted phosphoesterases include Drosophila prune protein and bacterial RecJ exonuclease. Trends Biol. Sci. 23, 17-19.
16. Baker, P.J., et al., & Rice, D.W. (1997). Determinants of substrate specificity in the superfamily of amino acid dehydrogenases. Biochemistry 36, 16109-16115.
17. Baker, A.S., et al., & Dunaway-Mariano, D. (1998). Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis. Biochemistry 37, 9305-9315.
18. Bork, P. & Koonin, E.V. ( 1994). A new family of carbon-nitrogen hydrolases. Protein Sci. 3, 1344-1346.
19. Bork, P., Holm, L., Koonin, E.V. & Sander, C. (1995). The cytidyltransferase superfamily: Identification of the nucleotide-binding site and fold prediction. Proteins 22, 259-266.
20. Bork, P., Brown, N.P., Hegyi, H. & Schultz, J. (1996). The protein phosphatase 2C (PP2C) superfamily: Detection of bacterial homologues. Protein Sci. 5, 1421-1425.
21. Galperin, M.Y., Bairoch, A. & Koonin, E.V. (1998). A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. Protein Sci. 7, 1829-1835.
22. Holm, L. & Sander, C. (1995). Evolutionary link between glycogen phosphorylase and a DNA modifying enzyme. EMBO J. 14, 1287-1293.
23. Holm, L. & Sander, C. (1997). Enzyme HIT. Trends Biochem. Sci. 22, 116-117.
24. Jez, J.M., Bennett, M.J., Schlegel, B.P., Lewis, M. & Penning, T.M. (1997). Comparative anatomy of the aldo-keto reductase superfamily. Biochem. J. 326, 625-636.
25. Koonin, E.V. & Tatusov, R.L (1994). Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. J. Mol. Biol. 244, 125-132.
26. Koonin, E.V. (1996). A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that include poxvirus envelope proteins. Trends Biochem. Sci. 21, 237-277.
27. Petsko, G.A., Kenyon, G.L., Gerlt, J.A., Ringe, D. & Kozarich, J.W. (1993). On the origin of enzymatic species. Trends Biochem. Sci. 18, 372-376.
28. Murzin, A.G. (1993). Can homologous proteins evolve different enzymatic activities? Trends Biol. Sci. 18, 403-405.
29. Murzin, A.G. (1998). How far divergent evolution goes in proteins. Curr. Opin. Struct. Biol. 8, 380-387.
30. Aravind, L., Galperin, M.Y. & Koonin, E.V. (1998). The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Trends Biochem. Sci. 23, 127-129.
31. Niedhart, D.J., Kenyon, G.L., Gerlt, J.A. & Petsko, G.A. (1990). Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous. Nature 347, 692-694.
32. Wagner, U.G., Hasslacher, M., Griengl, H., Schwab, H. & Kratky, C. (1996). Mechanism of cyanogenesis: The crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Structure 4, 811-822.
33. Diaz, E. & Timmis, K.N. (1995). Identification of functional residues in a 2-hydroxymuconic semialdehyde hydrolase: A new member of the α/β hydrolase-fold family of enzymes which cleaves carbon-carbon bonds. J. Biol. Chem. 270, 6403-6411.
34. Lebioda, L. & Stec, B. (1988). Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor. Nature 333, 683-686.
35. Hasson, M.S., et al., & Ringe, D. (1998). Evolution of an enzyme active site: The structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase. Proc. Natl Acad. Sci. USA 95, 10369-10401.
36. Palmer, D.R.J., Hubbard, B.K. & Gerlt, J.A. (1998). Evolution of enzymatic activities in the enolase superfamily: Partitioning of reactive intermediates by (D)-glucarate dehydratase from Pseudomonas putida. Biochemistry 37, 14350-14357.
37. Gulick, A.M., Palmer, D.R.J., Babbitt, P.C., Gerlt, J.A. & Rayment, I. (1998). Evolution of enzymatic activities in the enolase superfamily: Crystal structure of (D)-glucarate dehydratase from Pseudomonas putida. Biochemistry 37, 14358-14368.
38. Hubbard, B.K., Koch, M., Palmer, D.R.J., Babbitt, P.C. & Gerlt, J.A. (1998). Evolution of enzymatic activities in the enolase superfamily: Characterization of the (D)-glucarate/galactarate catabolic pathway in E. Coli. Biochemistry 37, 14369-14375.
39. Galperin, M.Y., Walker, D.R. & Koonin, E.V. (1998). Analogous enzymes: Independent inventions in enzyme evolution. Genome Res. 8, 779-790.
40. Hedstrom, L. (1994). Engineering for redesign. Curr. Opin. Struct. Biol. 4, 608-611.
41. Wedemayer, G.J., Patten, P.A., Wang, L.H., Schultz, P.G. & Stevens, R.C. (1997). Structural insights into the evolution of an antibody combining site. Science 276, 1665-1669.
42. Yano, T., Oue, S. & Kagamiyama, H. (1998). Directed evolution of an aspartate aminotransferase with new substrate specificities. Proc. Natl Acad. Sci. USA 95, 5511-5515.
43. Hughes, A.L (1994). The evolution of functionally novel proteins after gene duplication. Proc. Roy. Soc. London B 256, 119-124.
44. Parsot, C. (1987). A common origin for enzymes involved in the terminal step of the threonine and tryptophan biosynthetic pathways. Proc. Natl Acad. Sci. USA 84, 5207-5210.
45. Jensen, R.A. & Gu, W. (1996). Evolutionary recruitment of biochemically specialized subdivisions of family I within the protein superfamily of aminotransferases. J. Bacteriol. 178, 2161-2171.
46. Walsh, C. (1979). Enzymatic Reaction Mechanisms. W.H. Freeman & Co., New York.
47. Kovach, I.M, Larson, M. & Schoweu, R.L. (1986). Catalytic recruitment in the inactivation of serine proteases by phosphonate esters. Recruitment of acid-base catalysis. J. Am. Chem. Soc. 108, 5490-5495.
48. Zhao, Q., Kovach, I.M., Bencsura, A. & Papathanassiu, A. (1994). Enantioselective and reversible inhibition of trypsin and α-chymotrypsin by phosphonate esters. Biochemistry 33, 8128-8138.
49. Pocker, Y. & Sarkanen, S. (1978). Oxonase and esterase activities of erythrocyte carbonic anhydrase. Biochemistry 17, 1110-1118.
50. Earnhardt, J.N. & Silverman, D.N. (1998). Carbonic anhydrase. In Comprehensive Biological Catalysis. (Sinnott, M., ed.), pp. 483-495, Academic Press, London.
51. Koester, M.K., Pullan, L.M. & Noltmann, E.A. (1981). The p-nitrophenyl phosphatase activity of muscle carbonic anhydrase. Arch. Biochem. Biophys. 211, 632-642.
52. Pullan, L.M. & Noltmann, E.A. (1985). Specific arginine modification at the phosphatase site of muscle carbonic anhydrase. Biochemistry 24, 635-640.
53. Cabiscol, E. & Levine, R.L. (1995). Carbonic anhydrase III: Oxidative modification in vivo and loss of phosphatase activity during aging. J. Biol. Chem. 270, 14742-14747.
54. Cabiscol, E. & Levine, R.L. (1996). The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation. Proc. Natl Acad. Sci. USA 93, 4170-4174.
55. Means, G.E. & Bender, M.L. (1975). Acetylation of human serum albumin by p-nitrophenyl acetate. Biochemistry 14, 4989-4994.
56. Hollfelder, F., Kirby, A.J. & Tawfik, D.S. (1996). Off-the-shelf proteins that rival tailor-made antibodies as catalysts. Nature 383, 60-63.
57. Kikuchi, K., Thorn, S.N. & Hilvert, D. (1996). Albumin-catalyzed proton transfer. J. Am. Chem. Soc. 118, 8184-8185.
58. Awad-Elkarim, A. & Means, G.E. (1988). The reactivity of p-nitrophenyl acetate with serum albumins. Comp. Biochem. Physiol. B. 91, 267-272.
59. Shaw, E. (1970). Chemical modification by active-site-directed reagents. In The Enzymes. (Boyer, P.D., ed.), pp. 91-146, Academic Press, New York.
60. Bond, C.S., et al., & Guss, J.M (1997). Structure of a human lysosomal sulfatase. Structure 5, 277-289.
61. Lukatela, G., et al., & Saenger, W. (1998). 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, 3654-3664.
62. O'Brien, P.J. & Herschlag, D. (1998). Sulfatase activity of E. coli alkaline phosphatase demonstrates a functional link to arylsulfatases, an evolutionarily related enzyme family. J. Am. Chem. Soc. 120, 12369-12370.
63. Claire, T., Lee, H.Y., Liotta, L.A. & Stracke, M.L. (1997). Autotaxin is an exoenzyme possessing 5′-nucleotide phosphodiesterase/ATP pyrophosphatase and ATPase activities. J. Biol. Chem. 272, 996-1001.
64. Oda, Y., Kuo, M.-D., Huang, S.S. & Huang, J.S. (1993). The major acidic fibroblast growth factor (aFGF)-stimulated phosphoprotein from bovine liver plasma membranes has aFGF-stimulated kinase, autoadenylation, and alkaline phosphodiesterase activities. J. Biol. Chem. 268, 27318-27326.
65. Kakuta, Y., Pedersen, L.G., Carter, C.W., Negishi, M. & Pedersen, L.C. (1997). Crystal structure of estrogen sulphotransferase. Nat. Struct. Biol. 4, 904-908.
66. Peliska, J.A. & O'Leary, M.H. (1989). Sulfuryl transfer catalyzed by pyruvate kinase. Biochemistry 28, 1604-1611.
67. Hemrika, W., Renirie, R., Dekker, H.L, Barnett, P. & Wever, R. (1997). From phosphatases to vanadium peroxidases: A similar architecture of the active site. Proc. Natl Acad. Sci. USA 94, 2145-2149.
68. Neuwald, A.F. (1997). An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases. Protein Sci. 6, 1764-1767.
69. Stukey, J. & Carman, G.M. (1997). Identification of a novel phosphatase sequence motif. Protein Sci. 6, 469-472.
70. van Etten, R.L, Waymack, P.P. & Rehkop, D.M. (1974). Transition metal ion inhibition of enzyme-catalyzed phosphate ester displacement reaction. J. Am. Chem. Soc. 96, 6782-6785.
71. Stankiewicz, P.J. & Gresser, M.J. (1988). Inhibition of phosphatase and sulfatase by transition-state analogues. Biochemistry 27, 206-212.
72. Messerschmidt, A. & Wever, R. (1996). X-ray structure of a vanadium-containing enzyme: Chloroperoxidase from the fungus Curvalaria inaequalis. Proc. Natl Acad. Sci. USA 93, 392-396.
73. Messerschmidt, A., Prade, L. & Wever, R. (1997). Implications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form. Biol. Chem. 378, 309-315.
74. Butler, A. (1998). Vanadium haloperoxidases. Curr. Opin. Chem. Biol. 2, 279-285.
75. Skarstedt, M.T. & Greer, S.B. (1973). Threonine synthetase of Bacillus subtilis: The nature of an associated dehydratase activity. J. Biol. Chem. 248, 1032-1044.
76. Parsot, C. (1986). Evolution of biosynthetic pathways: A common ancestor for threonine synthase, threonine dehydratase, and D-serine dehydratase. EMBO J. 5, 3013-3019.
77. Laber, B., Gerbling, K.-P., Harde, C., Neff, K.-H., Nordhoff, E. & Pohlenz, H.-D. (1994). Mechanisms of interaction of E. Coli threonine synthase with substrates and inhibitors. Biochemistry 33, 3413-3423.
78. John, R.A., (1998). Pyridoxal phosphate-dependent enzymes. In Comprehensive Biological Catalysis. pp 173-200 (Sinnot, M., ed.) Academic Press, London.
79. Graber, R., et al., & Christen, P. (1995). Changing the reaction specificity of a pyridoxal-5′-phosphate-dependent enzyme. Eur. J. Biochem. 232, 686-690.
80. Vacca, R.A., Giannattasio, S., Graber, R., Sandmeier, E., Marra, E. & Christen, P. (1997). Active-site Arg → Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase. J. Biol. Chem. 272, 21932-21937.
81. Cronin, C.N., Malcolm, B.A. & Kirsch, J.F. (1987). Reversal of substrate charge specificity by site-directed mutagenesis of aspartate aminotransferase. J. Am. Chem. Soc. 109, 2222-2223.
82. Malashkevich, V.N., Onuffer, J.J., Kirsch, J.F. & Jansonius, J.N. (1995). Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase. Nat. Struct. Biol. 2, 548-553.
83. Chen, R., Greer, A. & Dean, A.M. (1995). A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity. Proc. Natl Acad. Sci. USA 92, 11666-11670.
84. Sakowicz, R., Gold, M. & Jones, J.B. (1995). Partial reversal of the substrate stereospecificity of an L-lactate dehydrogenase by site-directed mutagenesis. J. Am. Chem. Soc. 117, 2387-2394.
85. Zhang, J.H., Dawes, G. & Stemmer, W.P.C. (1997). Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Proc. Natl. Acad. Sci. USA 94, 4504-4509.
86. Dean, A.M. & Golding, G.B. (1997). Protein engineering reveals ancient adaptive replacements in isocitrate dehydrogenase. Proc. Natl Acad. Sci. USA 94, 3104-3109.
87. Cronin, C.N. (1998). Redesign of choline acetyltransferase specificity by protein engineering. J. Biol. Chem. 273, 24465-24469.
88. Hopfner, K.-P., Kopetzki, E., Krebe, G.-B., Bode, W., Huber, R. & Engh, R.A. (1998). New enzyme lineages by subdomain shuffling. Proc. Natl Acad. Sci. USA 95, 9813-9818.
89. Nixon, A.E., Warren, M.S. & Benkovic, S.J. (1997). Assembly of an active enzyme by the linkage of 2 protein modules. Proc. Natl Acad. Sci. USA 94, 1069-1073.
90. Crameri, A., Raillard, S.-A., Bermudez, E. & Stemmer, W.P.C. (1998). DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391, 288-291.
91. Shuman, S. (1998). Polynucleotide ligase activity of eukaryotic topoisomerase I. Molec. Cell 1, 741-748.
92. Brown, P., Shanklin, J., Whittle, E. & Somerville, C. (1998). Catalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids. Science 282, 1315-1317.
93. Jez, J. & Penning, T. (1998). Engineering 5β-reductase activity into rat liver 3α-hydroxysteroid dehydrogenase. Biochemistry 57, 9695-9705.
94. Millard, C.B., Lockridge, O. & Broomfield, C.A. (1995). Design and expression of organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase. Biochemistry 34, 15925-15933.
95. Lockridge, O., Blong, R.M., Masson, P., Foment, M.-T., Millard, C.B. & Broomfield, C.A. (1997). A single amino acid substitution, Gly1 17His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase. Biochemistry 36, 786-795.
96. Millard, C.B., Lockridge, O. & Broomfield, C.A. (1998). Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: Synergy results in a somanase. Biochemistry 37, 237-247.
97. Campbell, P.M., Trott, J.F., Claudianos, C., Smyth, K.A., Russell, R.J. & Oakeshott, J.G. (1997). Biochemistry of esterases associated with organophosphate resistance in Lucilia cuprina with comparisons to putative orthologues in other Diptera. Biochem. Genet. 35, 1 7-40.
98. Newcomb, R.D., Campbell, P.M., Ollis, D.L, Cheah, E., Russell, R.J. & Oakeshott, J.G. (1997). A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly. Proc. Natl. Acad. Sci. USA 94, 7464-7468.
99. Dufour, E., Storer, A.C. & Menard, R. (1995). Engineering nitrile hydratase activity into a cysteine protease by a single mutation. Biochemistry 34, 16382-16388.
100. Boehlein, S.K., Rosa-Rodriguez, J.G., Schuster, S.M. & Richards, N.G.J. (1997). Catalytic activity of the N-terminal domain of Escherichia coli asparagine synthetase B can be reengineered by a single-point mutation. J. Am. Chem. Soc. 119, 5785-5791.
101. Quemeneur, E., Moutiez, M., Charbonnier, J.-B. & Menez, A. (1998). Engineering cyclophilin into a proline-specific endopeptidase. Nature 391, 301-304.
102. Dreyer, M.K. & Shulz, G.E. (1996). Refined high-resolution structure of the metal-ion dependent l-fuculose-1-phosphate aldolase (class II) from Escherichia coli. Acta Crystallogr. D 52, 1082-1091.
103. Dreyer, M.K. & Schulz, G.E. (1996). Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. J. Mol. Biol. 259, 458-466.
104. Johnson, A.E. & Tanner, M.E. (1997). Epimerization via carbon-carbon bond cleavage. L-ribulose-5-phosphate 4-epimerase as a masked class II aldolase. Biochemistry 37, 5764-5754.
105. Piatigorsky, J. & Wistow, G. (1991). The recruitment of crystallins: New functions precede gene duplication. Science 252, 1078-1079.
106. Farber, G.K. & Petsko, G.A. (1990). The evolution of α/β barrel enzymes. Trends Biochem. Sci. 15, 228-234.
107. Farber, G.K. (1993). An α/β-barrel full of evolutionary trouble. Curr Opin. Struct. Biol. 3, 409-412.
108. Reardon, D. & Farber, G.K. (1995). The structure and evolution of α/β barrel proteins. FASEB J. 9, 497-503.
109. Murzin, A.G., Brenner, S.E., Hubbard, T. & Chothia, C. (1995). SCOP: A structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540.
110. Radzicka, A. & Wolfenden, R. (1995). A proficient enzyme. Science 267, 90-93.
111. Jackson, R.C. & Handshumacher, R.E. (1970). Escherichia coli L-asparaginase. Catalytic activity and subunit nature. Biochemistry 9, 3585-3590.
112. Gan, K.N., Smolen, A., Eckerson, H.W. & Du, B.N.L (1991 ). Purification of human serum paraoxonase/arylesterase: Evidence for one esterase catalyzing both activities. Drug Metab. Dispos. 19, 100-106.
113. Ba-Saif, S.A., Davis, A.M. & Williams, A. (1989). Effective charge distribution for attack of phenoxide ion on aryl methyl phosphate monoanion: Studies related to the action of ribonuclease. J. Org. Chem. 54, 5483-5486.
114. Hay, R.W. & Govan, N. (1996). The reactivity of metal-hydroxo nucleophiles and a range of bases in the hydrolysis of the phosphate triester 2,4-dinitrophenyl diethyl phosphate. Polyhedron 15, 2381-2386.
115. Kirby, A.J. & Jencks, W.P. (1965). The reactivity of nucleophilic reagents roward the p-nitrophenyl phosphate dianion. J. Am. Chem. Soc. 87, 3209-3216.
116. Shaw, E. & Ruscica, J. (1971). The reactivity of His-57 in chymotrypsin to alkylation. Arch. Biochem. Biophys. 145, 484-489.
117. Nakagawa, Y. & Bender, M.L. (1969). Modification of α-chymotrypsin by methyl p-nitrobenzenesulfonate. J. Am. Chem. Soc. 91, 1566-1567.
118. Yebra, M.J. & Bhagwat, A.S. (1995). A cytosine methyltransferase converts 5-methylcytosine in DNA to thymine. Biochemistry 34, 14752-14757.
119. Ozaki, S., Matsui, T. & Watanabe, Y. (1996). Conversion of myoglobin into a highly stereospecific peroxygenase by the L29H/H64L mutation. J. Am. Chem. Soc. 118, 9784-9785.
120. van de Velde, F., Konemann, L, Rantwijk, R.V. & Sheldon, R.A. (1998). Enantioselective sulfoxidation mediated by vanadium-incorporated phytase: A hydrolase acting as a peroxidase. Chem. Commun. 17, 1891-1892.
121. Matsui, T., Nagano, S., Ishimori, K., Watanabe, Y. & Morishima, I. (1996). Preparation and reactions of myoglobin mutants bearing both proximal cysteine ligand and hydrophobic distal cavity: Protein models for the active site of P-450. J. Am. Chem. Soc. 35, 13118-13124.
122. Ozaki, S.-I., Matsui, T. & Watanabe, Y. (1997). Conversion of a myoglobin into a peroxygenase: A catalytic intermediate of sulfoxidation and epoxidation by the F34H/H64L mutant. J. Am. Chem. Soc. 119, 6666-6667.
123. Wan, L., Twitchett, M.B., Eltis, L.D., Mauk, A.G. & Smith, M. (1998). In vitro evolution of horse heart myoglobin to increase peroxidase activity. Proc. Natl Acad. Sci. USA 95, 12825-12831.
124. Reid, T.W. & Fahrney, D. (1967). The pepsin-catalyzed hydrolysis of sulfite esters. J. Am. Chem. Soc. 89, 3941-3943.
125. Shim, H, Hong, S. & Raushel, F.M. (1998). Hydrolysis of phosphodiesters through transformation of the bacterial phosphotriesterase. J. Biol. Chem. 273, 17445-17450.
126. Chin, J., Banaszczyk, M., Jubian, V. & Zou, X. (1989). Co(III) complex promoted hydrolysis of phosphate diesters: Comparison in reactivity of rigid cis-diaquotetraazacobalt(III) complexes. J. Am. Chem. Soc. 111, 186-190.
127. Jencks, W.P. & Carriuolo, J. (1959). Reactivity of nucleophilic reagents toward esters. J. Am. Chem. Soc. 82, 1778-1786.
128. Andrews, R.K., Dexter, A., Blakeley, R.L. & Zerner, B. (1986). Jack bean urease (EC 3.5.1.5). On the inhibition of urease by amides and esters of phosphoric acid. J. Am. Chem. Soc. 108, 7124-7125.
129. Peliska, J.A. & O'Leary, M.H. (1991 ). Sulfuryl transfer catalyzed by phosphokinases. Biochemistry 30(4), 1049-1057.
130. Rezende, A.A., Pizauro, J.M., Ciancaglini, P. & Leone, F.A. (1994). Phosphodiesterase activity is a novel property of alkaline phosphatase from osseous plate. Biochem. J. 301, 517-522.
131. Smile, D.H., Donohue, M., Yeh, M., Kenkel, T. & Trela, J.M. (1976). Repressible alkaline phosphatase from Thermus aquaticus. J. Biol. Chem. 252, 3399-3401.
132. Uchida, T., Egami, F. & Roy, A.B. (1981). 3′,5′-cyclic nucleotide phosphodiesterase activity of the sulfatase A of ox liver. Biochimica Biophys. Acta 657, 356-363.
133. Chin, J. & Zou, X. (1987). Catalytic hydrolysis of cAMP. Can. J. Chem. 65, 1882-1884.
134. John, R.A. & Tudball, N. (1972). Evidence for induced fit of a pseudo-substrate of aspartate aminotransferase. Eur. J. Biochem. 31, 135-138.
135. John, R.A. & Fasella, P. (1969). The reaction of L-serine O-sulfate with aspartate aminotransferase. Biochemistry 8, 4477-4482.
136. Fujimoto, M., Kuninaka, A. & Yoshino, H. (1974). Identity of phosphodiesterase and phosphomonesterase activities with nuclease P1 (a nuclease from Penicillium citrinum). Agr. Biol. Chem. 38, 785-790.
137. Polya, G.M., Brownlee, A.G. & Hynes, M.J. (1975). Enzymology and genetic regulation of a cyclic nucleotide-binding phosphodiesterase-phosphomonoesterase from Aspergillus nidulans. J. Bacteriol. 124, 693-703.
138. Richardson, C.C. & Kornberg, A. (1964). A deoxyribonucleic acid phosphatase-exonuclease from Escherichia coli. I. Purification of the enzyme and characterization of the phosphatase activity. J. Biol. Chem. 239, 242-250.
139. Yamane, K. & Maruo, B. (1978). Alkaline phosphatase possessing alkaline phosphodiesterase activity and other phosphodiesterases in Bacillus subtilis. J. Bacteriol. 134, 108-114.
140. Palmer, D.R.J. & Gerlt, J.A. (1996). Evolution of enzymatic activities: Multiple pathways for generating and partitioning a common enolic intermediate by glucarate dehydratase from Pseudomonas putida. J. Am. Chem. Soc. 118, 10323-10324.
141. Tokuyama, S. & Hatano, K. (1995). Cloning, DNA sequencing, and heterologous expression of the gene for thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1 -60 in Escherichia coli. Appl. Microbiol. Biotechnol. 42, 884-889.
142. Chang, Y.-Y. & Cronan, J.E. (1988). Common ancestory of Escherichi coli pyruvate oxidase and the acetohydroxy acid synthases of the branched-chain amino acid biosynthetic pathway. J. Bacteriol. 170, 3937-3945.
143. Kim, E.E. & Wyckoff, H.W. (1991 ). Reaction mechanism of alkaline phosphatase based on crystal structures. J. Mol. Biol. 218, 449-464.
144. 2+. Proteins 32, 276-288.