메뉴 건너뛰기




Volumn 36, Issue 10, 2003, Pages 757-765

Avoiding the Road Less Traveled: How the Topology of Enzyme-Substrate Complexes Can Dictate Product Selection

Author keywords

[No Author keywords available]

Indexed keywords

1 AMINOCYCLOPROPANECARBOXYLATE SYNTHASE; 7,8 DIAMINOPELARGONIC ACID SYNTHASE; BUTYRIC ACID DERIVATIVE; PYRIDOXAL 5 PHOSPHATE; QUINONE DERIVATIVE; S ADENOSYL 4 METHYLTHIO 2 OXOBUTANOATE; S ADENOSYLMETHIONINE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 0142213274     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar0202767     Document Type: Article
Times cited : (13)

References (35)
  • 1
    • 0142191983 scopus 로고    scopus 로고
    • note
    • Abbreviations: AATase, aspartate aminotransferase; ACC, 1-aminocyclopropane-1-carboxylate; AVG, L-aminoethoxyvinylglycine; AMPSO, N-(1,1-dimethyl-2-hydroxyethyl)-3-amino-2-hydroxypropanesulfonic acid; CSA, cysteine sulfinic acid; DAPA, 7,8-diaminopelargonic acid (7,8-diaminononanoic acid); dcSAM, decarboxylated SAM (S-adenosyl-(5′ )-3-methylthiopropylamine); DTT, dithiothreitol; EDTA, ethylenediaminetetraacetic acid; KAPA, 7-keto-8-aminopelargonic acid (8-amino-7-oxononanoic acid); MES, 2-(N-morpholino)ethanesulfonic acid; MOPS, 3-(N-morpholino)propanesulfonic acid; MTA, 5′-deoxy-5′ -methylthioadenosine; oxo-SAM, S-adenosyl-4-methylthio-2-oxobutanoate; PLP, pyridoxal 5′-phosphate; PMP, pyridoxamine 5′-phosphate; SAM, S-adenosyl-L-methionine; WT, wild-type.
  • 2
    • 0035997385 scopus 로고    scopus 로고
    • Formation of Unusual Sugars: Mechanistic Studies and Biosynthetic Applications
    • He, X. M.; Liu, H. W. Formation of Unusual Sugars: Mechanistic Studies and Biosynthetic Applications. Annu. Rev. Biochem. 2002, 71, 701-754.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 701-754
    • He, X.M.1    Liu, H.W.2
  • 3
    • 0010386231 scopus 로고    scopus 로고
    • GABA Signalling Therapeutic Targets for Epilepsy, Parkinson's Disease and Huntington's Disease
    • Kleppner, S. R.; Tobin, A. J. GABA Signalling: Therapeutic Targets for Epilepsy, Parkinson's Disease and Huntington's Disease. Emerging Ther. Targets 2001, 5, 219-239.
    • (2001) Emerging Ther. Targets , vol.5 , pp. 219-239
    • Kleppner, S.R.1    Tobin, A.J.2
  • 4
    • 0024601238 scopus 로고
    • Effects of a Triazine Antifolate (NSC 127755) on Serine Hydroxymethyltransferase in Myeloma Cells in Culture
    • Snell, K.; Riches, D. Effects of a Triazine Antifolate (NSC 127755) on Serine Hydroxymethyltransferase in Myeloma Cells in Culture. Cancer Lett. 1989, 44, 217-220.
    • (1989) Cancer Lett. , vol.44 , pp. 217-220
    • Snell, K.1    Riches, D.2
  • 6
    • 0033649909 scopus 로고    scopus 로고
    • The Molecular Evolution of Pyridoxal-5′-Phosphate-Dependent Enzymes
    • Mehta, P. K.; Christen, P. The Molecular Evolution of Pyridoxal-5′-Phosphate-Dependent Enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 1998, 74, 129-183.
    • (1998) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.74 , pp. 129-183
    • Mehta, P.K.1    Christen, P.2
  • 8
    • 0013902457 scopus 로고
    • Conformation and Reaction Specificity in Pyridoxal Phosphate Enzymes
    • Dunathan, H. C. Conformation and Reaction Specificity in Pyridoxal Phosphate Enzymes. Proc. Natl. Acad. Sci. U.S.A. 1966, 55, 712-716.
    • (1966) Proc. Natl. Acad. Sci. U.S.A. , vol.55 , pp. 712-716
    • Dunathan, H.C.1
  • 9
    • 0032539994 scopus 로고    scopus 로고
    • Reactions of Alternate Substrates Demonstrate Stereoelectronic Control of Reactivity in Dialkylglycine Decarboxylase
    • Sun, S.; Zabinski, R. F.; Toney, M. D. Reactions of Alternate Substrates Demonstrate Stereoelectronic Control of Reactivity in Dialkylglycine Decarboxylase. Biochemistry 1998, 37, 3865-3875.
    • (1998) Biochemistry , vol.37 , pp. 3865-3875
    • Sun, S.1    Zabinski, R.F.2    Toney, M.D.3
  • 10
    • 0026783258 scopus 로고
    • Escherichia coli Serine Hydroxymethyltransferase: The role of histidine 228 in determining reaction specificity
    • Stover, P.; Zamorga, M.; Shostak, K.; Gautam-Basak, M.; Schirch, V. Escherichia coli Serine Hydroxymethyltransferase: the role of histidine 228 in determining reaction specificity. J. Biol. Chem. 1992, 267, 17679-17687.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17679-17687
    • Stover, P.1    Zamorga, M.2    Shostak, K.3    Gautam-Basak, M.4    Schirch, V.5
  • 11
    • 0030822630 scopus 로고    scopus 로고
    • Active-site Arg → Lys Substitutions Alter Reaction and Substrate Specificity of Aspartate Aminotransferase
    • Vacca, R. A.; Giannattasio, S.; Graber, R.; Sandmeier, E.; Marra, E.; Christen, P. Active-site Arg → Lys Substitutions Alter Reaction and Substrate Specificity of Aspartate Aminotransferase. J. Biol. Chem. 1997, 272, 21932-21937.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21932-21937
    • Vacca, R.A.1    Giannattasio, S.2    Graber, R.3    Sandmeier, E.4    Marra, E.5    Christen, P.6
  • 12
    • 0033615621 scopus 로고    scopus 로고
    • Conversion of Aspartate Aminotransferase into an L-Aspartate β-Decarboxylase by a Triple Active-site Mutation
    • Graber, R.; Kasper, P.; Malashkevich, V.; Strop, P.; Gehring, H.; Jansonius, J. N.; Christen, P. Conversion of Aspartate Aminotransferase into an L-Aspartate β-Decarboxylase by a Triple Active-site Mutation. J. Biol. Chem. 1999, 274, 31203-31208.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31203-31208
    • Graber, R.1    Kasper, P.2    Malashkevich, V.3    Strop, P.4    Gehring, H.5    Jansonius, J.N.6    Christen, P.7
  • 14
    • 0001212489 scopus 로고
    • Ethylene Biosynthesis and its Regulation in Higher Plants
    • Yang, S. F.; Hoffman, N. E. Ethylene Biosynthesis and its Regulation in Higher Plants. Annu. Rev. Plant Physiol. 1984, 35, 155-189.
    • (1984) Annu. Rev. Plant Physiol. , vol.35 , pp. 155-189
    • Yang, S.F.1    Hoffman, N.E.2
  • 15
    • 0025913925 scopus 로고
    • Two Genes Encoding 1-Aminocyclopropane-1-Carboxylate Synthase in Zucchini (Cucurbita pepo) are Clustered and Similar but Differentially Regulated
    • Huang, P. L.; Parks, J. E.; Rottmann, W. H.; Theologis, A. Two Genes Encoding 1-Aminocyclopropane-1-Carboxylate Synthase in Zucchini (Cucurbita pepo) are Clustered and Similar but Differentially Regulated. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 7021-7025.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 7021-7025
    • Huang, P.L.1    Parks, J.E.2    Rottmann, W.H.3    Theologis, A.4
  • 16
    • 0028358526 scopus 로고
    • Homology of 1-Aminocyclopropane-1-carboxylate Synthase, 8-Amino-7-oxononanoate Synthase, 2-Amino-6-caprolactam Racemase, 2,2-Dialkylglycine Decarboxylase, Glutamate-1-semialdehyde 2,1-Aminomutase and Isopenicillin-N-epimerase with Aminotransferases
    • Mehta, P. K.; Christen, P. Homology of 1-Aminocyclopropane-1-carboxylate Synthase, 8-Amino-7-oxononanoate Synthase, 2-Amino-6-caprolactam Racemase, 2,2-Dialkylglycine Decarboxylase, Glutamate-1-semialdehyde 2,1-Aminomutase and Isopenicillin-N-epimerase with Aminotransferases. Biochem. Biophys. Res. Commun. 1994, 198, 138-143.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 138-143
    • Mehta, P.K.1    Christen, P.2
  • 17
    • 0033521228 scopus 로고    scopus 로고
    • Structure of 1-Aminocyclopropane-1-carboxylate Synthase, a Key Enzyme in the Biosynthesis of the Plant Hormone Ethylene
    • Capitani, G.; Hohenester, E.; Feng, L.; Storici, P.; Kirsch, J. F.; Jansonius, J. N. Structure of 1-Aminocyclopropane-1-carboxylate Synthase, a Key Enzyme in the Biosynthesis of the Plant Hormone Ethylene. J. Mol. Biol. 1999, 294, 745-756.
    • (1999) J. Mol. Biol. , vol.294 , pp. 745-756
    • Capitani, G.1    Hohenester, E.2    Feng, L.3    Storici, P.4    Kirsch, J.F.5    Jansonius, J.N.6
  • 18
    • 0035901517 scopus 로고    scopus 로고
    • Structures of Escherichia coli Histidinol-phosphate Aminotransferase and its Complexes with Histidinol-phosphate and N-(5′ -Phosphopyridoxyl)-L-glutamate: Double Substrate Recognition of the Enzyme
    • Haruyama, K.; Nakai, T.; Miyahara, I.; Hirotsu, K.; Mizuguchi, H.; Hayashi, H.; Kagamiyama, H. Structures of Escherichia coli Histidinol-phosphate Aminotransferase and its Complexes with Histidinol-phosphate and N-(5′-Phosphopyridoxyl)-L-glutamate: Double Substrate Recognition of the Enzyme. Biochemistry 2001, 40, 4633-4644.
    • (2001) Biochemistry , vol.40 , pp. 4633-4644
    • Haruyama, K.1    Nakai, T.2    Miyahara, I.3    Hirotsu, K.4    Mizuguchi, H.5    Hayashi, H.6    Kagamiyama, H.7
  • 19
    • 0034642189 scopus 로고    scopus 로고
    • Aminotransferase Activity and Bioinformatic Analysis of 1-Aminocyclopropane-1-carboxylate Synthase
    • Feng, L.; Geck, M. K.; Eliot, A. C.; Kirsch, J. F. Aminotransferase Activity and Bioinformatic Analysis of 1-Aminocyclopropane-1-carboxylate Synthase. Biochemistry 2000, 39, 15242-15249.
    • (2000) Biochemistry , vol.39 , pp. 15242-15249
    • Feng, L.1    Geck, M.K.2    Eliot, A.C.3    Kirsch, J.F.4
  • 20
    • 0029078229 scopus 로고
    • Accumulation of the Quinonoid Intermediate in the Reaction Catalyzed by Aspartate Aminotransferase with Cysteine Sulfinic Acid
    • Furumo, N. C.; Kirsch, J. F. Accumulation of the Quinonoid Intermediate in the Reaction Catalyzed by Aspartate Aminotransferase with Cysteine Sulfinic Acid. Arch. Biochem. Biophys. 1995, 319, 49-54.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 49-54
    • Furumo, N.C.1    Kirsch, J.F.2
  • 21
    • 0346037270 scopus 로고    scopus 로고
    • Apple 1-Aminocyclopropane-1-carboxylate Synthase in Complex with the Inhibitor L-Aminoethoxyvinylglycine, evidence for a ketimine intermediate
    • Capitani, G.; McCarthy, D. L.; Gut, H.; Grütter, M. G.; Kirsch, J. F. Apple 1-Aminocyclopropane-1-carboxylate Synthase in Complex with the Inhibitor L-Aminoethoxyvinylglycine, evidence for a ketimine intermediate. J. Biol. Chem. 2002, 277, 49735-49742.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49735-49742
    • Capitani, G.1    McCarthy, D.L.2    Gut, H.3    Grütter, M.G.4    Kirsch, J.F.5
  • 22
    • 0034646183 scopus 로고    scopus 로고
    • L-Vinylglycine is an Alternative Substrate as Well as a Mechanism-based Inhibitor of 1-Aminocyclopropane-1-carboxylate Synthase
    • Feng, L.; Kirsch, J. F. L-Vinylglycine is an Alternative Substrate as Well as a Mechanism-based Inhibitor of 1-Aminocyclopropane-1-carboxylate Synthase. Biochemistry 2000, 39, 2436-2444.
    • (2000) Biochemistry , vol.39 , pp. 2436-2444
    • Feng, L.1    Kirsch, J.F.2
  • 23
    • 0000367461 scopus 로고
    • Inactivation of 1-Aminocyclopropane-1-carboxylate Synthase by L-Vinylglycine as Related to the Mechanism-based Inactivation of the Enzyme by S-Adenosyl-L-methionine
    • Satoh, S.; Yang, S. F. Inactivation of 1-Aminocyclopropane-1-carboxylate Synthase by L-Vinylglycine as Related to the Mechanism-based Inactivation of the Enzyme by S-Adenosyl-L-methionine. Plant Physiol. 1989, 91, 1036-1039.
    • (1989) Plant Physiol. , vol.91 , pp. 1036-1039
    • Satoh, S.1    Yang, S.F.2
  • 24
    • 0035900007 scopus 로고    scopus 로고
    • Glutamate 47 in 1-Aminocyclopropane-1-carboxylate Synthase is a Major Specificity Determinant
    • McCarthy, D. L.; Capitani, G.; Feng, L.; Gruetter, M. G.; Kirsch, J. F. Glutamate 47 in 1-Aminocyclopropane-1-carboxylate Synthase is a Major Specificity Determinant. Biochemistry 2001, 40, 12276-12284.
    • (2001) Biochemistry , vol.40 , pp. 12276-12284
    • McCarthy, D.L.1    Capitani, G.2    Feng, L.3    Gruetter, M.G.4    Kirsch, J.F.5
  • 25
    • 0142161057 scopus 로고    scopus 로고
    • note
    • 33,34 and is inactivated once every 500 turnovers of L-vinylglycine.22 Assuming that the inactivation by SAM is entirely the result of β,γ-elimination to generate a vinylglycine-related intermediate and that this intermediate partitions just as in the reaction with free vinylglycine, then the ratio of α,γ- to β,γ-elimination in the reaction with SAM is approximately 30 000/500 = 60.
  • 26
    • 0014549461 scopus 로고
    • Uptake of Pimelic Acid by Escherichia coli and Pseudomonas denitrificans
    • Pai, C. H.; McLaughlin, G. E. Uptake of Pimelic Acid by Escherichia coli and Pseudomonas denitrificans. Can. J. Microbiol. 1969, 15, 809-810.
    • (1969) Can. J. Microbiol. , vol.15 , pp. 809-810
    • Pai, C.H.1    McLaughlin, G.E.2
  • 27
    • 0242538842 scopus 로고    scopus 로고
    • Crystal structure of Diaminopelargonic Acid Synthase: Evolutionary Relationships Between Pyridoxal-5′-phosphate-dependent Enzymes
    • Käck, H.; Sandmark, J.; Gibson, K.; Schneider, G.; Lindqvist, Y. Crystal structure of Diaminopelargonic Acid Synthase: Evolutionary Relationships Between Pyridoxal-5′-phosphate-dependent Enzymes. J. Mol. Biol. 1999, 291, 857-876.
    • (1999) J. Mol. Biol. , vol.291 , pp. 857-876
    • Käck, H.1    Sandmark, J.2    Gibson, K.3    Schneider, G.4    Lindqvist, Y.5
  • 28
    • 0037159244 scopus 로고    scopus 로고
    • The Dual-Specific Active Site of 7,8-Diaminopelargonic Acid Synthase and the Effect of the R391A Mutation
    • Eliot, A. C.; Sandmark, J.; Schneider, G.; Kirsch, J. F. The Dual-specific Active Site of 7,8-Diaminopelargonic Acid Synthase and the Effect of the R391A Mutation. Biochemistry 2002, 41, 12582-12589.
    • (2002) Biochemistry , vol.41 , pp. 12582-12589
    • Eliot, A.C.1    Sandmark, J.2    Schneider, G.3    Kirsch, J.F.4
  • 29
    • 0029981787 scopus 로고    scopus 로고
    • The Reaction Catalyzed by Escherichia coli Aspartate Aminotransferase Has Multiple Partially Rate-determining Steps, While that Catalyzed by the Y225F Mutant is Dominated by Ketimine Hydrolysis
    • Goldberg, J. M.; Kirsch, J. F. The Reaction Catalyzed by Escherichia coli Aspartate Aminotransferase Has Multiple Partially Rate-determining Steps, While that Catalyzed by the Y225F Mutant is Dominated by Ketimine Hydrolysis. Biochemistry 1996, 35, 5280-5291.
    • (1996) Biochemistry , vol.35 , pp. 5280-5291
    • Goldberg, J.M.1    Kirsch, J.F.2
  • 32
    • 0026504874 scopus 로고
    • Mechanism of Racemization of Amino Acids by Aspartate Aminotransferase
    • Kochhar, S.; Christen, P. Mechanism of Racemization of Amino Acids by Aspartate Aminotransferase. Eur. J. Biochem. 1992, 203, 563-569.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 563-569
    • Kochhar, S.1    Christen, P.2
  • 33
    • 0028604575 scopus 로고
    • Expression of Apple 1-Aminocyclopropane-1-carboxylate synthase in Escherichia coli: Kinetic Characterization of Wild-Type and Active-site Mutant forms
    • White, M. F.; Vasquez, J.; Yang, S. F.; Kirsch, J. F. Expression of Apple 1-Aminocyclopropane-1-carboxylate synthase in Escherichia coli: Kinetic Characterization of Wild-type and Active-site Mutant forms. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 12428-12432.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12428-12432
    • White, M.F.1    Vasquez, J.2    Yang, S.F.3    Kirsch, J.F.4
  • 34
    • 0024970472 scopus 로고
    • Specificity of S-Adenosyl-L-methionine in the Inactivation and the Labeling of 1-Aminocyclopropane-1-carboxylate Synthase Isolated from Tomato Fruits
    • Satoh, S.; Yang, S. F. Specificity of S-Adenosyl-L-methionine in the Inactivation and the Labeling of 1-Aminocyclopropane-1-carboxylate Synthase Isolated from Tomato Fruits. Arch. Biochem. Biophys. 1989, 271, 107-112.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 107-112
    • Satoh, S.1    Yang, S.F.2
  • 35
    • 0022450919 scopus 로고
    • Recent Advances in the Biochemistry of Polyamines in Eukaryotes
    • Pegg, A. E. Recent Advances in the Biochemistry of Polyamines in Eukaryotes. Biochem. J. 1986, 234, 248-262.
    • (1986) Biochem. J. , vol.234 , pp. 248-262
    • Pegg, A.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.