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Volumn 11, Issue 10, 2004, Pages 1383-1394

Crystal structure and mechanistic implications of 1-aminocyclopropane-1- carboxylic acid oxidase - The ethylene-forming enzyme

Author keywords

[No Author keywords available]

Indexed keywords

1 AMINOCYCLOPROPANE 1 CARBOXYLIC ACID OXIDASE; 1-AMINOCYCLOPROPANE-1-CARBOXYLIC ACID OXIDASE; ARGININE; ETHYLENE FORMING ENZYME; LYASE; OXIDOREDUCTASE; VEGETABLE PROTEIN;

EID: 5544323881     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2004.08.012     Document Type: Article
Times cited : (123)

References (52)
  • 1
    • 0030754175 scopus 로고    scopus 로고
    • Ethylene biosynthesis: The role of 1-aminocyclopropane-1-carboxylate (ACC) oxidase, and its possible evolutionary origin
    • John P. Ethylene biosynthesis. the role of 1-aminocyclopropane-1- carboxylate (ACC) oxidase, and its possible evolutionary origin Physiol. Plant. 100:1997;583-592
    • (1997) Physiol. Plant. , vol.100 , pp. 583-592
    • John, P.1
  • 2
    • 0032878824 scopus 로고    scopus 로고
    • Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid
    • Pirrung M.C. Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid. Acc. Chem. Res. 32:1999;711-718
    • (1999) Acc. Chem. Res. , vol.32 , pp. 711-718
    • Pirrung, M.C.1
  • 4
    • 0001587338 scopus 로고
    • Ethylene the gaseous plant hormone - Mechanism and regulation of biosysnthesis
    • Adam D.O., Yang S.F. Ethylene the gaseous plant hormone - mechanism and regulation of biosysnthesis. Trends Biochem. Sci. 6:1981;161-164
    • (1981) Trends Biochem. Sci. , vol.6 , pp. 161-164
    • Adam, D.O.1    Yang, S.F.2
  • 5
    • 0000581881 scopus 로고
    • Ethylene biosynthesis: Identification of ACC as an intermediate in the conversion of methionine to ethylene
    • Adam D.O., Yang S.F. Ethylene biosynthesis. identification of ACC as an intermediate in the conversion of methionine to ethylene Proc. Natl. Acad. Sci. USA. 76:1979;170-174
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 170-174
    • Adam, D.O.1    Yang, S.F.2
  • 6
    • 0033521228 scopus 로고    scopus 로고
    • Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of 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 plant hormone ethylene. J. Mol. Biol. 294:1999;749-756
    • (1999) J. Mol. Biol. , vol.294 , pp. 749-756
    • Capitani, G.1    Hohenester, E.2    Feng, L.3    Storici, P.4    Kirsch, J.F.5    Jansonius, J.N.6
  • 7
    • 0001375191 scopus 로고
    • Antisense gene that inhibits synthesis of the hormone ethylene in transgenic plants
    • Hamilton A.J., Lycett G.W., Grierson D. Antisense gene that inhibits synthesis of the hormone ethylene in transgenic plants. Nature. 346:1990;284-287
    • (1990) Nature , vol.346 , pp. 284-287
    • Hamilton, A.J.1    Lycett, G.W.2    Grierson, D.3
  • 8
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • Schofield C.J., Zhang Z.H. Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. Curr. Opin. Struct. Biol. 9:1999;722-731
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.H.2
  • 9
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active site: Enzymes, models and intermediates
    • Costas M., Mehn M.P., Jensen M.P., Que L. Jr. Dioxygen activation at mononuclear nonheme iron active site. enzymes, models and intermediates Chem. Rev. 104:2004;939-986
    • (2004) Chem. Rev. , vol.104 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que Jr., L.4
  • 12
    • 0038375539 scopus 로고    scopus 로고
    • Carbapenem biosynthesis: Confirmation of stereochemical assignments and the role of CarC in the ring stereoinversion process from L-Proline
    • Stapon A., Li R.-F., Townsend C.A. Carbapenem biosynthesis. confirmation of stereochemical assignments and the role of CarC in the ring stereoinversion process from L-Proline J. Am. Chem. Soc. 125:2003;8486-8493
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8486-8493
    • Stapon, A.1    Li, R.-F.2    Townsend, C.A.3
  • 14
    • 0026699542 scopus 로고
    • Purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from apple fruit
    • Dong J.G., Fernandez-Maculet J.C., Yang S.F. Purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from apple fruit. Proc. Natl. Acad. Sci. USA. 89:1992;9789-9793
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9789-9793
    • Dong, J.G.1    Fernandez-Maculet, J.C.2    Yang, S.F.3
  • 15
    • 0001213003 scopus 로고
    • Formation of cyanide from carbon 1 of 1-aminocyclopropane-1-carboxylic acid during its conversion to ethylene
    • Peiser G.D., Wang T.-T., Hoffman N.E., Yang S.F., Liu H.-w., Walsh C.T. Formation of cyanide from carbon 1 of 1-aminocyclopropane-1-carboxylic acid during its conversion to ethylene. Proc. Natl. Acad. Sci. USA. 81:1984;3059-3063
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3059-3063
    • Peiser, G.D.1    Wang, T.-T.2    Hoffman, N.E.3    Yang, S.F.4    Liu, H.-W.5    Walsh, C.T.6
  • 17
    • 0000050279 scopus 로고
    • Activation of 1-aminocyclopropane-1-carboxylate oxidase by bicarbonate/carbon dioxide
    • Smith J.J., John P. Activation of 1-aminocyclopropane-1-carboxylate oxidase by bicarbonate/carbon dioxide. Phytochemistry. 32:1993;1381-1386
    • (1993) Phytochemistry , vol.32 , pp. 1381-1386
    • Smith, J.J.1    John, P.2
  • 18
    • 1542328170 scopus 로고    scopus 로고
    • Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: Single turnover reaction
    • Rocklin A.M., Kato K., Liu H.-w., Que L. Jr., Lipscomb J.D. Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase. single turnover reaction J. Biol. Inorg. Chem. 9:2004;171-182
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 171-182
    • Rocklin, A.M.1    Kato, K.2    Liu, H.-W.3    Que Jr., L.4    Lipscomb, J.D.5
  • 22
    • 0037165643 scopus 로고    scopus 로고
    • Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate- substrate-NO complex: Evidence for metal centred rearrangements
    • Zhang Z.H., Ren J.S., Harlos K., McKinnon C.H., Clifton I.J., Schofield C.J. Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate- substrate-NO complex. evidence for metal centred rearrangements FEBS Lett. 517:2002;7-12
    • (2002) FEBS Lett. , vol.517 , pp. 7-12
    • Zhang, Z.H.1    Ren, J.S.2    Harlos, K.3    McKinnon, C.H.4    Clifton, I.J.5    Schofield, C.J.6
  • 23
    • 0030947388 scopus 로고    scopus 로고
    • Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
    • Roach P.L., Clifton I.J., Hensgens C.M., Shibata N., Schofield C.J., Hajdu J., Baldwin J.E. Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature. 387:1997;827-830
    • (1997) Nature , vol.387 , pp. 827-830
    • Roach, P.L.1    Clifton, I.J.2    Hensgens, C.M.3    Shibata, N.4    Schofield, C.J.5    Hajdu, J.6    Baldwin, J.E.7
  • 26
    • 0029802674 scopus 로고    scopus 로고
    • Heterologous expression and site-directed mutagenesis of the 1-aminocyclopropane-1-carboxylate oxidase from kiwi fruit
    • Lay V.J., Prescott A.G., Thomas P.G., John P. Heterologous expression and site-directed mutagenesis of the 1-aminocyclopropane-1-carboxylate oxidase from kiwi fruit. Eur. J. Biochem. 242:1996;228-234
    • (1996) Eur. J. Biochem. , vol.242 , pp. 228-234
    • Lay, V.J.1    Prescott, A.G.2    Thomas, P.G.3    John, P.4
  • 29
    • 0346463040 scopus 로고    scopus 로고
    • Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of flavonoid biosynthesis: Anthocyanidin synthase, flavonol synthase and flavanone 3-hydroxylase
    • Turnbull J.J., Nakajima J., Welford R.W.D., Yamazaki M., Saito K., Schofield C.J. Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of flavonoid biosynthesis. Anthocyanidin synthase, flavonol synthase and flavanone 3-hydroxylase J. Biol. Chem. 279:2004;1206-1216
    • (2004) J. Biol. Chem. , vol.279 , pp. 1206-1216
    • Turnbull, J.J.1    Nakajima, J.2    Welford, R.W.D.3    Yamazaki, M.4    Saito, K.5    Schofield, C.J.6
  • 32
    • 0035068434 scopus 로고    scopus 로고
    • Collagens and collagen-related diseases
    • Myllyharju J., Kivirikko K.I. Collagens and collagen-related diseases. Ann. Med. 33:2001;7-21
    • (2001) Ann. Med. , vol.33 , pp. 7-21
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 33
    • 0037470162 scopus 로고    scopus 로고
    • Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau
    • Lee C., Kim S.J., Jeong D.G., Lee S.M., Ryu S.E. Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau. J. Biol. Chem. 278:2003;7558-7563
    • (2003) J. Biol. Chem. , vol.278 , pp. 7558-7563
    • Lee, C.1    Kim, S.J.2    Jeong, D.G.3    Lee, S.M.4    Ryu, S.E.5
  • 35
    • 0037180452 scopus 로고    scopus 로고
    • Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway
    • Dann C.E. III, Bruick R.K., Deisenhofer J. Structure of factor-inhibiting hypoxia-inducible factor 1. an asparaginyl hydroxylase involved in the hypoxic response pathway Proc. Natl. Acad. Sci. USA. 99:2002;15351-15356
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15351-15356
    • Dann III, C.E.1    Bruick, R.K.2    Deisenhofer, J.3
  • 36
    • 0035859918 scopus 로고    scopus 로고
    • Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase
    • Thrower J.S., Blalock R. III, Klinman J.P. Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase. Biochemistry. 40:2001;9717-9724
    • (2001) Biochemistry , vol.40 , pp. 9717-9724
    • Thrower, J.S.1    Blalock III, R.2    Klinman, J.P.3
  • 37
    • 0034609545 scopus 로고    scopus 로고
    • Steady-state kinetic mechanism of recombinant avocado ACC oxidase: Initial velocity and inhibitor studies
    • Brunhuber N.M., Mort J.L., Christoffersen R.E., Reich N.O. Steady-state kinetic mechanism of recombinant avocado ACC oxidase. initial velocity and inhibitor studies Biochemistry. 39:2000;10730-10738
    • (2000) Biochemistry , vol.39 , pp. 10730-10738
    • Brunhuber, N.M.1    Mort, J.L.2    Christoffersen, R.E.3    Reich, N.O.4
  • 38
    • 0343986411 scopus 로고    scopus 로고
    • One motif - Many different reactions
    • Que L. Jr. One motif - many different reactions. Nat. Struct. Biol. 7:2000;182-184
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 182-184
    • Que Jr., L.1
  • 39
    • 0034927651 scopus 로고    scopus 로고
    • Effect of inhibitors of ethylene biosynthesis and signal transduction pathway on the mutiplication of in vitro-growth Hancornia speciosa
    • Pereira-Netto A.B. Effect of inhibitors of ethylene biosynthesis and signal transduction pathway on the mutiplication of in vitro-growth Hancornia speciosa. Plant Cell Tiss. Org. 66:2001;1-7
    • (2001) Plant Cell Tiss. Org. , vol.66 , pp. 1-7
    • Pereira-Netto, A.B.1
  • 40
    • 0031455762 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase
    • Zhang Z.H., Barlow J.N., Baldwin J.E., Schofield C.J. Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase. Biochemistry. 36:1997;15999-16007
    • (1997) Biochemistry , vol.36 , pp. 15999-16007
    • Zhang, Z.H.1    Barlow, J.N.2    Baldwin, J.E.3    Schofield, C.J.4
  • 41
    • 0034802889 scopus 로고    scopus 로고
    • Alternative reactivity of an α-ketoglutarate-dependent iron(II) oxygenase: Enzyme self-hydroxylation
    • Liu A., Raymond Y.N.H., Que L. Jr. Alternative reactivity of an α-ketoglutarate-dependent iron(II) oxygenase. enzyme self-hydroxylation J. Am. Chem. Soc. 123:2001;5126-5127
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5126-5127
    • Liu, A.1    Raymond, Y.N.H.2    Que Jr., L.3
  • 42
    • 0037389772 scopus 로고    scopus 로고
    • Interconversion of two oxidized forms of taurine/α-ketoglutarate dioxygenase, a non-heme iron hydroxylase: Evidence for bicarbonate binding
    • Ryle M.J., Koehntop K.D., Liu A., Que L. Jr., Hausinger R.P. Interconversion of two oxidized forms of taurine/α-ketoglutarate dioxygenase, a non-heme iron hydroxylase. evidence for bicarbonate binding Proc. Natl. Acad. Sci. USA. 100:2003;3790-3795
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3790-3795
    • Ryle, M.J.1    Koehntop, K.D.2    Liu, A.3    Que Jr., L.4    Hausinger, R.P.5
  • 44
    • 0346100345 scopus 로고    scopus 로고
    • Free redical-mediated oxidation of free amino acids and amino acid residues in proteins
    • Stadtman E.R., Levire R.L. Free redical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids. 25:2003;207-218
    • (2003) Amino Acids , vol.25 , pp. 207-218
    • Stadtman, E.R.1    Levire, R.L.2
  • 45
    • 0001334552 scopus 로고
    • Stereospecific conversion of 1-aminocyclopropanecarboxylic acid to ethylene by plant tissue
    • Hoffman N.E., Yang S.F., Ichihara A., Sakamura S. Stereospecific conversion of 1-aminocyclopropanecarboxylic acid to ethylene by plant tissue. Plant Physiol. 70:1982;195-199
    • (1982) Plant Physiol. , vol.70 , pp. 195-199
    • Hoffman, N.E.1    Yang, S.F.2    Ichihara, A.3    Sakamura, S.4
  • 46
    • 0001265024 scopus 로고
    • Ethylene biosynthesis. 6. Synthesis and evaluation of methylaminocyclopropanecarboxylic acid
    • Pirrung M.C., Mcgeehan G.M. Ethylene biosynthesis. 6. Synthesis and evaluation of methylaminocyclopropanecarboxylic acid. J. Org. Chem. 51:1986;2103-2106
    • (1986) J. Org. Chem. , vol.51 , pp. 2103-2106
    • Pirrung, M.C.1    McGeehan, G.M.2
  • 47
    • 37049112292 scopus 로고
    • On the biosynthesis of ethylene. Determination of the stereochemical course using modified substrates
    • Baldwin J.E., Adlington R.M., Lajoie G.A., Rawlings B.J. On the biosynthesis of ethylene. Determination of the stereochemical course using modified substrates. J. Chem. Soc. Chem. Commun. 1496-1498:1985
    • (1985) J. Chem. Soc. Chem. Commun. , vol.1496-1498
    • Baldwin, J.E.1    Adlington, R.M.2    Lajoie, G.A.3    Rawlings, B.J.4
  • 49
    • 0037388770 scopus 로고    scopus 로고
    • Crystal structure of the ascorbate peroxidase-ascorbate complex
    • Sharp K.H., Mewies M., Moody P.C.E., Raven M.L. Crystal structure of the ascorbate peroxidase-ascorbate complex. Nat. Struct. Biol. 10:2003;303-307
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 303-307
    • Sharp, K.H.1    Mewies, M.2    Moody, P.C.E.3    Raven, M.L.4
  • 51
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;11-119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 11-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4


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