메뉴 건너뛰기




Volumn 277, Issue 12, 2010, Pages 2628-2640

New insights into structure-function relationships of oxalyl CoA decarboxylase from escherichia coli

Author keywords

ADP activation; Crystal structure; Oxalate degradation; Thiamine diphosphate; X ray scattering

Indexed keywords

ACETYL COENZYME A; ADENOSINE DIPHOSPHATE; CARBOXYLYASE; COCARBOXYLASE; COENZYME A; OXALIC ACID; OXALYL COENZYME A DECARBOXYLASE; UNCLASSIFIED DRUG;

EID: 77953207313     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07673.x     Document Type: Article
Times cited : (20)

References (35)
  • 1
    • 2342637453 scopus 로고
    • Oxalate content of foods and nutrition
    • In. Hodgkinson, A. ed. pp. Academic Press
    • Hodgkinson A (1977) Oxalate content of foods and nutrition. In Oxalic Acid in Biology and Medicine (Hodgkinson A, ed pp. 193 212. Academic Press
    • (1977) Oxalic Acid in Biology and Medicine , pp. 193-212
    • Hodgkinson, A.1
  • 2
    • 0024672742 scopus 로고
    • Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes
    • Baetz AL Allison MJ (1989) Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes. J Bacteriol 171, 2605 2608.
    • (1989) J Bacteriol , vol.171 , pp. 2605-2608
    • Baetz, A.L.1    Allison, M.J.2
  • 3
    • 29244469942 scopus 로고    scopus 로고
    • Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate
    • Berthold CL, Moussatche P, Richards NG Lindqvist Y (2005) Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate. J Biol Chem 280, 41645 41654.
    • (2005) J Biol Chem , vol.280 , pp. 41645-41654
    • Berthold, C.L.1    Moussatche, P.2    Richards, N.G.3    Lindqvist, Y.4
  • 4
    • 34447260286 scopus 로고    scopus 로고
    • Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases
    • Berthold CL, Toyota CG, Moussatche P, Wood MD, Leeper F, Richards NG Lindqvist Y (2007) Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases. Structure 15, 853 861.
    • (2007) Structure , vol.15 , pp. 853-861
    • Berthold, C.L.1    Toyota, C.G.2    Moussatche, P.3    Wood, M.D.4    Leeper, F.5    Richards, N.G.6    Lindqvist, Y.7
  • 5
    • 0027918180 scopus 로고
    • A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase
    • Muller YA, Lindqvist Y, Furey W, Schulz GE, Jordan F Schneider G (1993) A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase. Structure 1, 95 103.
    • (1993) Structure , vol.1 , pp. 95-103
    • Muller, Y.A.1    Lindqvist, Y.2    Furey, W.3    Schulz, G.E.4    Jordan, F.5    Schneider, G.6
  • 6
    • 0042707939 scopus 로고    scopus 로고
    • Oxalotrophic bacteria
    • Sahin N (2003) Oxalotrophic bacteria. Res Microbiol 154, 399 407.
    • (2003) Res Microbiol , vol.154 , pp. 399-407
    • Sahin, N.1
  • 7
    • 0011233849 scopus 로고
    • Carbon assimilation by Pseudomonas oxalaticus (Ox1). 7. Decarboxylation of oxalyl-coenzyme A to formyl-coenzyme A
    • Quayle JR (1963) Carbon assimilation by Pseudomonas oxalaticus (Ox1). 7. Decarboxylation of oxalyl-coenzyme A to formyl-coenzyme A. Biochem J 89, 492 503.
    • (1963) Biochem J , vol.89 , pp. 492-503
    • Quayle, J.R.1
  • 8
    • 0141706603 scopus 로고    scopus 로고
    • The crystal structure of the Escherichia coli yfdW gene product reveals a new fold of two interlaced rings identifying a wide family of CoA transferases
    • Gruez A, Roig-Zamboni V, Valencia C, Campanacci V Cambillau C (2003) The crystal structure of the Escherichia coli yfdW gene product reveals a new fold of two interlaced rings identifying a wide family of CoA transferases. J Biol Chem 278, 34582 34586.
    • (2003) J Biol Chem , vol.278 , pp. 34582-34586
    • Gruez, A.1    Roig-Zamboni, V.2    Valencia, C.3    Campanacci, V.4    Cambillau, C.5
  • 9
    • 41549156949 scopus 로고    scopus 로고
    • Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase
    • Toyota CG, Berthold CL, Gruez A, Jónsson S, Lindqvist Y, Cambillau C Richards NGJ (2008) Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase. J Bacteriol 190, 2556 2564.
    • (2008) J Bacteriol , vol.190 , pp. 2556-2564
    • Toyota, C.G.1    Berthold, C.L.2    Gruez, A.3    Jónsson, S.4    Lindqvist, Y.5    Cambillau, C.6    Richards, N.G.J.7
  • 10
    • 0024432768 scopus 로고
    • A common structural motif in thiamin pyrophosphate-binding enzymes
    • Hawkins CF, Borges A Perham RN (1989) A common structural motif in thiamin pyrophosphate-binding enzymes. FEBS Lett 255, 77 82.
    • (1989) FEBS Lett , vol.255 , pp. 77-82
    • Hawkins, C.F.1    Borges, A.2    Perham, R.N.3
  • 13
    • 34247131943 scopus 로고    scopus 로고
    • Protein-protein interactions in complex cosolvent solutions
    • Javid N, Vogtt K, Krywka C, Tolan M Winter R (2007) Protein-protein interactions in complex cosolvent solutions. Chemphyschem 8, 679 689.
    • (2007) Chemphyschem , vol.8 , pp. 679-689
    • Javid, N.1    Vogtt, K.2    Krywka, C.3    Tolan, M.4    Winter, R.5
  • 14
    • 35848931491 scopus 로고    scopus 로고
    • The influence of protein concentration on oligomer structure and catalytic function of two pyruvate decarboxylases
    • Kutter S, Spinka M, Koch MHJ König S (2007) The influence of protein concentration on oligomer structure and catalytic function of two pyruvate decarboxylases. Protein J 26, 585 591.
    • (2007) Protein J , vol.26 , pp. 585-591
    • Kutter, S.1    Spinka, M.2    Koch, M.H.J.3    König, S.4
  • 15
    • 0038025249 scopus 로고    scopus 로고
    • Studies on structure-function relationships of indolepyruvate decarboxylase from Enterobacter cloacae- A key enzyme of the indole acetic acid pathway
    • Schütz A, Golbik R, Tittmann K, Svergun DI, Koch MHJ, Hübner G König S (2003) Studies on structure-function relationships of indolepyruvate decarboxylase from Enterobacter cloacae- a key enzyme of the indole acetic acid pathway. Eur J Biochem 270, 2322 2331.
    • (2003) Eur J Biochem , vol.270 , pp. 2322-2331
    • Schütz, A.1    Golbik, R.2    Tittmann, K.3    Svergun, D.I.4    Koch, M.H.J.5    Hübner, G.6    König, S.7
  • 16
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D, Barberato C Koch MHJ (1995) CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr 28, 768 773.
    • (1995) J Appl Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 17
    • 4143147626 scopus 로고    scopus 로고
    • Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes
    • Jonsson S, Ricagno S, Lindqvist Y Richards NG (2004) Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes. J Biol Chem 279, 36003 36012.
    • (2004) J Biol Chem , vol.279 , pp. 36003-36012
    • Jonsson, S.1    Ricagno, S.2    Lindqvist, Y.3    Richards, N.G.4
  • 18
    • 34250707247 scopus 로고    scopus 로고
    • Determination of oxalyl-coenzyme A decarboxylase activity in Oxalobacter formigenes and Lactobacillus acidophilus by capillary electrophoresis
    • Bendazzoli C, Turroni S, Gotti R, Olmo S, Brigidi P Cavrini V (2007) Determination of oxalyl-coenzyme A decarboxylase activity in Oxalobacter formigenes and Lactobacillus acidophilus by capillary electrophoresis. J Chromatogr B Analyt Technol Biomed Life Sci 854, 350 356.
    • (2007) J Chromatogr B Analyt Technol Biomed Life Sci , vol.854 , pp. 350-356
    • Bendazzoli, C.1    Turroni, S.2    Gotti, R.3    Olmo, S.4    Brigidi, P.5    Cavrini, V.6
  • 19
    • 84956768859 scopus 로고
    • Über methylthionaphtenchinon
    • Stolle R (1914) Über Methylthionaphtenchinon. Ber Dtsch Chem Ges 47, 1130 1132.
    • (1914) Ber Dtsch Chem Ges , vol.47 , pp. 1130-1132
    • Stolle, R.1
  • 20
    • 0000114734 scopus 로고
    • Formate metabolism: I. Formyl coenzyme A, an intermediate in the formate-dependent decomposition of acetyl-phosphate in Clostridium kluyveri
    • Sly W Stadtman ER (1963) Formate metabolism: I. Formyl coenzyme A, an intermediate in the formate-dependent decomposition of acetyl-phosphate in Clostridium kluyveri. J Biol Chem 238, 2632 2638.
    • (1963) J Biol Chem , vol.238 , pp. 2632-2638
    • Sly, W.1    Stadtman, E.R.2
  • 22
    • 0014959829 scopus 로고
    • Mechanism of thiamine-catalyzed reactions. A kinetic analysis of the decarboxylation of pyruvate by 3,4-dimethylthiazolium ion in water and ethanol
    • Crosby J Lienhard GE (1970) Mechanism of thiamine-catalyzed reactions. A kinetic analysis of the decarboxylation of pyruvate by 3,4-dimethylthiazolium ion in water and ethanol. J Am Chem Soc 92, 5707 5716.
    • (1970) J Am Chem Soc , vol.92 , pp. 5707-5716
    • Crosby, J.1    Lienhard, G.E.2
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0002394619 scopus 로고
    • A specific micromethod for the determination of acyl phosphates
    • Lipmann F Tuttle C (1945) A specific micromethod for the determination of acyl phosphates. J Biol Chem 159, 21 28.
    • (1945) J Biol Chem , vol.159 , pp. 21-28
    • Lipmann, F.1    Tuttle, C.2
  • 26
    • 34248359067 scopus 로고    scopus 로고
    • ATSAS2.1 - Towards automated and web-supported small-angle scattering data analysis
    • Petoukhov MV, Konarev PV, Kikhney AG Svergun DI (2007) ATSAS2.1 - towards automated and web-supported small-angle scattering data analysis. J Appl Crystallogr 40, 223 228.
    • (2007) J Appl Crystallogr , vol.40 , pp. 223-228
    • Petoukhov, M.V.1    Konarev, P.V.2    Kikhney, A.G.3    Svergun, D.I.4
  • 28
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 25, 495 503.
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 29
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76, 2879 2886.
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.1
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing X-ray diffraction data collected in oscillation mode
    • Otwinowski Z Minor W (1997) Processing X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307 326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760 763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 33
    • 0000952473 scopus 로고
    • Treatment of negative intensity observations
    • French S Wilson K (1978) Treatment of negative intensity observations. Acta Crystallogr A 34, 517 525.
    • (1978) Acta Crystallogr A , vol.34 , pp. 517-525
    • French, S.1    Wilson, K.2
  • 34
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31, 3381 3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 35


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.