메뉴 건너뛰기




Volumn 183, Issue 1, 2012, Pages 70-77

Engagement of the S1, S1′ and S2′ subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum

Author keywords

Enzyme kinetics; Hemoglobin; Malaria; Peptidase; Vacuole

Indexed keywords

AMINOPEPTIDASE; HEMOGLOBIN;

EID: 84858702136     PISSN: 01666851     EISSN: 18729428     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2012.02.003     Document Type: Article
Times cited : (17)

References (37)
  • 2
    • 0034744491 scopus 로고    scopus 로고
    • 4) hydrolase as potential anti-inflammatory agents
    • DOI 10.2174/1381612013398248
    • T.D. Penning Inhibitors of leukotriene A4 (LTA4) hydrolase as potential anti-inflammatory agents Curr Pharm Des 7 2001 163 179 (Pubitemid 32409714)
    • (2001) Current Pharmaceutical Design , vol.7 , Issue.3 , pp. 163-179
    • Penning, T.D.1
  • 3
    • 33644875741 scopus 로고    scopus 로고
    • Aminopeptidase-N/CD13 (EC 3.4.11.2) inhibitors: Chemistry, biological evaluations, and therapeutic prospects
    • DOI 10.1002/med.20044
    • B. Bauvois, and DauzonneF D. Aminopeptidase-N/CD13 (EC 3.4.11.2) inhibitors: chemistry, biological evaluations, and therapeutic prospects Med Res Rev 26 2006 88 130 (Pubitemid 43986471)
    • (2006) Medicinal Research Reviews , vol.26 , Issue.1 , pp. 88-130
    • Bauvois, B.1    Dauzonne, D.2
  • 4
    • 0032879805 scopus 로고    scopus 로고
    • Estimating mortality, morbidity and disability due to malaria among Africa's non-pregnant population
    • R.W. Snow, M. Craig, U. Deichmann, and K. Marsh Estimating mortality, morbidity and disability due to malaria among Africa's non-pregnant population Bull World Health Organ 77 1999 624 640 (Pubitemid 29446615)
    • (1999) Bulletin of the World Health Organization , vol.77 , Issue.8 , pp. 624-640
    • Snow, R.W.1    Craig, M.2    Deichmann, U.3    Marsh, K.4
  • 5
    • 84857034908 scopus 로고    scopus 로고
    • Soft X-ray microscopy analysis of cell volume and hemoglobin content in erythrocytes infected with asexual and sexual stages of Plasmodium falciparum
    • 10.1016/j.jsb.2011.09.003
    • E. Hanssen, C. Knoechel, M. Dearnley, M.W. Dixon, M. Le Gros, and C. Larabell Soft X-ray microscopy analysis of cell volume and hemoglobin content in erythrocytes infected with asexual and sexual stages of Plasmodium falciparum J Struct Biol 2011 10.1016/j.jsb.2011.09.003
    • (2011) J Struct Biol
    • Hanssen, E.1    Knoechel, C.2    Dearnley, M.3    Dixon, M.W.4    Le Gros, M.5    Larabell, C.6
  • 6
    • 37249008065 scopus 로고    scopus 로고
    • Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum
    • DOI 10.1074/jbc.M703643200
    • S. Dalal, and M. Klemba Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum J Biol Chem 282 2007 35978 35987 (Pubitemid 350277126)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35978-35987
    • Dalal, S.1    Klemba, M.2
  • 8
    • 5644247394 scopus 로고    scopus 로고
    • A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation
    • DOI 10.1074/jbc.M408123200
    • M. Klemba, I. Gluzman, and D.E. Goldberg A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation J Biol Chem 279 2004 43000 43007 (Pubitemid 39372193)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 43000-43007
    • Klemba, M.1    Gluzman, I.2    Goldberg, D.E.3
  • 9
    • 12744262976 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites
    • P.J. Rosenthal Cysteine proteases of malaria parasites Int J Parasitol 34 2004 1489 1499
    • (2004) Int J Parasitol , vol.34 , pp. 1489-1499
    • Rosenthal, P.J.1
  • 10
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • I. Schechter, and A. Berger On the size of the active site in proteases. I. Papain Biochem Biophys Res Commun 27 1967 157 162
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 11
    • 69949153735 scopus 로고    scopus 로고
    • Evidence for catalytic roles for Plasmodium falciparum aminopeptidase P in the food vacuole and cytosol
    • D. Ragheb, K. Bompiani, S. Dalal, and M. Klemba Evidence for catalytic roles for Plasmodium falciparum aminopeptidase P in the food vacuole and cytosol J Biol Chem 284 2009 24806 24815
    • (2009) J Biol Chem , vol.284 , pp. 24806-24815
    • Ragheb, D.1    Bompiani, K.2    Dalal, S.3    Klemba, M.4
  • 12
    • 0032583101 scopus 로고    scopus 로고
    • A Plasmodium falciparum aminopeptidase gene belonging to the M1 family of zinc-metallopeptidases is expressed in erythrocytic stages
    • DOI 10.1016/S0166-6851(98)00143-1, PII S0166685198001431
    • I. Florent, Z. Derhy, M. Allary, M. Monsigny, R. Mayer, and J. Schrevel A Plasmodium falciparum aminopeptidase gene belonging to the M1 family of zinc-metallopeptidases is expressed in erythrocytic stages Mol Biochem Parasitol 97 1998 149 160 (Pubitemid 28558709)
    • (1998) Molecular and Biochemical Parasitology , vol.97 , Issue.1-2 , pp. 149-160
    • Florent, I.1    Derhy, Z.2    Allary, M.3    Monsigny, M.4    Mayer, R.5    Schrevel, J.6
  • 13
    • 77954037366 scopus 로고    scopus 로고
    • Plasmodium falciparum PfA-M1 aminopeptidase is trafficked via the parasitophorous vacuole and marginally delivered to the food vacuole
    • O. Azimzadeh, C. Sow, M. Geze, J. Nyalwidhe, and I. Florent Plasmodium falciparum PfA-M1 aminopeptidase is trafficked via the parasitophorous vacuole and marginally delivered to the food vacuole Malar J 9 2010 189 205
    • (2010) Malar J , vol.9 , pp. 189-205
    • Azimzadeh, O.1    Sow, C.2    Geze, M.3    Nyalwidhe, J.4    Florent, I.5
  • 14
    • 79960991925 scopus 로고    scopus 로고
    • Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism
    • D. Ragheb, S. Dalal, K.M. Bompiani, W.K. Ray, and M. Klemba Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism J Biol Chem 286 2011 27255 27265
    • (2011) J Biol Chem , vol.286 , pp. 27255-27265
    • Ragheb, D.1    Dalal, S.2    Bompiani, K.M.3    Ray, W.K.4    Klemba, M.5
  • 15
    • 80052154599 scopus 로고    scopus 로고
    • Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases
    • M.B. Harbut, G. Velmourougane, S. Dalal, G. Reiss, J.C. Whisstock, and O. Onder Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases Proc Natl Acad Sci USA 108 2011 E526 E534
    • (2011) Proc Natl Acad Sci USA , vol.108
    • Harbut, M.B.1    Velmourougane, G.2    Dalal, S.3    Reiss, G.4    Whisstock, J.C.5    Onder, O.6
  • 16
    • 33947632299 scopus 로고    scopus 로고
    • Novel selective inhibitors of the zinc plasmodial aminopeptidase PfA-M1 as potential antimalarial agents
    • DOI 10.1021/jm061169b
    • M. Flipo, T. Beghyn, V. Leroux, I. Florent, B.P. Deprez, and R.F. Deprez-Poulain Novel selective inhibitors of the zinc plasmodial aminopeptidase PfA-M1 as potential antimalarial agents J Med Chem 50 2007 1322 1334 (Pubitemid 46496331)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.6 , pp. 1322-1334
    • Flipo, M.1    Beghyn, T.2    Leroux, V.3    Florent, I.4    Deprez, B.P.5    Deprez-Poulain, R.F.6
  • 17
    • 0038825686 scopus 로고    scopus 로고
    • Design, synthesis and antimalarial activity of novel, quinoline-based, zinc metallo-aminopeptidase inhibitors
    • DOI 10.1016/S0960-894X(03)00550-X
    • M. Flipo, I. Florent, P. Grellier, C. Sergheraert, and R. Deprez-Poulain Design, synthesis and antimalarial activity of novel, quinoline-based, zinc metallo-aminopeptidase inhibitors Bioorg Med Chem Lett 13 2003 2659 2662 (Pubitemid 36851544)
    • (2003) Bioorganic and Medicinal Chemistry Letters , vol.13 , Issue.16 , pp. 2659-2662
    • Flipo, M.1    Florent, I.2    Grellier, P.3    Sergheraert, C.4    Deprez-Poulain, R.5
  • 18
    • 7444271910 scopus 로고    scopus 로고
    • A high-performance liquid chromatography method for determining transition metal content in proteins
    • DOI 10.1016/j.ab.2004.08.013, PII S0003269704006633
    • A. Atanassova, R. Lam, and D.B. Zamble A high-performance liquid chromatography method for determining transition metal content in proteins Anal Biochem 335 2004 103 111 (Pubitemid 39446236)
    • (2004) Analytical Biochemistry , vol.335 , Issue.1 , pp. 103-111
    • Atanassova, A.1    Lam, R.2    Zamble, D.B.3
  • 21
    • 0000484499 scopus 로고
    • Hydrophobic parameters of pi amino-acid side chains from the partitioning of N-acetyl-amino acid amides
    • J-L. Fauchre, and V. Pliška Hydrophobic parameters of pi amino-acid side chains from the partitioning of N-acetyl-amino acid amides Eur J Med Chem Chim Ther 18 1983 369 375
    • (1983) Eur J Med Chem Chim Ther , vol.18 , pp. 369-375
    • Fauchre, J.-L.1    Pliška, V.2
  • 23
    • 35748956775 scopus 로고    scopus 로고
    • Evaluation of pH during cytostomal endocytosis and vacuolar catabolism of haemoglobin in Plasmodium falciparum
    • DOI 10.1042/BJ20070934
    • N. Klonis, O. Tan, K. Jackson, D. Goldberg, M. Klemba, and L. Tilley Evaluation of pH during cytostomal endocytosis and vacuolar catabolism of hemoglobin in Plasmodium falciparum Biochem J 407 2007 343 354 (Pubitemid 350058468)
    • (2007) Biochemical Journal , vol.407 , Issue.3 , pp. 343-354
    • Klonis, N.1    Tan, O.2    Jackson, K.3    Goldberg, D.4    Klemba, M.5    Tilley, L.6
  • 24
    • 0022347074 scopus 로고
    • Antimalarials increase vesicle pH in Plasmodium falciparum
    • DOI 10.1083/jcb.101.6.2302
    • D.J. Krogstad, P.H. Schlesinger, and I.Y. Gluzman Antimalarials increase vesicle pH in Plasmodium falciparum J Cell Biol 101 1985 2302 2309 (Pubitemid 16169961)
    • (1985) Journal of Cell Biology , vol.101 , Issue.6 , pp. 2302-2309
    • Krogstad, D.J.1    Schlesinger, P.H.2    Gluzman, I.Y.3
  • 25
    • 33947125517 scopus 로고    scopus 로고
    • Quantitative pH measurements in Plasmodium falciparum-infected erythrocytes using pHluorin
    • DOI 10.1111/j.1462-5822.2006.00847.x
    • Y. Kuhn, P. Rohrbach, and M. Lanzer Quantitative pH measurements in Plasmodium falciparum-infected erythrocytes using pHluorin Cell Microbiol 9 2007 1004 1013 (Pubitemid 46394910)
    • (2007) Cellular Microbiology , vol.9 , Issue.4 , pp. 1004-1013
    • Kuhn, Y.1    Rohrbach, P.2    Lanzer, M.3
  • 26
    • 0027305020 scopus 로고
    • Synthesis of a fluorescent derivatizing reagent, 6-aminoquinolyl-N- hydroxysuccinimidyl carbamate, and its application for the analysis of hydrolysate amino acids via high-performance liquid chromatography
    • DOI 10.1006/abio.1993.1270
    • S.A. Cohen, and D.P. Michaud Synthesis of a fluorescent derivatizing reagent, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate, and its application for the analysis of hydrolysate amino acids via high-performance liquid chromatography Anal Biochem 211 1993 279 287 (Pubitemid 23207730)
    • (1993) Analytical Biochemistry , vol.211 , Issue.2 , pp. 279-287
    • Cohen, S.A.1    Michaud, D.P.2
  • 27
    • 0028835221 scopus 로고
    • A study of the substrate specificity of aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2
    • G.W. Niven, S.A. Holder, and P. Stroman A study of the substrate specificity of aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2 Appl Microbiol Biotechnol 44 1995 100 105
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 100-105
    • Niven, G.W.1    Holder, S.A.2    Stroman, P.3
  • 28
    • 0028179367 scopus 로고
    • The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity
    • L. Orning, J.K. Gierse, and F.A. Fitzpatrick The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity J Biol Chem 269 1994 11269 11273
    • (1994) J Biol Chem , vol.269 , pp. 11269-11273
    • Orning, L.1    Gierse, J.K.2    Fitzpatrick, F.A.3
  • 29
    • 77449129432 scopus 로고    scopus 로고
    • Aminopeptidase fingerprints, an integrated approach for identification of good substrates and optimal inhibitors
    • M. Drag, M. Bogyo, J.A. Ellman, and G.S. Salvesen Aminopeptidase fingerprints, an integrated approach for identification of good substrates and optimal inhibitors J Biol Chem 285 2010 3310 3318
    • (2010) J Biol Chem , vol.285 , pp. 3310-3318
    • Drag, M.1    Bogyo, M.2    Ellman, J.A.3    Salvesen, G.S.4
  • 30
    • 0030679556 scopus 로고    scopus 로고
    • Alanyl aminopeptidase from human seminal plasma: Purification characterization, and immunohistochemical localization in the male genital tract
    • K. Huang, S. Takahara, T. Kinouchi, M. Takeyama, T. Ishida, and H. Ueyama Alanyl aminopeptidase from human seminal plasma: purification, characterization, and immunohistochemical localization in the male genital tract J Biochem 122 1997 779 787 (Pubitemid 27474948)
    • (1997) Journal of Biochemistry , vol.122 , Issue.4 , pp. 779-787
    • Huang, K.1    Takahara, S.2    Kinouchi, T.3    Takeyama, M.4    Ishida, T.5    Ueyama, H.6    Nishi, K.7    Ohkubo, I.8
  • 31
    • 0025181826 scopus 로고
    • Studies on the subsite specificity of the rat brain puromycin-sensitive aminopeptidase
    • DOI 10.1016/0003-9861(90)90724-D
    • G.D. Johnson, and L.B. Hersh Studies on the subsite specificity of the rat brain puromycin-sensitive aminopeptidase Arch Biochem Biophys 276 1990 305 309 (Pubitemid 20081957)
    • (1990) Archives of Biochemistry and Biophysics , vol.276 , Issue.2 , pp. 305-309
    • Johnson, G.D.1    Hersh, L.B.2
  • 32
    • 0017636755 scopus 로고
    • Aminopeptidase N from Escherichia coli: Ionizable active-center groups and substrate specificity
    • D. Chappelet-Tordo, C. Lazdunski, M. Murgier, and A. Lazdunski Aminopeptidase N from Escherichia coli: ionizable active-center groups and substrate specificity Eur J Biochem 81 1977 293 305
    • (1977) Eur J Biochem , vol.81 , pp. 293-305
    • Chappelet-Tordo, D.1    Lazdunski, C.2    Murgier, M.3    Lazdunski, A.4
  • 34
    • 43249098656 scopus 로고    scopus 로고
    • Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
    • DOI 10.1021/bi7022333
    • A. Addlagatta, L. Gay, and B.W. Matthews Structural basis for the unusual specificity of Escherichia coli aminopeptidase N Biochemistry 47 2008 5303 5311 (Pubitemid 351656974)
    • (2008) Biochemistry , vol.47 , Issue.19 , pp. 5303-5311
    • Addlagatta, A.1    Gay, L.2    Matthews, B.W.3
  • 35
    • 68349147918 scopus 로고    scopus 로고
    • Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250
    • M.C. Fournie-Zaluski, H. Poras, B.P. Roques, Y. Nakajima, K. Ito, and T. Yoshimoto Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250 Acta Crystallogr D 65 2009 814 822
    • (2009) Acta Crystallogr D , vol.65 , pp. 814-822
    • Fournie-Zaluski, M.C.1    Poras, H.2    Roques, B.P.3    Nakajima, Y.4    Ito, K.5    Yoshimoto, T.6
  • 36
    • 33845954688 scopus 로고    scopus 로고
    • Crystal structure of aminopeptidase N (Proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition
    • DOI 10.1074/jbc.M605203200
    • K. Ito, Y. Nakajima, Y. Onohara, M. Takeo, K. Nakashima, and F. Matsubara Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition J Biol Chem 281 2006 33664 33676 (Pubitemid 46036745)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.44 , pp. 33664-33676
    • Ito, K.1    Nakajima, Y.2    Onohara, Y.3    Takeo, M.4    Nakashima, K.5    Matsubara, F.6    Ito, T.7    Yoshimoto, T.8
  • 37
    • 51849151991 scopus 로고    scopus 로고
    • Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: Implications for M1 aminopeptidases and inhibitor design
    • F. Tholander, A. Muroya, B.P. Roques, M.C. Fournie-Zaluski, M.M. Thunnissen, and J.Z. Haeggstrom Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design Chem Biol 15 2008 920 929
    • (2008) Chem Biol , vol.15 , pp. 920-929
    • Tholander, F.1    Muroya, A.2    Roques, B.P.3    Fournie-Zaluski, M.C.4    Thunnissen, M.M.5    Haeggstrom, J.Z.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.