메뉴 건너뛰기




Volumn 30, Issue 1, 2012, Pages 62-73

Dissecting structural basis of the unique substrate selectivity of human enteropeptidase catalytic subunit

Author keywords

Active site; Enteropeptidase; Enzymatic catalysis; Molecular modeling; Substrate selectivity

Indexed keywords

ARGININE; ENTEROPEPTIDASE; GLUTAMINE; LYSINE; N BENZOYLARGININE 2 NAPHTHYLAMIDE; ASPARTIC ACID; PEPTIDE;

EID: 84863870147     PISSN: 07391102     EISSN: None     Source Type: Journal    
DOI: 10.1080/07391102.2012.674249     Document Type: Article
Times cited : (3)

References (43)
  • 3
    • 0037465824 scopus 로고    scopus 로고
    • Mechanistic origins of the substrate selectivity of serine proteases
    • DOI 10.1021/bi020668l
    • Case, A., & Stein, R.L. (2003). Mechanistic origins of the substrate selectivity of serine proteases. Biochemistry, 42, 3335-3348. (Pubitemid 36348643)
    • (2003) Biochemistry , vol.42 , Issue.11 , pp. 3335-3348
    • Case, A.1    Stein, R.L.2
  • 4
    • 33846823909 scopus 로고
    • Particle mesh Ewald - An N.Log(N) method for ewald sums in large systems
    • Darden, T., York, D., & Pedersen, L. (1993). Particle mesh Ewald - an N.Log(N) method for ewald sums in large systems. Journal of Chemical Physics, 98, 10089-10092.
    • (1993) Journal of Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 5
    • 67650361071 scopus 로고    scopus 로고
    • Serine proteases
    • Di Cera, E. (2009). Serine proteases. IUBMB Life, 61, 510-515.
    • (2009) IUBMB Life , vol.61 , pp. 510-515
    • Di Cera, E.1
  • 6
    • 0015378776 scopus 로고
    • The graphical determination of Km and Ki
    • Dixon, M. (1972). The graphical determination of Km and Ki. Biochemical Journal, 129, 197-202.
    • (1972) Biochemical Journal , vol.129 , pp. 197-202
    • Dixon, M.1
  • 7
    • 4344703330 scopus 로고    scopus 로고
    • Molecular modelling of the nucleotide-binding domain of Wilson's disease protein: Location of the ATP-binding site, domain dynamics and potential effects of the major disease mutations
    • DOI 10.1042/BJ20040326
    • Efremov, R.G., Kosinsky, Y.A., Nolde, D.E., Tsivkovskii, R., Arseniev, A.S., & Lutsenko, S. (2004). Molecular modelling of the nucleotide-binding domain of Wilson' disease protein: Location of the ATP-binding site, domain dynamics, and potential effects of the major disease mutations. Biochemical Journal, 382, 293-305. (Pubitemid 39141593)
    • (2004) Biochemical Journal , vol.382 , Issue.1 , pp. 293-305
    • Efremov, R.G.1    Kosinsky, Y.A.2    Nolde, D.E.3    Tsivkovskii, R.4    Arseniev, A.S.5    Lutsenko, S.6
  • 9
    • 0141762591 scopus 로고    scopus 로고
    • Expression, purification, and characterization of human enteropeptidase catalytic subunit in Escherichia coli
    • DOI 10.1016/S1046-5928(03)00159-1
    • Gasparian, M.E., Ostapchenko, V.G., Schulga, A.A., Dolgikh, D.A., & Kirpichnikov, M.P. (2003). Expression, purification, and characterization of human enteropeptidase catalytic subunit in escherichia coli. Protein Expression and Purification, 31, 133-139. (Pubitemid 37207651)
    • (2003) Protein Expression and Purification , vol.31 , Issue.1 , pp. 133-139
    • Gasparian, M.E.1    Ostapchenko, V.G.2    Schulga, A.A.3    Dolgikh, D.A.4    Kirpichnikov, M.P.5
  • 10
    • 34548125801 scopus 로고    scopus 로고
    • Overexpression and refolding of thioredoxin/TRAIL fusion from inclusion bodies and further purification of TRAIL after cleavage by enteropeptidase
    • DOI 10.1007/s10529-007-9446-y
    • Gasparian, M.E., Ostapchenko, V.G., Yagolovich, A.V., Tsygannik, I.N., Chernyak, B.V., Dolgikh, D.A., & Kirpichnikov, M.P. (2007). Overexpression and refolding of thioredoxin/TRAIL fusion from inclusion bodies and further purification of TRAIL after cleavage by enteropeptidase. Biotechnology Letters, 29, 1567-1573. (Pubitemid 47301377)
    • (2007) Biotechnology Letters , vol.29 , Issue.10 , pp. 1567-1573
    • Gasparian, M.E.1    Ostapchenko, V.G.2    Yagolovich, A.V.3    Tsygannik, I.N.4    Chernyak, B.V.5    Dolgikh, D.A.6    Kirpichnikov, M.P.7
  • 11
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom, L. (2002). Serine protease mechanism and specificity. Chemical Reviews, 102, 4501-4524.
    • (2002) Chemical Reviews , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 13
    • 0344925815 scopus 로고    scopus 로고
    • Expression of enteropeptidase in differentiated enterocytes, goblet cells, and the tumor cells in human duodenum
    • Imamura, T., & Kitamoto, Y. (2003). Expression of enteropeptidase in differentiated enterocytes, goblet cells, and the tumor cells in human duodenum. American Journal of Physiology-Gastrointestinal and Liver Physiology, 285, G1235-G1241. (Pubitemid 37449011)
    • (2003) American Journal of Physiology - Gastrointestinal and Liver Physiology , vol.285 , Issue.6
    • Imamura, T.1    Kitamoto, Y.2
  • 14
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure - Pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., & Sander, C. (1983). Dictionary of protein secondary structure - pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 17
    • 0342445397 scopus 로고    scopus 로고
    • What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?
    • Laskowski, M., & Qasim, M.A. (2000). What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes? Biochimica et Biophysica Acta, 1477, 324-337.
    • (2000) Biochimica et Biophysica Acta , vol.1477 , pp. 324-337
    • Laskowski, M.1    Qasim, M.A.2
  • 19
    • 84863862241 scopus 로고    scopus 로고
    • Enterokinase cleavage sequences
    • USA patent 6,906,176 B2
    • Ley, A.C., Luneau, C.J., & Lander, R.C. (2005). Enterokinase cleavage sequences. USA patent 6,906,176 B2.
    • (2005)
    • Ley, A.C.1    Luneau, C.J.2    Lander, R.C.3
  • 20
    • 0021750643 scopus 로고
    • The preparation and properties of the catalytic subunit of bovine enterokinase
    • Light, A., & Fonseca, P. (1984). The preparation and properties of the catalytic subunit of bovine enterokinase. Journal of Biological Chemistry, 259, 13195-13198. (Pubitemid 15223840)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.21 , pp. 13195-13198
    • Light, A.1    Fonseca, P.2
  • 21
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • DOI 10.1007/S008940100045
    • Lindahl, E., Hess, B., & van der Spoel, D. (2001). GROMACS 3.0: A package for molecular simulation and trajectory analysis. Journal of Molecular Modeling, 7, 306-317. (Pubitemid 36153547)
    • (2001) Journal of Molecular Modeling , vol.7 , Issue.8 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 22
    • 0344631102 scopus 로고    scopus 로고
    • Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide
    • DOI 10.1006/jmbi.1999.3089
    • Lu, D., Futterer, K., Korolev, S., Zheng, X., Tan, K., Waksman, G., & Sadler, J.E. (1999). Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide. Journal of Molecular Biology, 292, 361-373. (Pubitemid 29435772)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 361-373
    • Lu, D.1    Futterer, K.2    Korolev, S.3    Zheng, X.4    Tan, K.5    Waksman, G.6    Sadler, J.E.7
  • 23
    • 0031466897 scopus 로고    scopus 로고
    • Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain
    • DOI 10.1074/jbc.272.50.31293
    • Lu, D., Yuan, X., Zheng, X., & Sadler, J.E. (1997). Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain. Journal of Biological Chemistry, 272, 31293-31300. (Pubitemid 28013261)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.50 , pp. 31293-31300
    • Lu, D.1    Yuan, X.2    Zheng, X.3    Sadler, J.E.4
  • 27
    • 27844585652 scopus 로고    scopus 로고
    • Effect of calcium ions on enteropeptidase catalysis
    • DOI 10.1007/s10541-005-0235-8
    • Mikhailova, A.G., Likhareva, V.V., Prudchenko, I.A., &Rumsh, L.D. (2005). Effect of calcium ions on enteropeptidase catalysis. Biochemistry (Moscow), 70, 1129-1135. (Pubitemid 41641416)
    • (2005) Biochemistry (Moscow) , vol.70 , Issue.10 , pp. 1129-1135
    • Mikhailova, A.G.1    Likhareva, V.V.2    Prudchenko, I.A.3    Rumsh, L.D.4
  • 28
    • 0032933143 scopus 로고    scopus 로고
    • Autolysis of bovine enteropeptidase heavy chain: Evidence of fragment 118-465 involvement in trypsinogen activation
    • DOI 10.1016/S0014-5793(98)01656-1, PII S0014579398016561
    • Mikhailova, A.G., & Rumsh, L.D. (1999). Autolysis of bovine enteropeptidase heavy chain: Evidence of fragment 118-465 involvement in trypsinogen activation. FEBS Letters, 442, 226-230. (Pubitemid 29070838)
    • (1999) FEBS Letters , vol.442 , Issue.2-3 , pp. 226-230
    • Mikhailova, A.G.1    Rumsh, L.D.2
  • 29
    • 33847742147 scopus 로고    scopus 로고
    • The ways of realization of high specificity and efficiency of enteropeptidase
    • DOI 10.2174/092986607780090793
    • Mikhailova, A.G., Likhareva, V.V., Teich, N., & Rumsh, L.D. (2007). The ways of realization of high specificity and efficiency of enteropeptidase. Protein and Peptide Letters, 14, 227-232. (Pubitemid 46376852)
    • (2007) Protein and Peptide Letters , vol.14 , Issue.3 , pp. 227-232
    • Mikhailova, A.G.1    Likhareva, V.V.2    Teich, N.3    Rumsh, L.D.4
  • 31
    • 77949518419 scopus 로고    scopus 로고
    • Keratinocytes synthesize enteropeptidase and multiple forms of trypsinogen during terminal differentiation
    • Nakanishi, J., Yamamoto, M., Koyama, J., Sato, J., & Hibino, T. (2010). Keratinocytes synthesize enteropeptidase and multiple forms of trypsinogen during terminal differentiation. Journal of Investigative Dermatology, 130, 944-952.
    • (2010) Journal of Investigative Dermatology , vol.130 , pp. 944-952
    • Nakanishi, J.1    Yamamoto, M.2    Koyama, J.3    Sato, J.4    Hibino, T.5
  • 32
    • 23844507473 scopus 로고    scopus 로고
    • The tetra-aspartate motif in the activation peptide of human cationic trypsinogen is essential for autoactivation control but not for enteropeptidase recognition
    • DOI 10.1074/jbc.M505661200
    • Nemoda, Z., & Sahin-Toth, M. (2005). The tetra-aspartate motif in the activation peptide of human cationic trypsinogen is essential for autoactivation control but not for enteropeptidase recognition. Journal of Biological Chemistry, 280, 29645-29652. (Pubitemid 41177040)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.33 , pp. 29645-29652
    • Nemoda, Z.1    Sahin-Toth, M.2
  • 33
    • 42249109450 scopus 로고    scopus 로고
    • Serine peptidases: Classification, structure and function
    • Page, M.J., & Di Cera, E. (2008). Serine peptidases: Classification, structure and function. Cellular and Molecular Life Sciences, 65, 1220-1236.
    • (2008) Cellular and Molecular Life Sciences , vol.65 , pp. 1220-1236
    • Page, M.J.1    Di Cera, E.2
  • 34
    • 0028905227 scopus 로고
    • Structural origins of substrate discrimination in trypsin and chymotrypsin
    • Perona, J.J., Hedstrom, L., Rutter, W.J., & Fletterick, R.J. (1995). Structural origins of substrate discrimination in trypsin and chymotrypsin. Biochemistry, 34, 1489-1499.
    • (1995) Biochemistry , vol.34 , pp. 1489-1499
    • Perona, J.J.1    Hedstrom, L.2    Rutter, W.J.3    Fletterick, R.J.4
  • 35
    • 21444453418 scopus 로고    scopus 로고
    • Human mesotrypsin defies natural trypsin inhibitors: From passive resistance to active destruction
    • Sahin-Toth, M. (2005). Human mesotrypsin defies natural trypsin inhibitors: From passive resistance to active destruction. Protein and Peptide Letters, 12, 457-464.
    • (2005) Protein and Peptide Letters , vol.12 , pp. 457-464
    • Sahin-Toth, M.1
  • 36
    • 0015911769 scopus 로고
    • Dependence of the kinetic parameters for elastase-catalyzed amide hydrolysis on the length of peptide substrates
    • Thompson, R.C., & Blout, E.R. (1973). Dependence of the kinetic parameters for elastase-catalyzed amide hydrolysis on the length of peptide substrates. Biochemistry, 12, 57-65.
    • (1973) Biochemistry , vol.12 , pp. 57-65
    • Thompson, R.C.1    Blout, E.R.2
  • 37
    • 0023380976 scopus 로고
    • Thermodynamic cycle integration by computer simulation as a tool for obtaining free energy differences in molecular chemistry
    • van Gunsteren, W.F., & Berendsen, H.J. (1987). Thermodynamic cycle integration by computer simulation as a tool for obtaining free energy differences in molecular chemistry. Journal of Computer-Aided Molecular Design, 1, 171-176.
    • (1987) Journal of Computer-Aided Molecular Design , vol.1 , pp. 171-176
    • Van Gunsteren, W.F.1    Berendsen, H.J.2
  • 38
    • 0342655945 scopus 로고    scopus 로고
    • Expression of rat chymotrypsinogen in yeast: A study on the structural and functional significance of the chymotrypsinogen propeptide
    • DOI 10.1016/0014-5793(95)01483-7
    • Venekei, I., Graf, L., & Rutter, W.J. (1996). Expression of rat chymotrypsinogen in yeast: A study on the structural and functional significance of the chymotrypsinogen propeptide. FEBS Letters, 379, 139-142. (Pubitemid 26037841)
    • (1996) FEBS Letters , vol.379 , Issue.2 , pp. 139-142
    • Venekei, I.1    Graf, L.2    Rutter, W.J.3
  • 39
    • 38949121712 scopus 로고    scopus 로고
    • Intracellular colocalization of trypsin-2 and matrix metalloprotease-9: Possible proteolytic cascade of trypsin-2, MMP-9 and enterokinase in carcinoma
    • Vilen, S.T., Nyberg, P., Hukkanen, M., Sutinen, M., Ylipalosaari, M., Bjartell, A., ... Salo, T. (2008). Intracellular colocalization of trypsin-2 and matrix metalloprotease-9: Possible proteolytic cascade of trypsin-2, MMP-9 and enterokinase in carcinoma. Experimental Cell Research, 314, 914-926.
    • (2008) Experimental Cell Research , vol.314 , pp. 914-926
    • Vilen, S.T.1    Nyberg, P.2    Hukkanen, M.3    Sutinen, M.4    Ylipalosaari, M.5    Bjartell, A.6    Salo, T.7
  • 40
    • 38549103718 scopus 로고    scopus 로고
    • Trypsin and trypsin-like proteases in the brain: Proteolysis and cellular functions
    • DOI 10.1007/s00018-007-7288-3
    • Wang, Y., Luo, W., & Reiser, G. (2008). Trypsin and trypsin-like proteases in the brain: Proteolysis and cellular functions. Cellular and Molecular Life Sciences, 65, 237-252. (Pubitemid 351161480)
    • (2008) Cellular and Molecular Life Sciences , vol.65 , Issue.2 , pp. 237-252
    • Wang, Y.1    Luo, W.2    Reiser, G.3
  • 42
    • 0031936659 scopus 로고    scopus 로고
    • Structure of murine enterokinase (enteropeptidase) and expression in small intestine during development
    • Yuan, X., Zheng, X., Lu, D., Rubin, D.C., Pung, C.Y., & Sadler, J.E. (1998). Structure of murine enterokinase (enteropeptidase) and expression in small intestine during development. American Journal of Physiology, 274, G342-G349.
    • (1998) American Journal of Physiology , vol.274
    • Yuan, X.1    Zheng, X.2    Lu, D.3    Rubin, D.C.4    Pung, C.Y.5    Sadler, J.E.6
  • 43
    • 77953625365 scopus 로고    scopus 로고
    • Enteropeptidase, a type II transmembrane serine protease
    • Elite Edition
    • Zheng, X.L., Kitamoto, Y., & Sadler, J.E. (2009). Enteropeptidase, a type II transmembrane serine protease. Frontiers in Bioscience (Elite Edition), 1, 242-249.
    • (2009) Frontiers in Bioscience , vol.1 , pp. 242-249
    • Zheng, X.L.1    Kitamoto, Y.2    Sadler, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.