메뉴 건너뛰기




Volumn 45, Issue 38, 2006, Pages 11425-11431

Aspartic acid 405 contributes to the substrate specificity of aminopeptidase B

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DNA; ENZYME KINETICS; ORGANIC ACIDS; SUBSTRATES; SYNTHESIS (CHEMICAL);

EID: 33749005419     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0604577     Document Type: Article
Times cited : (19)

References (29)
  • 1
    • 0009807345 scopus 로고
    • A peptidase from rat tissues selectively hydrolysing N-terminal arginine and lysine residues
    • Hopsu, V. K., Kantonen, U.-M., and Glenner, G. G. (1964) A peptidase from rat tissues selectively hydrolysing N-terminal arginine and lysine residues, Life Sci. 3 1449-1453.
    • (1964) Life Sci. , vol.3 , pp. 1449-1453
    • Hopsu, V.K.1    Kantonen, U.-M.2    Glenner, G.G.3
  • 2
    • 0029803859 scopus 로고    scopus 로고
    • Molecular cloning and exression of rat liver aminopeptidase B
    • Fukasawa, K. M., Fukasawa, K., Kanai, M., Fujii, S., and Harada, M. (1996) Molecular cloning and exression of rat liver aminopeptidase B, J. Biol. Chem. 271, 30731-30735.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30731-30735
    • Fukasawa, K.M.1    Fukasawa, K.2    Kanai, M.3    Fujii, S.4    Harada, M.5
  • 3
    • 0024511780 scopus 로고
    • Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N
    • Watt, V. M., and Yip, C. C. (1989) Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N, J. Biol. Chem. 264, 5480-5487.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5480-5487
    • Watt, V.M.1    Yip, C.C.2
  • 4
    • 0025139262 scopus 로고
    • Molecular cloning of the murine BP-1/6C3 antigen: A member of the zinc-dependent metallopeptidase family
    • Wu, Q., Lahti, J. M., Air, G. M., Burrows, P. D., and Cooper, M. D. (1990) Molecular cloning of the murine BP-1/6C3 antigen: a member of the zinc-dependent metallopeptidase family, Proc. Natl. Acad. Sci. U.S.A. 87, 993-997.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 993-997
    • Wu, Q.1    Lahti, J.M.2    Air, G.M.3    Burrows, P.D.4    Cooper, M.D.5
  • 5
    • 0023618035 scopus 로고
    • Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis
    • Minami, M., Ohno, S., Kawasaki, H., Radmark, O., Samuelsson, B., Jörnvall, H., Shimizu, T., Seyama, Y., and Suzuki, K. (1987) Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis, J. Biol. Chem. 262, 13873-13876.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13873-13876
    • Minami, M.1    Ohno, S.2    Kawasaki, H.3    Radmark, O.4    Samuelsson, B.5    Jörnvall, H.6    Shimizu, T.7    Seyama, Y.8    Suzuki, K.9
  • 6
    • 0026533451 scopus 로고
    • Molecular cloning and functional expression of rat leukotriene A4 hydrolase using the polymerase chain reaction
    • Makita, N., Funk, C. D., Imai, E., Hoover, R.-L., and Badr, K. F. (1992) Molecular cloning and functional expression of rat leukotriene A4 hydrolase using the polymerase chain reaction, FEBS Lett. 299, 273-277.
    • (1992) FEBS Lett. , vol.299 , pp. 273-277
    • Makita, N.1    Funk, C.D.2    Imai, E.3    Hoover, R.-L.4    Badr, K.F.5
  • 8
    • 0029103116 scopus 로고
    • Amino-acid sequence and tissue distribution of guinea-pig leukotriene A4 hydrolase
    • Minami, M., Mutoh, H., Ohishi, N., Honda, Z., Bito, H., and Shimizu, T. (1995) Amino-acid sequence and tissue distribution of guinea-pig leukotriene A4 hydrolase, Gene 161, 249-251.
    • (1995) Gene , vol.161 , pp. 249-251
    • Minami, M.1    Mutoh, H.2    Ohishi, N.3    Honda, Z.4    Bito, H.5    Shimizu, T.6
  • 9
    • 0033137055 scopus 로고    scopus 로고
    • Aminopeptidase B is structurally related to leukotriene-A4 hydrolase but is not a bifunctional enzyme with epoxide hydrolase activity
    • Fukasawa, K. M., Fukasawa, K., Harada, M., Hirose, J., Izumi, T., and Shimizu, T. (1999) Aminopeptidase B is structurally related to leukotriene-A4 hydrolase but is not a bifunctional enzyme with epoxide hydrolase activity, Biochem. J. 339, 497-502.
    • (1999) Biochem. J. , vol.339 , pp. 497-502
    • Fukasawa, K.M.1    Fukasawa, K.2    Harada, M.3    Hirose, J.4    Izumi, T.5    Shimizu, T.6
  • 10
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidase
    • Matthews, B. W. (1988) Structural basis of the action of thermolysin and related zinc peptidase, Acc. Chem. Res. 21, 333-340.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 11
    • 0027208935 scopus 로고
    • Aminopeptidases: Towards a mechanism of action
    • Taylor, A. (1993) Aminopeptidases: towards a mechanism of action, Trends Biochem. Sci. 18, 167-172.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 167-172
    • Taylor, A.1
  • 12
    • 0001165102 scopus 로고
    • Soluble Arginyl Aminopeptidase
    • (McDonald, J. K., and Barrett, A. J., Eds), Academic Press, Inc., London
    • McDonald, J. K., and Barrett, A. J. (1986) Soluble Arginyl Aminopeptidase, in Mammalian Proteases (McDonald, J. K., and Barrett, A. J., Eds), Vol. 2, pp. 48-55, Academic Press, Inc., London.
    • (1986) Mammalian Proteases , vol.2 , pp. 48-55
    • McDonald, J.K.1    Barrett, A.J.2
  • 13
    • 0035146853 scopus 로고    scopus 로고
    • Crystal structure of human leukotriene A4 hydrolase, a bifunctinal enzyme in inflammation
    • Thunnissen, M. M. G. M., Nordlund, P., and Haeggström, J. Z. (2001) Crystal structure of human leukotriene A4 hydrolase, a bifunctinal enzyme in inflammation, Nat. Struct. Biol. 8, 131-135.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 131-135
    • Thunnissen, M.M.G.M.1    Nordlund, P.2    Haeggström, J.Z.3
  • 14
    • 0013858809 scopus 로고
    • Purification of mammalian peptidase selective for N-terminal arginine and lysine residues: Aminopeptidase B
    • Hopsu, V. K., Mäkinen, K. K., and Glenner, G. G. (1966) Purification of mammalian peptidase selective for N-terminal arginine and lysine residues: aminopeptidase B, Arch. Biochem. Biophys. 114, 557-566.
    • (1966) Arch. Biochem. Biophys. , vol.114 , pp. 557-566
    • Hopsu, V.K.1    Mäkinen, K.K.2    Glenner, G.G.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., Olson, A. J. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function, J. Comput. Chem. 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 17
    • 84874647051 scopus 로고    scopus 로고
    • AutoDockTools, http://www.scripps.edu/%7Esanner/python/index.html.
    • AutoDockTools
  • 18
    • 0842341771 scopus 로고
    • Development and use of quantum mechanical molecular models. 76. AM1: A new general purpose quantum mechanical molecular model
    • Dewar, M. J. S., Zoebisch, E. G., Healy, E. F., and Stewart, J. J. P. (1985) Development and use of quantum mechanical molecular models. 76. AM1: a new general purpose quantum mechanical molecular model, J. Am. Chem. Soc. 107, 3902-3909.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 3902-3909
    • Dewar, M.J.S.1    Zoebisch, E.G.2    Healy, E.F.3    Stewart, J.J.P.4
  • 19
    • 0032168209 scopus 로고    scopus 로고
    • Aglutamate residue contributes to the exopeptidase specificity in aminopeptidase A
    • Vazeux, G., Iturrioz, X., Corvol, P., and Llorens-Cortes, C. (1998) Aglutamate residue contributes to the exopeptidase specificity in aminopeptidase A, Biochem. J. 334, 407-413.
    • (1998) Biochem. J. , vol.334 , pp. 407-413
    • Vazeux, G.1    Iturrioz, X.2    Corvol, P.3    Llorens-Cortes, C.4
  • 20
    • 0032512368 scopus 로고    scopus 로고
    • Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): Insights into its mechanism of action
    • Luciani, N., Marie-Claire, C., Ruffet, E., Beaumont, A., Roques, B. P., and Fournie-Zaluski, M.-C. (1998) Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): insights into its mechanism of action, Biochemistry 37, 686-692.
    • (1998) Biochemistry , vol.37 , pp. 686-692
    • Luciani, N.1    Marie-Claire, C.2    Ruffet, E.3    Beaumont, A.4    Roques, B.P.5    Fournie-Zaluski, M.-C.6
  • 21
    • 0037059334 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms
    • Rudberg, P. C., Tholander, F., Thunnissen, M. M. G. M., and Haeggström, J. Z. (2002) Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms, J. Biol. Chem. 277, 1398-1404.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1398-1404
    • Rudberg, P.C.1    Tholander, F.2    Thunnissen, M.M.G.M.3    Haeggström, J.Z.4
  • 22
    • 0030914274 scopus 로고    scopus 로고
    • Aminopeptidase B from rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase
    • Cadel, S., Foulon, T., Viron, A., Balogh, A., Midol-Monnet, S., Noel, N., and Cohen, P. (1997) Aminopeptidase B from rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase, Proc. Natl. Acad. Sci. U.S.A. 94, 2964-2968.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2964-2968
    • Cadel, S.1    Foulon, T.2    Viron, A.3    Balogh, A.4    Midol-Monnet, S.5    Noel, N.6    Cohen, P.7
  • 23
    • 0036778551 scopus 로고    scopus 로고
    • Crystal structures of leukotriene A4 hydrolase in complex with captopril and two competitive tight-binding inhibitors
    • Thunnissen, M. M. G. M., Andersson, B., Samuelsson, B., Wong, C.-H., and Haeggström, J. Z. (2002) Crystal structures of leukotriene A4 hydrolase in complex with captopril and two competitive tight-binding inhibitors, FASEB J. 16, 1648-1650.
    • (2002) FASEB J. , vol.16 , pp. 1648-1650
    • Thunnissen, M.M.G.M.1    Andersson, B.2    Samuelsson, B.3    Wong, C.-H.4    Haeggström, J.Z.5
  • 25
    • 0029103125 scopus 로고
    • Evidence for a catalytic role of tyrosine 383 in the peptidase reaction of leukotriene A4 hydrolase
    • Blomster, M., Wetterholm, A., Mueller, M. J., and Haeggström, J. Z. (1995) Evidence for a catalytic role of tyrosine 383 in the peptidase reaction of leukotriene A4 hydrolase, Eur. J. Biochem. 231, 528-534.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 528-534
    • Blomster, M.1    Wetterholm, A.2    Mueller, M.J.3    Haeggström, J.Z.4
  • 26
    • 0030713348 scopus 로고    scopus 로고
    • A tyrosine residue essential for catalytic activity in aminopeptidase A
    • Vazeux, G., Iturrioz, X., Corvol, P., and Llorens-Cortes, C. (1997) A tyrosine residue essential for catalytic activity in aminopeptidase A, Biochem. J. 327, 883-889.
    • (1997) Biochem. J. , vol.327 , pp. 883-889
    • Vazeux, G.1    Iturrioz, X.2    Corvol, P.3    Llorens-Cortes, C.4
  • 28
    • 3042549380 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase: Identification of common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates
    • Rudberg, P. C., Tholander, F., Andberg, A., Thunnissen, M. M. G. M., and Haeggström, J. Z. (2004) Leukotriene A4 hydrolase: Identification of common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates, J. Biol. Chem. 279, 27376-27382.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27376-27382
    • Rudberg, P.C.1    Tholander, F.2    Andberg, A.3    Thunnissen, M.M.G.M.4    Haeggström, J.Z.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.