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Volumn 70, Issue 2, 2010, Pages 211-217

High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: Comparison with human MAO A

Author keywords

Flavoenzyme; Monoamine oxidase A; Pichia pastoris; Rat liver MAO A; Thermal stability

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); BENZYLAMINE; BENZYLAMINE DERIVATIVE; PHENETHYLAMINE; PHENETHYLAMINE DERIVATIVE;

EID: 76749104256     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.10.013     Document Type: Article
Times cited : (19)

References (23)
  • 1
    • 0025074333 scopus 로고
    • Biochemistry and genetics of monoamine oxidase
    • Weyler W., Hsu Y.P., and Breakefield X.O. Biochemistry and genetics of monoamine oxidase. Pharmacol. Ther. 47 (1990) 391-417
    • (1990) Pharmacol. Ther. , vol.47 , pp. 391-417
    • Weyler, W.1    Hsu, Y.P.2    Breakefield, X.O.3
  • 2
    • 24644437716 scopus 로고    scopus 로고
    • Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B
    • De Colibus L., Li M., Binda C., Lustig A., Edmondson D.E., and Mattevi A. Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc. Natl. Acad. Sci. USA 102 (2005) 12684-12689
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12684-12689
    • De Colibus, L.1    Li, M.2    Binda, C.3    Lustig, A.4    Edmondson, D.E.5    Mattevi, A.6
  • 3
    • 44449117421 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase A at 2,2-angstrom resolution: the control of opening the entry for substrates/inhibitors
    • Son S.Y., Ma J., Kondou Y., Yoshimura M., Yamashita E., and Tsukihara T. Structure of human monoamine oxidase A at 2,2-angstrom resolution: the control of opening the entry for substrates/inhibitors. Proc. Natl. Acad. Sci. USA 105 (2008) 5739-5744
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5739-5744
    • Son, S.Y.1    Ma, J.2    Kondou, Y.3    Yoshimura, M.4    Yamashita, E.5    Tsukihara, T.6
  • 4
    • 1842474296 scopus 로고    scopus 로고
    • Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors
    • Ma J., Yoshimura M., Yamashita E., Nakagawa A., Ito A., and Tsukihara T. Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors. J. Mol. Biol. 338 (2004) 103-114
    • (2004) J. Mol. Biol. , vol.338 , pp. 103-114
    • Ma, J.1    Yoshimura, M.2    Yamashita, E.3    Nakagawa, A.4    Ito, A.5    Tsukihara, T.6
  • 5
    • 38949096792 scopus 로고    scopus 로고
    • Determination of the oligomeric states of human and rat monoamine oxidases in the outer mitochondrial membrane and octyl β-d-glucopyranoside micelles using pulsed dipolar electron spin resonance spectroscopy
    • Upadhyay A.K., Borbat P.P., Wang J., Freed J.H., and Edmondson D.E. Determination of the oligomeric states of human and rat monoamine oxidases in the outer mitochondrial membrane and octyl β-d-glucopyranoside micelles using pulsed dipolar electron spin resonance spectroscopy. Biochemistry 47 (2008) 1554-1566
    • (2008) Biochemistry , vol.47 , pp. 1554-1566
    • Upadhyay, A.K.1    Borbat, P.P.2    Wang, J.3    Freed, J.H.4    Edmondson, D.E.5
  • 6
    • 34249940141 scopus 로고    scopus 로고
    • Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: insights from molecular modeling studies
    • Fierro A., Osorio-Olivares M., Cassels B.K., Edmondson D.E., Sepulveda-Boza S., and Reyes-Parada M. Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: insights from molecular modeling studies. Bioorg. Med. Chem. 15 (2007) 5198-5206
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 5198-5206
    • Fierro, A.1    Osorio-Olivares, M.2    Cassels, B.K.3    Edmondson, D.E.4    Sepulveda-Boza, S.5    Reyes-Parada, M.6
  • 7
    • 0035996741 scopus 로고    scopus 로고
    • High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae
    • Li M., Hubalek F., Newton-Vinson P., and Edmondson D.E. High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr. Purif. 24 (2002) 152-162
    • (2002) Protein Expr. Purif. , vol.24 , pp. 152-162
    • Li, M.1    Hubalek, F.2    Newton-Vinson, P.3    Edmondson, D.E.4
  • 8
    • 0017600026 scopus 로고
    • Purification and immunochemical characterization of monoamine-oxidase from rat and human liver
    • Dennick R.G., and Mayer R.J. Purification and immunochemical characterization of monoamine-oxidase from rat and human liver. Biochem. J. 161 (1977) 167-174
    • (1977) Biochem. J. , vol.161 , pp. 167-174
    • Dennick, R.G.1    Mayer, R.J.2
  • 9
    • 0020479807 scopus 로고
    • 2 and cytochrome-c peroxidase are located in the intermembrane space of yeast mitochondria
    • 2 and cytochrome-c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257 (1982) 13028-13033
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 10
    • 77957012032 scopus 로고
    • Spectrophotometric and turbidimetric methods for measuring proteins
    • Layne E. Spectrophotometric and turbidimetric methods for measuring proteins. Methods Enzymol. 3 (1957) 447-454
    • (1957) Methods Enzymol. , vol.3 , pp. 447-454
    • Layne, E.1
  • 11
    • 0018085511 scopus 로고
    • Quantitation of sub-microgram quantities of protein by an improved protein-dye binding assay
    • Bearden J.C. Quantitation of sub-microgram quantities of protein by an improved protein-dye binding assay. Biochim. Biophys. Acta 533 (1978) 525-529
    • (1978) Biochim. Biophys. Acta , vol.533 , pp. 525-529
    • Bearden, J.C.1
  • 13
    • 0033773601 scopus 로고    scopus 로고
    • High-level expression of human liver monoamine oxidase B in Pichia pastoris
    • Newton-Vinson P., Hubalek F., and Edmondson D.E. High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr. Purif. 20 (2000) 334-345
    • (2000) Protein Expr. Purif. , vol.20 , pp. 334-345
    • Newton-Vinson, P.1    Hubalek, F.2    Edmondson, D.E.3
  • 14
    • 0036140732 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
    • Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., and Mattevi A. Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat. Struct. Biol. 9 (2002) 22-26
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 22-26
    • Binda, C.1    Newton-Vinson, P.2    Hubalek, F.3    Edmondson, D.E.4    Mattevi, A.5
  • 15
    • 18144423424 scopus 로고    scopus 로고
    • Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors
    • Hubalek F., Binda C., Khalil A., Li M., Mattevi A., Castagnoli N., and Edmondson D.E. Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors. J. Biol. Chem. 280 (2005) 15761-15766
    • (2005) J. Biol. Chem. , vol.280 , pp. 15761-15766
    • Hubalek, F.1    Binda, C.2    Khalil, A.3    Li, M.4    Mattevi, A.5    Castagnoli, N.6    Edmondson, D.E.7
  • 16
    • 0025871857 scopus 로고
    • Kinetic mechanism of monoamine oxidase A
    • Ramsay R.R. Kinetic mechanism of monoamine oxidase A. Biochemistry 30 (1991) 4624-4629
    • (1991) Biochemistry , vol.30 , pp. 4624-4629
    • Ramsay, R.R.1
  • 17
    • 0032127904 scopus 로고    scopus 로고
    • N-terminal processing: the methionine aminopeptidase and N-alpha-acetyl transferase families
    • Bradshaw R.A., Brickey W.W., and Walker K.W. N-terminal processing: the methionine aminopeptidase and N-alpha-acetyl transferase families. Trends Biochem. Sci. 23 (1998) 263-267
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 263-267
    • Bradshaw, R.A.1    Brickey, W.W.2    Walker, K.W.3
  • 18
    • 0023754392 scopus 로고
    • Cotranslational processing and protein turnover in eukaryotic cells
    • Arfin S.M., and Bradshaw R.A. Cotranslational processing and protein turnover in eukaryotic cells. Biochemistry 27 (1988) 7979-7984
    • (1988) Biochemistry , vol.27 , pp. 7979-7984
    • Arfin, S.M.1    Bradshaw, R.A.2
  • 19
    • 0026744480 scopus 로고
    • 2 terminus is necessary for virus particle assembly
    • 2 terminus is necessary for virus particle assembly. J. Biol. Chem. 267 (1992) 20277-20281
    • (1992) J. Biol. Chem. , vol.267 , pp. 20277-20281
    • Tercero, J.C.1    Wickner, R.B.2
  • 20
    • 0022094817 scopus 로고
    • Methionine or not methionine at the beginning of a protein
    • Sherman F., Stewart J.W., and Tsunasawa S. Methionine or not methionine at the beginning of a protein. Bioessays 3 (1985) 27-31
    • (1985) Bioessays , vol.3 , pp. 27-31
    • Sherman, F.1    Stewart, J.W.2    Tsunasawa, S.3
  • 21
    • 0033550070 scopus 로고    scopus 로고
    • Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A
    • Miller J.R., and Edmondson D.E. Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A. Biochemistry 38 (1999) 13670-13683
    • (1999) Biochemistry , vol.38 , pp. 13670-13683
    • Miller, J.R.1    Edmondson, D.E.2
  • 22
    • 0035846625 scopus 로고    scopus 로고
    • Loss of serotonin oxidation as a component of the altered substrate specificity in the Y444F mutant of recombinant human liver MAO A
    • Nandigama R.K., Miller J.R., and Edmondson D.E. Loss of serotonin oxidation as a component of the altered substrate specificity in the Y444F mutant of recombinant human liver MAO A. Biochemistry 40 (2001) 14839-14846
    • (2001) Biochemistry , vol.40 , pp. 14839-14846
    • Nandigama, R.K.1    Miller, J.R.2    Edmondson, D.E.3
  • 23
    • 0036496911 scopus 로고    scopus 로고
    • Phentermine inhibition of recombinant human liver monoamine oxidases A and B
    • Nandigama R.K., Newton-Vinson P., and Edmondson D.E. Phentermine inhibition of recombinant human liver monoamine oxidases A and B. Biochem. Pharmacol. 63 (2002) 865-869
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 865-869
    • Nandigama, R.K.1    Newton-Vinson, P.2    Edmondson, D.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.