메뉴 건너뛰기




Volumn 114, Issue 6, 2007, Pages 721-724

Do monomeric vs dimeric forms of MAO-A make a difference? A direct comparison of the catalytic properties of rat and human MAO-A's

Author keywords

Human; Monoamine oxidase A; Oligomerization state; Rat

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A;

EID: 34250873549     PISSN: 03009564     EISSN: 14351463     Source Type: Journal    
DOI: 10.1007/s00702-007-0678-8     Document Type: Conference Paper
Times cited : (15)

References (11)
  • 1
    • 5044248542 scopus 로고    scopus 로고
    • Positive selection in MAO a gene is human exclusive: Determination of the putative amino acid change selected in the human lineage
    • AM Andrés M Soldevila A Navarro KK Kidd B Oliva J Bertranpetit 2004 Positive selection in MAO A gene is human exclusive: determination of the putative amino acid change selected in the human lineage Hum Genet 115 377 386
    • (2004) Hum Genet , vol.115 , pp. 377-386
    • Andrés, A.M.1    Soldevila, M.2    Navarro, A.3    Kidd, K.K.4    Oliva, B.5    Bertranpetit, J.6
  • 2
    • 20544433165 scopus 로고
    • Van der Waals volumes and radii
    • A Bondi 1964 Van der Waals volumes and radii J Phys Chem 68 441 451
    • (1964) J Phys Chem , vol.68 , pp. 441-451
    • Bondi, A.1
  • 3
    • 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
    • LD Colibus M Li C Binda A Lustig DE Edmondson A Mattevi 2005 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 12684 12689
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12684-12689
    • Colibus, L.D.1    Li, M.2    Binda, C.3    Lustig, A.4    Edmondson, D.E.5    Mattevi, A.6
  • 5
    • 0001222320 scopus 로고
    • Calculation of substrate dissociation constants from steady-state isotope effects in enzyme-catalyzed reactions
    • JP Klinman RG Matthews 1985 Calculation of substrate dissociation constants from steady-state isotope effects in enzyme-catalyzed reactions J Am Chem Soc 107 1058 1060
    • (1985) J Am Chem Soc , vol.107 , pp. 1058-1060
    • Klinman, J.P.1    Matthews, R.G.2
  • 6
    • 0035996741 scopus 로고    scopus 로고
    • High-level expression of human liver monoamine oxidase a in Pichia pastoris: Comparison with the enzyme expressed in Saccharomyces cervisiae
    • M Li F Hubálek P Newton-Vinson DE Edmondson 2002 High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cervisiae Protein Expr Purif 24 152 162
    • (2002) Protein Expr Purif , vol.24 , pp. 152-162
    • Li, M.1    Hubálek, F.2    Newton-Vinson, P.3    Edmondson, D.E.4
  • 7
    • 1842474296 scopus 로고    scopus 로고
    • Structure of rat monoamine oxidase a and its specific recognitions for substrates and inhibitors
    • J Ma M Yoshimura E Yamashita A Nakagawa A Ito T Tsukihara 2004 Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors J Mol Biol 338 103 114
    • (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
  • 8
    • 0014430090 scopus 로고
    • Human liver mitochondrial monoamine oxidase. I. Kinetic studies of model interactions
    • CM McEwen G Sasaki WR Lenz 1968 Human liver mitochondrial monoamine oxidase. I. Kinetic studies of model interactions J Biol Chem 243 5217 5225
    • (1968) J Biol Chem , vol.243 , pp. 5217-5225
    • McEwen, C.M.1    Sasaki, G.2    Lenz, W.R.3
  • 9
    • 0014594785 scopus 로고
    • Human liver mitochondrial monoamine oxidase. II. Determinants of substrate and inhibitor specificities
    • CM McEwen G Sasaki DC Jones 1969 Human liver mitochondrial monoamine oxidase. II. Determinants of substrate and inhibitor specificities Biochemistry 8 3952 3962
    • (1969) Biochemistry , vol.8 , pp. 3952-3962
    • McEwen, C.M.1    Sasaki, G.2    Jones, D.C.3
  • 10
    • 0033550070 scopus 로고    scopus 로고
    • Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase a
    • JR Miller DE Edmondson 1999 Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A Biochemistry 38 13670 13683
    • (1999) Biochemistry , vol.38 , pp. 13670-13683
    • Miller, J.R.1    Edmondson, D.E.2
  • 11
    • 0028278443 scopus 로고
    • Structure-activity relationships in the oxidation of benzylamine analogues by bovine liver mitochondrial monoamine oxidase B
    • MC Walker DE Edmondson 1994 Structure-activity relationships in the oxidation of benzylamine analogues by bovine liver mitochondrial monoamine oxidase B Biochemistry 33 7088 7098
    • (1994) Biochemistry , vol.33 , pp. 7088-7098
    • Walker, M.C.1    Edmondson, D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.