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Volumn 43, Issue 2, 2001, Pages 175-185

Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase

Author keywords

Crystal structures; Electrostatic surface charges; Isoforms; Kinetics; Oxidoreductase

Indexed keywords

ISOENZYME; LACTATE DEHYDROGENASE;

EID: 0035342452     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0134(20010501)43:2<175::aid-prot1029>3.0.co;2-%23     Document Type: Article
Times cited : (264)

References (30)
  • 2
    • 4244132999 scopus 로고    scopus 로고
    • Nicotinamide cofactor-dependent enzymes
    • Sinnott M, editor. Comprehensive biological catalysis: a mechanistic reference. New York: Academic Press
    • (1998) , vol.3 , pp. 1-80
    • Clarke, A.R.1    Dafforn, T.R.2
  • 7
    • 0027402941 scopus 로고
    • Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
    • (1993) J Mol Biol , vol.230 , pp. 21-27
    • Iwata, S.1    Ohta, T.2
  • 24
    • 0030612614 scopus 로고    scopus 로고
    • Use of H-1 NMR spectroscopy and computer simulations to analyze histidine pK (a) changes in a protein tyrosine phosphatase: Experimental and theoretical determination of electrostatic properties in a small protein
    • (1997) Biochemistry , vol.36 , pp. 11984-11994
    • Tishmack, P.A.1    Bashford, D.2    Harms, E.3    VanEtten, R.L.4
  • 30
    • 0015817965 scopus 로고
    • The kinetics of the interconversion of intermediates of the reaction of pig muscle lactate dehydrogenase with oxidized nicotinamide-adenine dinucleotide and lactate
    • (1973) Biochem J , vol.135 , pp. 81-85
    • Bennett, N.G.1    Gutfreund, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.