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Volumn , Issue 47, 2005, Pages 5873-5875

Dependence of enzyme reaction mechanism on protonation state of titratable residues and QM level description: Lactate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

LACTATE DEHYDROGENASE;

EID: 29644432365     PISSN: 13597345     EISSN: None     Source Type: Journal    
DOI: 10.1039/b510735k     Document Type: Article
Times cited : (20)

References (18)
  • 1
    • 0027477251 scopus 로고
    • See the following references, where the method is explained and its accuracy compared with that obtained with other methods: (a) M. K. Gilson, Proteins: Struct., Funct., Genet., 1993, 15, 266-282;
    • (1993) Proteins: Struct., Funct., Genet. , vol.15 , pp. 266-282
    • Gilson, M.K.1
  • 4
    • 0035912951 scopus 로고    scopus 로고
    • and references therein
    • See: P. Kedzierski, K. Moreton, A. R. Clarke and J. J. Holbrook, Biochemistry, 2001, 40, 7247-7252 and references therein.
    • (2001) Biochemistry , vol.40 , pp. 7247-7252
    • Holbrook, J.J.1
  • 14
    • 29644445267 scopus 로고    scopus 로고
    • note
    • a calculations also showed changes in the protonated nitrogen (from Nδ to Nε) in some neutral histidines (157, 188, 266, 318).
  • 17
    • 29644439729 scopus 로고    scopus 로고
    • note
    • -1 which, considering that the chemical step is not the rate limiting step of LDH catalyzed reaction, would be the upper limit.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.