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Volumn 273, Issue 36, 1998, Pages 23219-23224

Amino acid substitutions in the C-terminal regulatory domain disrupt allosteric effector binding to biosynthetic threonine deaminase from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERISM; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; EFFECTOR CELL; ENZYME ACTIVITY; ENZYME KINETICS; ESCHERICHIA COLI; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; SIGMOID;

EID: 0032483527     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.36.23219     Document Type: Article
Times cited : (13)

References (23)
  • 1
    • 0001348712 scopus 로고
    • Neidhart, F. C., Ingraham, J. L., Low, K. B., Magasanik, B., Schaechter, M., and Umbarger, H. E., eds American Society for Microbiology, Washington, D. C.
    • Umbarger, H. E. (1987) in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhart, F. C., Ingraham, J. L., Low, K. B., Magasanik, B., Schaechter, M., and Umbarger, H. E., eds) pp. 352-367, American Society for Microbiology, Washington, D. C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 352-367
    • Umbarger, H.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.