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Volumn , Issue 1, 2006, Pages 60-62

Mechanism of α-oxoamine synthases: Identification of the intermediate Claisen product in the 8-amino-7-oxononanoate synthase reaction

Author keywords

[No Author keywords available]

Indexed keywords

8 AMINO 7 OXONONANOATE SYNTHASE; ALANINE DERIVATIVE; ALPHA OXOAMINE SYNTHASE; COENZYME A; ESTER DERIVATIVE; IMINE; METHYL GROUP; NONANOIC ACID; OXOACID; PYRIDOXAL 5 PHOSPHATE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 33645454058     PISSN: 13597345     EISSN: None     Source Type: Journal    
DOI: 10.1039/b511837a     Document Type: Article
Times cited : (30)

References (29)
  • 1
    • 0003796783 scopus 로고
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter and H. E. Umbarger, American Society for Microbiology, Washington, DC, pp. 544-550
    • M. A. Eisenberg, in Escherichia coli and Salmonella typhimurium, ed., F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter and H. E. Umbarger,, American Society for Microbiology, Washington, DC, 1987, vol. 1, pp. 544-550
    • (1987) Escherichia Coli and Salmonella Typhimurium, Ed. , vol.1
    • Eisenberg In, M.A.1
  • 25
    • 33645449906 scopus 로고    scopus 로고
    • m [l-alanine] = 1.14 (0.12) mM
    • m [l-alanine] = 1.14 (0.12) mM
  • 26
    • 33645458428 scopus 로고    scopus 로고
    • i = 2.8 mM). It seems reasonable to suggest that, in the absence of the second substrate, protonation of the methylated quinonoid adduct occurs on the solvent accessible Si face to give the unproductive enantiomeric d-alanine aldimine
    • i = 2.8 mM). It seems reasonable to suggest that, in the absence of the second substrate, protonation of the methylated quinonoid adduct occurs on the solvent accessible Si face to give the unproductive enantiomeric d-alanine aldimine


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.