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Volumn 115, Issue 45, 2011, Pages 13050-13060

The α-amino group of the threonine substrate as the general base during tRNA aminoacylation: A new version of substrate-assisted catalysis predicted by hybrid DFT

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMINO GROUP; AMINOACYL TRANSFER; AMINOACYLATION; CATALYTIC MECHANISMS; CHEMICAL MODEL; DENSITY FUNCTIONALS; GENERAL BASE; HYBRID DFT; O-H BOND; PROTON ACCEPTORS; PROTONATED; RATE LIMITING; RATE-LIMITING STEPS; SUBSTRATE-ASSISTED CATALYSIS; SYNTHETASES; TETRAHEDRAL INTERMEDIATES;

EID: 80855128989     PISSN: 10895639     EISSN: 15205215     Source Type: Journal    
DOI: 10.1021/jp205037a     Document Type: Article
Times cited : (17)

References (57)
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    • 80855124632 scopus 로고    scopus 로고
    • Mechanistics of Enzyme Catalysis: From Small to Large Active-Site Models
    • Matta, C. F. Wiley-VCH: Weinheim, Germany
    • Llano, J.; Gauld, J. W. Mechanistics of Enzyme Catalysis: From Small to Large Active-Site Models. In Quantum Biochemistry; Matta, C. F., Ed.; Wiley-VCH: Weinheim, Germany, 2010.
    • (2010) Quantum Biochemistry
    • Llano, J.1    Gauld, J.W.2
  • 47
    • 84855616651 scopus 로고    scopus 로고
    • version 2.0 ed. University of Applied Science: Bielefeld, Germany
    • Biegler-König, F.; Schönbohm, J. AIM2000, version 2.0 ed.; University of Applied Science: Bielefeld, Germany, 2002.
    • (2002) AIM2000
    • Biegler-König, F.1    Schönbohm, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.