메뉴 건너뛰기




Volumn 40, Issue 14, 2001, Pages 4242-4252

Interligand overhauser effects in type II dihydrofolate reductase

Author keywords

[No Author keywords available]

Indexed keywords

CHROMOSOMAL ENZYMES;

EID: 0035836454     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0026425     Document Type: Article
Times cited : (44)

References (37)
  • 4
    • 0018638966 scopus 로고
    • The amino acid sequence of the trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67
    • (1979) J. Biol. Chem. , vol.254 , pp. 10857-10861
    • Stone, D.1    Smith, S.L.2
  • 8
    • 0029738545 scopus 로고    scopus 로고
    • Unusual binding stoichiometries and cooperativity are observed during binary and ternary complex formation in the single active pore of R67 dihydrofolate reductase, a D2 symmetric protein
    • (1996) Biochemistry , vol.35 , pp. 11414-11424
    • Bradrick, T.D.1    Beechem, J.M.2    Howell, E.E.3
  • 11
    • 0033257882 scopus 로고    scopus 로고
    • Theoretical analysis of the Inter-Ligand Overhauser Effect, a new approach for mapping structural relationships of macromolecular ligands
    • (1999) J. Magn. Reson. , vol.141 , pp. 301-311
    • London, R.E.1
  • 21
    • 0015860668 scopus 로고
    • Proton magnetic resonance studies of folate, dihydrofolate and methotrexate. Evidence from pH and concentration studies for dimerization
    • (1978) J. Biol. Chem. , vol.248 , pp. 7025-7032
    • Poe, M.1
  • 22
    • 0014199125 scopus 로고
    • The measurement of triphosphopyridine nucleotide and reduced triphosphopyridine nucleotide and the role of hemoglobin in producing erroneous triphosphopyridine nucleotide values
    • (1967) J. Biol. Chem. , vol.242 , pp. 4546-4554
    • Burch, H.B.1    Bradley, M.E.2    Lowry, O.H.3
  • 29
    • 0020483210 scopus 로고
    • The stereoselectivity of alcohol dehydrogenases: A stereochemical imperative?
    • (1982) Experientia , vol.38 , pp. 633-636
    • Benner, S.A.1
  • 31
    • 0021903980 scopus 로고
    • Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions
    • (1985) Crit. Rev. Biochem. , vol.17 , pp. 313-451
    • You, K.S.1
  • 32
    • 0000046426 scopus 로고
    • The hydride-donation reaction of reduced nicotinamide adenine dinucleotide. 1. MINDO/3 and STO-3G calculations on analogue reactions with cyclopropene, tropilidene, and 1,4-dihydropyridine as hydride donors and the cyclopropenium cation as acceptor
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 6549-6554
    • Donkersloot, M.C.A.1    Buck, H.M.2
  • 35
    • 33845282135 scopus 로고
    • Theoretical transition structures for hydride transfer to methyleniminium ion from methylamine and dihydropyridine. On the nonlinearity of hydride transfers
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 226-227
    • Wu, Y.-D.1    Houk, K.N.2
  • 36
    • 0028908071 scopus 로고
    • Transition structures of hydride transfer reactions of protonated pyridinium ion with 1,4-dihydropyridine and protonated nicotinamide with 1,4-dihydronicotinamide
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 4100-4108
    • Wu, Y.-D.1    Lai, D.K.W.2    Houk, K.N.3
  • 37
    • 0033616094 scopus 로고    scopus 로고
    • Catalytic mechanism of dihydrofolate reductase enzyme. A combined quantum-mechanical/molecular-mechanical characterization of transition state structure for the hydride transfer step
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 12140-12147
    • Castillo, R.1    Andres, J.2    Moliner, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.