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Volumn 334, Issue 1, 2004, Pages 204-206

Nonlinear fitting of bisubstrate enzyme kinetic models using SAS computer software: Application to R67 dihydrofolate reductase

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CHEMISTRY;

EID: 4644269136     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.06.040     Document Type: Article
Times cited : (9)

References (9)
  • 1
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data.
    • W.W. Cleland Statistical analysis of enzyme kinetic data. Methods Enzymol. 63 1979 103 138
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 3
    • 33845914337 scopus 로고    scopus 로고
    • SAS Institute, Inc, Cary, NC., SAS/STAT Software, Version 9.1, (2003) see http://www.sas.com/technologies/analytics/statistics/stat/
    • (2003) SAS/STAT Software, Version 9.1
  • 5
    • 0028800949 scopus 로고
    • A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site
    • N. Narayana, D.A. Matthews, E.E. Howell, and N.H. Xuong A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site Nat. Struct. Biol. 2 1995 1018 1025
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1018-1025
    • Narayana, N.1    Matthews, D.A.2    Howell, E.E.3    Xuong, N.H.4
  • 6
    • 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
    • T.D. Bradrick, J.M. Beechem, and E.E. Howell 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 Biochemistry 35 1996 11414 11424
    • (1996) Biochemistry , vol.35 , pp. 11414-11424
    • Bradrick, T.D.1    Beechem, J.M.2    Howell, E.E.3
  • 7
    • 0031282924 scopus 로고    scopus 로고
    • A glutamine 67 → histidine mutation in homotetrameric R67 dihydrofolate reductase results in four mutations per single active site pore and causes substantial substrate and cofactor inhibition
    • H. Park, T.D. Bradrick, and E.E. Howell A glutamine 67 → histidine mutation in homotetrameric R67 dihydrofolate reductase results in four mutations per single active site pore and causes substantial substrate and cofactor inhibition Protein Eng. 10 1997 1415 1424
    • (1997) Protein Eng. , vol.10 , pp. 1415-1424
    • Park, H.1    Bradrick, T.D.2    Howell, E.E.3
  • 8
    • 2942595927 scopus 로고    scopus 로고
    • Defining the binding site of homotetrameric R67 dihydrofolate reductase and correlating binding enthalpy with catalysis
    • M.B. Strader, S. Chopra, M. Jackson, R.D. Smiley, L.G. Stinnett, J. Wu, and E.E. Howell Defining the binding site of homotetrameric R67 dihydrofolate reductase and correlating binding enthalpy with catalysis Biochemistry 43 2004 7403 7412
    • (2004) Biochemistry , vol.43 , pp. 7403-7412
    • Strader, M.B.1    Chopra, S.2    Jackson, M.3    Smiley, R.D.4    Stinnett, L.G.5    Wu, J.6    Howell, E.E.7
  • 9
    • 0037207139 scopus 로고    scopus 로고
    • Breaking symmetry: Mutations engineered into R67 dihydrofolate reductase, a D2 symmetric homotetramer possessing a single active site pore
    • R.D. Smiley, L.G. Stinnett, A.M. Saxton, and E.E. Howell Breaking symmetry: mutations engineered into R67 dihydrofolate reductase, a D2 symmetric homotetramer possessing a single active site pore Biochemistry 41 2002 15664 15675
    • (2002) Biochemistry , vol.41 , pp. 15664-15675
    • Smiley, R.D.1    Stinnett, L.G.2    Saxton, A.M.3    Howell, E.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.