메뉴 건너뛰기




Volumn 29, Issue 4, 1997, Pages 589-594

Partial inactivation of chorismate mutase-prephenate dehydrogenase from Escherichia coli in the presence of analogues of chorismate

Author keywords

Adamantane; Chorismate; Inactivation; Inhibition; Prephenate

Indexed keywords

ADAMANTANE DERIVATIVE; CHORISMATE MUTASE; MANDELIC ACID; PREPHENATE DEHYDROGENASE;

EID: 0030919543     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(96)00176-8     Document Type: Article
Times cited : (3)

References (13)
  • 1
    • 0027992458 scopus 로고
    • The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate and implications for the mechanism of the enzymatic reaction
    • Chook Y. M., Gray J. V., Ke H. and Lipscomb W. N. (1994) The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate and implications for the mechanism of the enzymatic reaction. J. Mol. Biol. 240, 476-500.
    • (1994) J. Mol. Biol. , vol.240 , pp. 476-500
    • Chook, Y.M.1    Gray, J.V.2    Ke, H.3    Lipscomb, W.N.4
  • 2
    • 0029863631 scopus 로고    scopus 로고
    • Identification of the active site residues of chorismate mutase-prephenate dehydrogenase from Escherichia coli
    • Christendat D. and Turnbull J. (1996) Identification of the active site residues of chorismate mutase-prephenate dehydrogenase from Escherichia coli. Biochemistry 35, 4468-4479.
    • (1996) Biochemistry , vol.35 , pp. 4468-4479
    • Christendat, D.1    Turnbull, J.2
  • 3
    • 0022263778 scopus 로고
    • Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Cooperative effects and inhibition by L-tyrosine
    • Christopherson R. I. (1985) Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Cooperative effects and inhibition by L-tyrosine. Arch. Biochem. Biophys. 240, 646-654.
    • (1985) Arch. Biochem. Biophys. , vol.240 , pp. 646-654
    • Christopherson, R.I.1
  • 4
    • 0020624492 scopus 로고
    • Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Spatial relationship of the mutase and dehydrogenase sites
    • Christopherson R. I., Heyde E. and Morrison J. F. (1983) Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Spatial relationship of the mutase and dehydrogenase sites. Biochemistry 22, 1650-1656.
    • (1983) Biochemistry , vol.22 , pp. 1650-1656
    • Christopherson, R.I.1    Heyde, E.2    Morrison, J.F.3
  • 5
    • 0021833727 scopus 로고
    • Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Positive cooperativity with substrates and inhibitors
    • Christopherson R. I. and Morrison J. F. (1985) Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Positive cooperativity with substrates and inhibitors. Biochemistry 24, 1116-1121.
    • (1985) Biochemistry , vol.24 , pp. 1116-1121
    • Christopherson, R.I.1    Morrison, J.F.2
  • 6
    • 0023044277 scopus 로고
    • Progress curves of reactions catalysed by unstable enzymes. A theoretical approach
    • Duggleby R. G. (1986) Progress curves of reactions catalysed by unstable enzymes. A theoretical approach. J. Theoret. Biol. 123, 67-80.
    • (1986) J. Theoret. Biol. , vol.123 , pp. 67-80
    • Duggleby, R.G.1
  • 7
    • 0017341713 scopus 로고
    • The analysis of progress curves for enzyme-catalysed reactions by non-linear regression
    • Duggleby R. G. and Morrison J. F. (1977) The analysis of progress curves for enzyme-catalysed reactions by non-linear regression. Biochim. Biophys. Acta 481, 297-312.
    • (1977) Biochim. Biophys. Acta , vol.481 , pp. 297-312
    • Duggleby, R.G.1    Morrison, J.F.2
  • 8
    • 0018802006 scopus 로고
    • Chorismate mutase-prephenate dehydrogenase from Atrobacter aerogenes: Evidence that the two reactions occur at one active site
    • Heyde E. (1979) Chorismate mutase-prephenate dehydrogenase from Atrobacter aerogenes: evidence that the two reactions occur at one active site. Biochemistry 18, 2766-2775.
    • (1979) Biochemistry , vol.18 , pp. 2766-2775
    • Heyde, E.1
  • 9
    • 0021755218 scopus 로고
    • Chorismate mutase-prephenate dehydrogenase from Escherichia coli K12: Purification, characterization and identification of a reactive cysteine
    • Hudson G. S., Wong V. and Davidson B. E. (1984) Chorismate mutase-prephenate dehydrogenase from Escherichia coli K12: purification, characterization and identification of a reactive cysteine. Biochemistry 23, 6240-6249.
    • (1984) Biochemistry , vol.23 , pp. 6240-6249
    • Hudson, G.S.1    Wong, V.2    Davidson, B.E.3
  • 10
    • 0018715101 scopus 로고
    • Study of chorismate mutase-prephenate dehydrogenase in crude cell extracts of Escherichia coli
    • Llewellyn D. J. and Smith G. D. (1979) Study of chorismate mutase-prephenate dehydrogenase in crude cell extracts of Escherichia coli. Biochemistry 18, 4707-4714.
    • (1979) Biochemistry , vol.18 , pp. 4707-4714
    • Llewellyn, D.J.1    Smith, G.D.2
  • 11
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme catalysed reactions
    • Morrison J. F. (1982) The slow-binding and slow, tight-binding inhibition of enzyme catalysed reactions. TIBS 7, 102-105.
    • (1982) TIBS , vol.7 , pp. 102-105
    • Morrison, J.F.1
  • 12
    • 0019963076 scopus 로고
    • Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Purification and properties of the bifunctional enzyme
    • SampathKumar P. and Morrison J. F. (1982) Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Purification and properties of the bifunctional enzyme. Biochim. Biophys. Acta 702, 204-211.
    • (1982) Biochim. Biophys. Acta , vol.702 , pp. 204-211
    • SampathKumar, P.1    Morrison, J.F.2
  • 13
    • 0025172991 scopus 로고
    • Chorismate mutase-prephenate dehydrogenase from Escherichia coli. 2. Evidence for two different active sites
    • Turnbull J. and Morrison J. F. (1990) Chorismate mutase-prephenate dehydrogenase from Escherichia coli. 2. Evidence for two different active sites. Biochemistry 29, 10255-10261.
    • (1990) Biochemistry , vol.29 , pp. 10255-10261
    • Turnbull, J.1    Morrison, J.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.