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Volumn 267, Issue 24, 2000, Pages 7158-7169

Sites of limited proteolysis in the pyruvate decarboxylase component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and their role in catalysis

Author keywords

Enzyme catalysis; Limited proteolysis; Multienzyme complex; Pyruvate decarboxylase; Pyruvate dehydrogenase

Indexed keywords

2,6 DICHLOROPHENOLINDOPHENOL; DIHYDROLIPOAMIDE ACETYLTRANSFERASE; PYRUVATE DECARBOXYLASE; PYRUVATE DEHYDROGENASE COMPLEX; PYRUVIC ACID;

EID: 0034533110     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01820.x     Document Type: Article
Times cited : (18)

References (49)
  • 1
    • 0026079562 scopus 로고
    • Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: A paradigm in the design of a multifunctional enzyme
    • (1991) Biochemistry , vol.30 , pp. 8501-8512
    • Perham, R.N.1
  • 2
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 963-1006
    • Perham, R.N.1
  • 11
    • 0028898978 scopus 로고
    • Interaction of component enzymes with the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: Stoichiometry and specificity in self assembly
    • (1995) Biochem. J. , vol.306 , pp. 727-733
    • Lessard, I.A.D.1    Perham, R.N.2
  • 12
    • 0030464497 scopus 로고    scopus 로고
    • Competitive interaction Of component enzymes with the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: Kinetic analysis using surface plasmon resonance detection
    • (1996) Biochemistry , vol.35 , pp. 16863-16870
    • Lessard, I.A.D.1    Fuller, C.2    Perham, R.N.3
  • 26
    • 0019811537 scopus 로고
    • Limited proteolysis and proton NMR spectroscopy of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli
    • (1981) Biochem. J. , vol.199 , pp. 733-740
    • Perham, R.N.1    Roberts, G.C.2
  • 30
    • 0019247949 scopus 로고
    • Bovine kidney pyruvate dehydrogenase complex. Limited proteolysis and molecular structure of the lipoate acetyltransferase component
    • (1980) Eur. J. Biochem. , vol.112 , pp. 589-599
    • Kresze, G.B.1    Ronft, H.2
  • 37
    • 0026521978 scopus 로고
    • Expression in Escherichia coli of a sub-gene encoding the lipoyl and peripheral subunit-binding domains of the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex of Bacillus stearothermophilus
    • (1992) Biochem. J. , vol.283 , pp. 665-671
    • Hipps, D.S.1    Perham, R.N.2
  • 38
    • 0028247161 scopus 로고
    • Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product
    • (1994) J. Biol. Chem. , vol.269 , pp. 16091-16100
    • Morris, T.W.1    Reed, K.E.2    Cronan, J.E.3
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 45
    • 0000861827 scopus 로고
    • Determination of the number of active-centers in the pyruvate dehydrogenase component of the pyruvate dehydrogenase complex from pigeon breast muscle
    • (1982) Biochem. Int. , vol.5 , pp. 525-532
    • Khailova, L.S.1    Korochkina, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.