Allosteric interactions within subsites of a monomeric enzyme: Kinetics of fluorogenic substrates of PI-specific phospholipase C

Biophysical Journal

Volumn 84, Issue 5, 2003, Pages 3264-3275

  Birrell, G Bruce ^a   Zaikova, Tatiana O ^a   Rukavishnikov, Aleksey V ^a   Keana, John F W ^a   Griffith, O Hayes ^a  

^a UNIVERSITY OF OREGON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; FLUORESCEIN; INOSITOL PHOSPHATE; MONOMER; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE PHOSPHODIESTERASE; PHOSPHOLIPID;

ALLOSTERISM; ARTICLE; BACILLUS CEREUS; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CURVE FITTING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE; HYDROPHOBICITY; KINETICS; NONHUMAN;

BACILLUS CEREUS; POSIBACTERIA;

EID: 0037960384     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0006-3495(03)70051-4     Document Type: Article

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