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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1982-9-24
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pubmed:abstractText |
Steady-state kinetic studies were made on the very efficient enzyme hydrolysis of acetylthiocholine by electric eel acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) in glycerol/water solvents of increased viscosity. Determinations of the very fast minimum substrate association rate constants kmin, (2 . 10(8) M-1 . s-1 at I approximately 0.1 M and 25 degrees C) from the Michaelis parameters, V/(Km[E0]), were made at low substrate concentrations in order to obtain kmin directly. kmin was shown to be strongly dependent upon viscosity, which is characteristic of a diffusion-controlled reaction. kmin is as large or larger than plausible models for a simple diffusion-controlled reaction between a charged enzyme and substrate would suggest. Enhancement of the diffusion-controlled reaction through nonspecific binding of substrate to the highly negatively charged acetylcholinesterase followed by two-dimensional surface diffusion in a random walk to the active site may be a factor in this enzyme mechanism. Evidence for this comes from the viscosity dependence of kmin. Using the surface diffusion model it is estimated that the binding-site target area on acetylcholinesterase is effectively increased a minimum of 8-fold.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholinesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Acetylthiocholine,
http://linkedlifedata.com/resource/pubmed/chemical/Choline,
http://linkedlifedata.com/resource/pubmed/chemical/Glycerol,
http://linkedlifedata.com/resource/pubmed/chemical/Solvents,
http://linkedlifedata.com/resource/pubmed/chemical/Water
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
704
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
52-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7093289-Acetylcholinesterase,
pubmed-meshheading:7093289-Acetylthiocholine,
pubmed-meshheading:7093289-Animals,
pubmed-meshheading:7093289-Choline,
pubmed-meshheading:7093289-Electrophorus,
pubmed-meshheading:7093289-Glycerol,
pubmed-meshheading:7093289-Kinetics,
pubmed-meshheading:7093289-Solvents,
pubmed-meshheading:7093289-Temperature,
pubmed-meshheading:7093289-Viscosity,
pubmed-meshheading:7093289-Water
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pubmed:year |
1982
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pubmed:articleTitle |
Kinetics of acetylthiocholine binding to electric eel acetylcholinesterase in glycerol/water solvents of increased viscosity. Evidence for a diffusion-controlled reaction.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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