Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1980-11-24
pubmed:abstractText
When beta-glucosidase from sweet almonds reacts with p-nitrophenyl-beta-D-glucoside at subzero temperatures, a rapid release of p-nitrophenol, stoichiometric with enzyme concentration, occurs prior to turnover. This observation is interpreted as reflecting rapid formation of a glucose-enzyme intermediate, followed by rate-limiting breakdown. The energies of activation for the formation and breakdown of the intermediate were 6.0 +/- 2 and 19.0 +/- 2 kcal mol-1, respectively. Extrapolation of the reaction rates to higher temperatures suggests an isokinetic temperature circa 24 degrees C. Measurement of kcat in aqueous solution as a function of temperature yields a breakpoint in the Arrhenius plot at 20 degrees C and activation energies above and below this point which correspond to the values at subzero temperatures (6.7 and 17.0 kcal mol-1, respectively). This breakpoint thus reflects a change in the rate-determining step from formation of the intermediate at higher temperatures to breakdown at lower values, and explains why a "burst" of p-nitrophenol is observed at low, but not high, temperatures with this substrate. The significance of this finding to other glycohydrolases, and enzyme catalysis in general, is considered.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
255
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9030-2
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Temperature-dependent change in the rate-limiting step of beta-glucosidase catalysis.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.