Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1976-4-30
pubmed:abstractText
Simple kinetic considerations derived from the ping-pong mechanism previously proposed for levansucrase of Bacillus subtillis allowed us to predict an easily operated method to approach the kinetic studies of exchange and hydrolytic activities of this enzyme. The experimental kinetic pattern obtained from the study of both activities is in close agreement with those predicted by theoretical approach. The combination of kinetic results enabled us to determine with a good accuracy the values of the apparent rate constant of the step of fructosylation of the enzyme from the sucrose-enzyme Michaelis complex and the apparent rate constants of the steps of defructosylation of the fructosyl enzyme to water or to glucose. The standard free energy reaction coordinate diagram for the transfructosylation process from sucrose to water was constructed. We found that the high energy of the glycosidic linkage of sucrose is preserved in the fructosyl-enzyme intermediate. The temperature dependence studies of the rate constants of fructosylation and defructosylation of the enzyme show that the entropy of activation for the two steps of defructosylation of the fructosyl enzyme are nearly the same. However the enthalpy of activation for the transfructosylation step to water is greater than that to glucose. We attempted to explain this discrepancy. Furthermore comparison of mechanism and efficiency of enzymatic and acid catalysis of sucrose hydrolysis was developed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
55-64
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Levansucrase of Bacillus subtilis: kinetic and thermodynamic aspects of transfructosylation processes.
pubmed:publicationType
Journal Article