Linked Life Data

10380338

Source:http://linkedlifedata.com/resource/pubmed/id/10380338

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-7-26
pubmed:abstractText
4-alpha-Glucanotransferase (GTase, D-enzyme) catalyzes disproportionation between two short polymers of maltooligosaccharides linked by alpha-1,4-glucoside bonds. Using action modes of the potato GTase for the donor and acceptor substrates, the Monte Carlo method was applied to simulate the GTase reaction. The simulation starts from a single enzyme molecule and a finite number (10(5)) of substrate molecules. All selection processes were performed using random numbers produced by computer. The initial substrates were from trimer to 10-mer. In every case, the final stage was the steady-state distribution of polymers. The steady-state distribution by the potato GTase reaction was different from those by the hypothetical random disproportionation reaction. The simulated data from the reaction of potato GTase and trimer almost quantitatively agreed with experimental data. The mechanism of the GTase reaction was accumulation of probabilistic processes and was well simulated by the Monte Carlo method. GTase randomizes the overall distribution of chain length of the substrate. Therefore the GTase reaction is an entropy-driven process.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3525
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
145-51
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Monte Carlo simulation of 4-alpha-glucanotransferase reaction.
pubmed:affiliation
Faculty of Agriculture, Kyoto University, Japan.
pubmed:publicationType
Journal Article