Linked Life Data

1473108

Source:http://linkedlifedata.com/resource/pubmed/id/1473108

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1993-2-3
pubmed:abstractText
The mechanism of action of the specific D-galacturonan digalacturonohydrolase [poly-(1----4)-alpha-D-galactosiduronate digalacturonohydrolase, EC 3.2.1.82] of Selenomonas ruminantium was investigated by using reducing-end [1-3H]-labeled oligogalactosiduronates having degree of polymerization 3-5 as the substrates. The reaction products, incorporation and distribution of radioactivity in products, and the frequency of oligogalactosiduronate bond-cleavage were quantitatively estimated as functions of the substrate concentration. An alternative cleavage of tri(D-galactosiduronate) occurred during the enzyme reaction, indicating the participation of some bimolecular mechanism in addition to unimolecular hydrolysis in the action of the enzyme. Unimolecular hydrolysis takes place at low initial concentration of the substrate. The shifted termolecular enzyme-substrate complex formation and the subsequent galactosyluronic transfer is the predominant mechanism in degradation of tri(D-galactosiduronate) at high concentration. Tetra(D-galactosiduronate) and penta(D-galactosiduronate) are degraded by unimolecular hydrolysis at low, as well as high concentration of the substrate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0008-6215
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
235
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
269-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Mechanism of action of D-galacturonan digalacturonohydrolase of Selenomonas ruminantium on oligogalactosiduronic acids.
pubmed:affiliation
Institute of Chemistry, Slovak Academy of Sciences, Czechoslovakia.
pubmed:publicationType
Journal Article