Linked Life Data

1524589

Source:http://linkedlifedata.com/resource/pubmed/id/1524589

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-10-13
pubmed:abstractText
Ligninases (lignin peroxidases) are heme-containing peroxidases excreted by some white-rot fungi as components of their lignolytic multienzyme complexes. These peroxidases functioning at rather acidic media catalyze oxidative cleavage of both synthetic non-phenolic lignin models and many other oxidation-proof compounds (chloroorganic pesticides, carcinogenic hydrocarbons, etc.). Data on the ligninase structure and functions not only shed light of the lignin biodegradation but also open new perspectives in peroxidation chemistry and biotechnology. Many aspects of ligninase catalytic mechanism can be understood in comparative studies of congruent chemical reactions, e.g., peroxidisulfate-supported oxidation, as well as of ligninase-like activity of some plant and animal peroxidases which is also manifested at low pH. Ligninases are not only more powerful oxidative agents than other peroxidases, but also, in contrast to latters, appear to be able to control the contributions of C-C and C-O bond splitting in primary radical-cations of substrates. The contribution of the oxidative-hydrolytic dealkylation of radical cations can be considered as one of classification criteria for lignolytic enzymes.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0132-3423
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
309-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
[Lignin and ligninase].
pubmed:publicationType
Journal Article, English Abstract, Review