Linked Life Data

16859404

Source:http://linkedlifedata.com/resource/pubmed/id/16859404

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-7-24
pubmed:abstractText
The amine oxidases of mammalian tissues are a heterogeneous family of enzymes that metabolise various monoamines, diamines and polyamines produced endogenously, or being absorbed as dietary or xenobiotic substances. The heterogeneous class of amine oxidases can be divided on an arbitrary basis of the chemical nature of their cofactors into two types. Monoamine oxidase (MAO) and an intracellular form of polyamine oxidase (PAO) contain flavin adenine dinucleotide (FAD) as their cofactor, whereas a second group of amine oxidases without FAD contain a cofactor possessing one or more carbonyl groups, making them sensitive to inhibition by carbonyl reagents such as semicarbazide; this group includes semicarbazide-sensitive amine oxidase (SSAO) and the connective tissue enzyme, lysyl oxidase. This article focuses on the general aspects of MAO's contribution to the metabolism of foreign toxic substances including toxins and illegal drugs. Another main objective of this review is to discuss the properties of PAO and SSAO and their involvement in the metabolism of xenobiotics.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1742-5255
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
559-71
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
The role of amine oxidases in xenobiotic metabolism.
pubmed:affiliation
University of Texas Medical Branch at Galveston, Department of Pathology, 77555, USA.
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Extramural