Linked Life Data

1483038

Source:http://linkedlifedata.com/resource/pubmed/id/1483038

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-2-12
pubmed:abstractText
The characterization of human selenocysteine lyase, an enzyme that specifically catalyzes the decomposition of L-selenocysteine to L-alanine and hydrogen selenide, is described. The enzyme is the first described that acts exclusively on a selenium compound. The enzyme from human tissues, analogous to that from pig tissues and bacteria, requires pyridoxal 5-phosphate as a cofactor. L-selenocysteine is the sole substrate with a Km = 0.50 mM. L-cysteine is a noncompetitive inhibitor of the enzyme with a Ki = 5.85 mM. The following amino acids and purines are inert: L-cysteine, selenocystamine, seleno-DL-methionine, 6-selenopurine, and 6-selenoguanosine. The enzyme was found in liver, kidney, heart, adrenal and muscle in decreasing order of specific activity. The enzyme activity in liver was found not to be related to tissue selenium concentration or glutathione peroxidase activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0931-2838
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
189-94
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Characterization of selenocysteine lyase in human tissues and its relationship to tissue selenium concentrations.
pubmed:affiliation
Department of Chemistry, Cleveland State University, Ohio 44115.
pubmed:publicationType
Journal Article