Linked Life Data

16487061

Source:http://linkedlifedata.com/resource/pubmed/id/16487061

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2006-2-20
pubmed:abstractText
Alanine is the most effective precursor for gluconeogenesis among amino acids, and the initial reaction is catalyzed by alanine aminotransferase (AlaAT). Although the enzyme activity increases during fasting, this effect has not been studied extensively. The present study describes the purification and characterization of an isoform of AlaAT from rat liver under fasting. The molecular mass of the enzyme is 17.7 kD with an isoelectric point of 4.2; glutamine is the N-terminal residue. The enzyme showed narrow substrate specificity for L-alanine with Km values for alanine of 0.51 mM and for 2-oxoglutarate of 0.12 mM. The enzyme is a glycoprotein. Spectroscopic and inhibition studies showed that pyridoxal phosphate (PLP) and free -SH groups are involved in the enzymatic catalysis. PLP activated the enzyme with a Km of 0.057 mM.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0006-2979
pubmed:author
pubmed:issnType
Print
pubmed:volume
71 Suppl 1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
S105-12
pubmed:dateRevised
2011-1-5
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
A novel low molecular weight alanine aminotransferase from fasted rat liver.
pubmed:affiliation
Department of Biochemistry, University of Mysore, Manasagangotri, Mysore 570006, India.
pubmed:publicationType
Journal Article, Retracted Publication