Linked Life Data

2939644

Source:http://linkedlifedata.com/resource/pubmed/id/2939644

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1986-6-2
pubmed:abstractText
A stable activity which transfers the amino group from glutamate to prephenate was extracted from 4-day old etiolated shoots of sorghum. The activity was retained on DEAE cellulose and eluted as a single peak. Prephenate aminotransferase co-eluted with a very abundant alpha-ketoglutarate: aspartate aminotransferase, but heating at 70 degrees C resulted in loss of alpha-ketoglutarate: aspartate activity with nearly full retention of prephenate: glutamate aminotransferase activity. The heated enzyme displayed high affinity and specificity for prephenate. Among 7 donors tested, only glutamate, and aspartate at less than 20% the rate with glutamate, supported prephenate aminotransferase activity. In the reverse direction, a reaction rate comparable to that in the forward direction was unchanged as the concentration of alpha-ketoglutarate was reduced from 1.0 to 0.09 mM. The apparent Km for arogenate was 0.8 mM. The forward reaction was unaffected by the inclusion of tyrosine, phenylalanine or tryptophan. Together with the discovery of arogenate dehydrogenase in sorghum [3], these data indicate that, in the sorghum plant, tyrosine derives from prephenate by transamination and aromatization, rather than the reverse sequence.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0939-5075
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
79-86
pubmed:dateRevised
2009-11-4
pubmed:meshHeading
pubmed:articleTitle
Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.