Linked Life Data

20836890

Source:http://linkedlifedata.com/resource/pubmed/id/20836890

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-9-24
pubmed:abstractText
Phosphoenolpyruvate carboxylase (PEPC) is a critical enzyme catalyzing the ?-carboxylation of phosphoenolpyruvate (PEP) to oxaloacetate, a tricarboxylic acid (TCA) cycle intermediate. PEPC typically exists as a Class-1 PEPC homotetramer composed of plant-type PEPC (PTPC) polypeptides, and two of the subunits were reported to be monoubiquitinated in germinating castor oil seeds. By the large-scale purification of ubiquitin (Ub)-related proteins from lily anther, two types of PEPCs, bacterial-type PEPC (BTPC) and plant-type PEPC (PTPC), were identified in our study as candidate Ub-related proteins. Until now, there has been no information about the properties of the PEPCs expressed in male reproductive tissues of higher plants.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1471-2229
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
200
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Characterization of bacterial-type phosphoenolpyruvate carboxylase expressed in male gametophyte of higher plants.
pubmed:affiliation
The Plant Science Education Unit, The Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma, Nara 630-0101, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't