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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0035647,
umls-concept:C0185117,
umls-concept:C0205474,
umls-concept:C0220841,
umls-concept:C0244104,
umls-concept:C0542341,
umls-concept:C1450780,
umls-concept:C1657244,
umls-concept:C1880022,
umls-concept:C2911684
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pubmed:issue |
6
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pubmed:dateCreated |
2009-4-23
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pubmed:abstractText |
Gamma-aminobutyrate transaminase (GABA-T) catalyses the breakdown of GABA to succinic semialdehyde. In this report, the previously identified Arabidopsis thaliana (L.) Heyhn GABA-T (AtGABA-T) was characterized in more detail. Full-length AtGABA-T contains an N-terminal 36 amino acid long targeting pre-sequence (36 amino acids) that is both sufficient and necessary for targeting the enzyme to mitochondria. Removal of the pre-sequence encoding this N-terminal targeting domain and co-expression of the resulting truncated AtGABA-T cDNA with the GroES/EL molecular chaperone complex in Escherichia coli yielded good recovery of the soluble recombinant proteins. Activity assays indicated that purified recombinant GABA-T has both pyruvate- and glyoxylate-dependent activities, but cannot utilize 2-oxoglutarate as amino acceptor. Kinetic parameters for glyoxylate- and pyruvate-dependent GABA-T activities were similar, with physiologically relevant affinities. Assays of GABA-T activity in cell-free leaf extracts from wild-type Arabidopsis and two knockout mutants in different genetic backgrounds confirmed that the native enzyme possesses both pyruvate- and glyoxylate-dependent activities. The GABA-T transcript was present throughout the plant, but its expression was highest in roots and increased as a function of leaf development. A GABA-T with dual functions suggests the potential for interaction between GABA metabolism and photorespiratory glyoxylate production.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19264755-10517851,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19264755-7971954,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19264755-9738973
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1460-2431
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1743-57
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pubmed:dateRevised |
2010-9-23
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pubmed:meshHeading |
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pubmed:year |
2009
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pubmed:articleTitle |
Biochemical characterization, mitochondrial localization, expression, and potential functions for an Arabidopsis gamma-aminobutyrate transaminase that utilizes both pyruvate and glyoxylate.
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pubmed:affiliation |
Department of Plant Agriculture, University of Guelph, Guelph, Ontario, Canada.
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pubmed:publicationType |
Journal Article
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