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L,L-diaminopimelate aminotransferase activity

Known as: LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase activity, LL-DAP-AT activity, LL-diaminopimelate aminotransferase activity 
Catalysis of the reaction: 2-oxoglutarate + LL-2,6-diaminopimelate = (S)-2,3,4,5-tetrahydrodipicolinate + L-glutamate + H(2)O + H(+). [EC:2.6.1.83… Expand
National Institutes of Health

Papers overview

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2016
2016
A Gram-staining positive, non-motile, rod-shaped, catalase positive and oxidase negative bacterium, designated NCCP-1331T, was… Expand
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2012
2012
Recently, LL-diaminopimelate aminotransferase (LL-DAP-AT), a pyridoxal-5'-phosphate (PLP)-dependent enzyme, was reported to… Expand
2012
2012
 
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Review
2011
Review
2011
The enzymes involved in the lysine biosynthetic pathway have long been considered to be attractive targets for novel antibiotics… Expand
2010
2010
The pathway of lysine biosynthesis in the methanococci has not been identified previously. A variant of the diaminopimelic acid… Expand
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2008
2008
LL-Diaminopimelate aminotransferase (LL-DAP-AT), a pyridoxal phosphate (PLP)-dependent enzyme in the lysine biosynthetic pathways… Expand
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2007
2007
The essential biosynthetic pathway to l-Lysine in bacteria and plants is an attractive target for the development of new… Expand
Highly Cited
2005
Highly Cited
2005
Although lysine (Lys) biosynthesis in plants is known to occur by way of a pathway that utilizes diaminopimelic acid (DAP) as a… Expand
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Highly Cited
1988
Highly Cited
1988
Recently a dapF mutant of Escherichia coli lacking the diaminopimelate epimerase was found to have an unusual large LL… Expand
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