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・ L-Ribonucleic acid aptamer
・ L-ribulose-5-phosphate 3-epimerase
・ L-ribulose-5-phosphate 4-epimerase
・ L-Ron
・ L-saccharopine oxidase
・ L-selectin
・ L-selectride
・ L-series
・ L-serine ammonia-lyase
・ L-serine dehydratase
・ L-serine-phosphatidylethanolamine phosphatidyltransferase
・ L-seryl-tRNASec selenium transferase
・ L-Seven
・ L-shell
・ L(R)
L,L-diaminopimelate aminotransferase
・ L-1 Identity Solutions
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・ L-11 76.2 mm tank gun
・ L-13 Light Industrial Workshop
・ L-160
・ L-165041
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・ L-2-amino-4-chloropent-4-enoate dehydrochlorinase
・ L-2-hydroxycarboxylate dehydrogenase (NAD+)
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L,L-diaminopimelate aminotransferase : ウィキペディア英語版
L,L-diaminopimelate aminotransferase

In enzymology, a L,L-diaminopimelate aminotransferase () is an enzyme that catalyzes the chemical reaction
:LL-2,6-diaminoheptanedioate + 2-oxoglutarate \rightleftharpoons (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
Thus, the two substrates of this enzyme are LL-2,6-diaminoheptanedioate and 2-oxoglutarate, whereas its 3 products are (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, L-glutamate, and H2O.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase. Other names in common use include LL-diaminopimelate transaminase, LL-DAP aminotransferase, and LL-DAP-AT. This enzyme participates in lysine biosynthesis.
==Structural studies==

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .

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