ID: | 2.6.1.83 | ||
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Description: | LL-diaminopimelate aminotransferase. | ||
Alternative Name: |
LL-diaminopimelate transaminase. LL-DAP-AT. LL-DAP aminotransferase. | ||
Prosite: | PDOC00098; | ||
PDB: |
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Cath: | 3.40.640.10; 3.90.1150.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.6.1.83 |
BRENDA Enzyme Link: | BRENDA 2.6.1.83 |
KEGG Enzyme Link: | KEGG2.6.1.83 |
BioCyc Enzyme Link: | BioCyc 2.6.1.83 |
ExPASy Enzyme Link: | ExPASy2.6.1.83 |
EC2PDB Enzyme Link: | EC2PDB 2.6.1.83 |
ExplorEnz Enzyme Link: | ExplorEnz 2.6.1.83 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.6.1.83 |
IntEnz Enzyme Link: | IntEnz 2.6.1.83 |
MEDLINE Enzyme Link: | MEDLINE 2.6.1.83 |
RHEA:23988 | 2-oxoglutarate + LL-2,6-diaminoheptanedioate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate |
RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].([*:5]-[CH;+0:6](-[*:7])-[NH2;+0:8].[*:9]-[NH2;+0:10])>>[*:5]-[C;H0;+0:6](-[*:7])=[N;H0;+0:10]-[*:9].[*:1]-[CH;+0:2](-[*:3])-[NH2;+0:8].[OH2;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Methanococci use the diaminopimelate aminotransferase (DapL) pathway for lysine biosynthesis. | Liu Y, White RH, Whitman WB | 2010 Jul | 20418392 |
Biochemical and phylogenetic characterization of a novel diaminopimelate biosynthesis pathway in prokaryotes identifies a diverged form of LL-diaminopimelate aminotransferase. | Hudson AO, Gilvarg C, Leustek T | 2008 May | 18310350 |
Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia. | Watanabe N, Cherney MM, van Belkum MJ, Marcus SL, Flegel MD, Clay MD, Deyholos MK, Vederas JC, James MN | 2007 Aug 17 | 17583737 |
L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine. | McCoy AJ, Adams NE, Hudson AO, Gilvarg C, Leustek T, Maurelli AT | 2006 Nov 21 | 17093042 |
An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants. | Hudson AO, Singh BK, Leustek T, Gilvarg C | 2006 Jan | 16361515 |