Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.6.1.83: LL-diaminopimelate aminotransferase

This is an abbreviated version!
For detailed information about LL-diaminopimelate aminotransferase, go to the full flat file.

Word Map on EC 2.6.1.83

Reaction

LL-2,6-Diaminoheptanedioate
+
2-oxoglutarate
=
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
 +
L-glutamate
 +
H2O

Synonyms

Ald1, aq_273, AtDAP-AT, Ava_1277, Ava_2354, BF2666, CT390, CtDAP-AT, Cthe_0816, DAP, DapI, DapL, Dhaf_1761, diaminopimelate aminotransferase, glr4108, GSU0162, L,L-diaminopimelate aminotransferase, LIC12841, LL-DAP aminotransferase, LL-DAP-AT, LL-DAPAT, LL-diaminopimelate aminotransferase, MA1712, Moth_0889, Msp_0924, MTH52, pc0685, Sfum_0054, sll0480, VsDapL

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.83 LL-diaminopimelate aminotransferase

Crystallization

Crystallization on EC 2.6.1.83 - LL-diaminopimelate aminotransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method at room temperature, 1.95 A resolution. The structure of AtDAP-AT is determined using the multiple-wavelength anomalous dispersion method with a seleno-methionine derivative
in complex with N-(5'-phosphopyridoxyl)-L-glutamate and N-(5'-phosphopyridoxyl)-LL-diaminopimelate, hanging drop vapor diffusion method, using 45% (w/v) (NH4)2SO4, 0.1 M HEPES pH 7.5, 3% (w/v) PEG400
to 2.3 A resolution. The large donain (Pro85–Ser338) consists of 254 residues and has an alpha-beta-alpha sandwich fold. The large domain includes both the pyridoxal phosphate-binding site and the dimerization site. The small domain is composed of the remaining residues, Gly34–Ile84 and Ser339–Thr441. The small domain has an alpha/beta architecture, with a beta-sheet surrounded by two outer layers alpha-helices
sitting-drop vapor diffusion methodPEG 6000
modeling of structure based on the structure of the Arabidopsis thaliana enzyme and comparison between strucutre of Arabidopsis thaliana, from Leptospira interrogans, Verrucomicrobium spinosum and Chlamydomonas reinhardtii enzymes
PEG 3350, sitting drop method
sitting-drop vapour-diffusion method, PEG 3350
-
modeling of structure based on the structure of the Arabidopsis thaliana enzyme and comparison between strucutre of Arabidopsis thaliana, from Leptospira interrogans, Verrucomicrobium spinosum and Chlamydomonas reinhardtii enzymes
purified recombinant enzyme in presence of malic acid, hanging drop vapor diffusion method, mixing of 200 nl of a protein/inhibitor solution containing 39 mg/ml protein in 100 mM HEPES-KOH, 20 mM NaCl, 1 mM DTT, pH 7.6, and 200 mM malic acid, with 200 nl of reservoir solution containing 60% v/v T-mate, pH 7.0, 20°C, 8 weeks, X-ray diffraction structure determination and analysis at 2.25 A resolution, molecular replacement using the crystal structure of Chlamydomonas reinhardtii LL-diaminopimelate aminotransferase (PDB ID 3QGU) as search model, model building