1.4.1.16: diaminopimelate dehydrogenase
This is an abbreviated version!
For detailed information about diaminopimelate dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.16
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1.4.1.16
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glutamicum
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corynebacterium
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d-amino
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deamination
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thermophilum
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symbiobacterium
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l-lysine
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dihydrodipicolinate
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2-keto
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thermosphaericus
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ureibacillus
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isoxazoline
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homoserine
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sphaericus
-
synthesis
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biotechnology
- 1.4.1.16
- glutamicum
- corynebacterium
-
d-amino
-
deamination
- thermophilum
- symbiobacterium
- l-lysine
- dihydrodipicolinate
-
2-keto
- thermosphaericus
-
ureibacillus
-
isoxazoline
- homoserine
- sphaericus
- synthesis
- biotechnology
Reaction
Synonyms
BAB07799, BF3690, DAPDH, DDH, meso-2,6-diaminopimelate dehydrogenase, meso-alpha,epsilon-diaminopimelate dehydrogenase, meso-DAPDH, meso-diaminopimelate dehydrogenase, NADP+-dependent meso-diaminopimelate dehydrogenase, Sth1425, Theth_1310
ECTree
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Crystallization
Crystallization on EC 1.4.1.16 - diaminopimelate dehydrogenase
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apo form and in complex with meso-diaminopimelate, D-leucine, and 4-methyl-2-oxopentanoic acid, sitting drop vapor diffusion method, using MES (0.1 M, pH 6.0), 15% (w/v) PEG 20000, and 5% (v/v) glycerol
crystallization in the presence of NADP+, only monoclinic crystals are suitable for X-ray diffraction, 2.2 A resolution
crystals of the ternary complex formed from the enzyme, NADP+ and the inhibitor (2S,5S)-2-amino-3(3-carboxy-2-isoxazolin-5-yl)propanoic acid
crystals of the ternary complex formed from the enzyme, NADP+ and the inhibitor L-2-amino-6-methylene-pimelate, 2.1 A resolution
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enzyme-NADP+ complex, hanging drop vapour diffusion, crystals of maximum dimensions of 0.05 x 0.05 x 0.5 mm are observed in 1 M ammonium sulfate, 1.2 M lithium sulfate, 100 mM HEPES, pH 7.5, crystals of dimensions 0.3 x 0.05 x 0.5 mm are obtained from 13-17% polyethylene glycol 8000 in 100 mM sodium cacodylate, pH 6.5 and 150-300 mM Mg(OAc)2
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apo form and in complex with NADP+ and both NADPH and meso-2,6-diaminoheptanedioate, sitting drop vapor diffusion method, using 0.1m HEPES buffer (pH 7.5) with 30% 2-methyl-2,4-pentanediol and 5% (v/v) glycerol
molecular docking of substrates meso-DAP and pyruvic acid to wild-type and mutant R71A. Substrate binding with meso-DAP or pyruvic acid changes the rigidity of the enzyme and the secondary structure around R71
apo form and in complex with NADP+ and N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid, sitting drop vapor diffusion method, using 1.9 M ammonium sulfate,0.1 M Tris-HCl pH 7.5