1.4.1.18: lysine 6-dehydrogenase
This is an abbreviated version!
For detailed information about lysine 6-dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.18
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1.4.1.18
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deamination
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tumefaciens
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agrobacterium
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saccharopine
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5-carboxylate
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corynebacterium
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pomeroyi
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non-proteinogenic
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silicibacter
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nad-dependent
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glutamicum
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pyrroline
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l-pipecolic
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tetramer
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albicans
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analysis
- 1.4.1.18
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deamination
- tumefaciens
-
agrobacterium
- saccharopine
-
5-carboxylate
-
corynebacterium
- pomeroyi
-
non-proteinogenic
-
silicibacter
-
nad-dependent
- glutamicum
-
pyrroline
-
l-pipecolic
- tetramer
- albicans
- analysis
Reaction
Synonyms
L-lysine 6-dehydrogenase, L-lysine 6-dehydrogenase (deaminating), L-lysine epsilon-dehydrogenase, Lys 6-DH, LysDH, lysine 6-dehydrogenase
ECTree
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Subunits
Subunits on EC 1.4.1.18 - lysine 6-dehydrogenase
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dimer
hexamer
6 * 40000 Da, gel filtration, enzyme elutes as a hexamer when a high concentration of L-lysine (10 mM) is supplemented to both the enzyme and the elution buffer
tetramer
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gel filtration and centrifugation in presence of L-lysine
additional information
dimer
2 * 42600, recombinant enzyme, SDS-PAGE, 2 * 42089, amino acid sequence
dimer
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2 * 42600, recombinant enzyme, SDS-PAGE, 2 * 42089, amino acid sequence
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each monomer consists of a Rossmann fold domain and a C-terminal catalytic domain, and the fold of the catalytic domain showed similarity to that of saccharopine reductase, three-dimensional structure of the enzyme, structure comparisons, overview. Subunit A active site contains a sulfate ion not seen in subunit B. Consequently, subunit A adopts a closed conformation, whereas subunit B adopts an open one. In each subunit, one NAD molecule was bound to the active site in an anti-conformation, indicating that the enzyme makes use of pro-R-specific hydride transfer between the two hydrides at C-4 of NADH with type A specificity
additional information
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each monomer consists of a Rossmann fold domain and a C-terminal catalytic domain, and the fold of the catalytic domain showed similarity to that of saccharopine reductase, three-dimensional structure of the enzyme, structure comparisons, overview. Subunit A active site contains a sulfate ion not seen in subunit B. Consequently, subunit A adopts a closed conformation, whereas subunit B adopts an open one. In each subunit, one NAD molecule was bound to the active site in an anti-conformation, indicating that the enzyme makes use of pro-R-specific hydride transfer between the two hydrides at C-4 of NADH with type A specificity
additional information
-
each monomer consists of a Rossmann fold domain and a C-terminal catalytic domain, and the fold of the catalytic domain showed similarity to that of saccharopine reductase, three-dimensional structure of the enzyme, structure comparisons, overview. Subunit A active site contains a sulfate ion not seen in subunit B. Consequently, subunit A adopts a closed conformation, whereas subunit B adopts an open one. In each subunit, one NAD molecule was bound to the active site in an anti-conformation, indicating that the enzyme makes use of pro-R-specific hydride transfer between the two hydrides at C-4 of NADH with type A specificity
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