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x * 117000, bifunctional protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, calculated from cDNA sequence
homodimer
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2 * 123000, bifunctional protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, additional 100 kDa band is a proteolytic cleavage product, SDS-PAGE
homodimer
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2 * 125000, bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, digestion with elastase separates the functional domains into a 65 kDa polypeptide with LOR activity and a 57 kDa polypeptide with SDH activity, SDS-PAGE
homotetramer
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limited proteolysis of aminoadipic semialdehyde synthase results in two fragments: 62700 with lysine-ketoglutarate reductase activity and 49200 with saccharopine dehydrogenase activity
homotetramer
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4 * 115000, single protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, SDS-PAGE
homotetramer
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4 * 115000, single protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, SDS-PAGE
homotetramer
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4 * 52000, enzyme clearly separated from saccharopine dehydrogenase EC 1.5.1.9, SDS-PAGE
homotetramer
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4 * 52000, enzyme clearly separated from saccharopine dehydrogenase EC 1.5.1.9, SDS-PAGE
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additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain
additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain
additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide
additional information
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369 kDa band may represent a dimeric or tetrameric molecule, multimeric form results from the association of the 202 kDa LOR/SDH band
additional information
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain
additional information
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369 kDa band may represent a dimeric or tetrameric molecule, multimeric form results from the association of the 202 kDa LOR/SDH band
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additional information
A0A3L6FCN0
the enzyme domains and activities LKR and SDH belong to a single about 120 kDa bifunctional polypeptide. In plants, the LKR and SDH domains of the bifunctional polypeptide are separated from each other by an about 130 amino acid interdomain