1.5.1.8: saccharopine dehydrogenase (NADP+, L-lysine-forming)

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For detailed information about saccharopine dehydrogenase (NADP+, L-lysine-forming), go to the full flat file.

Word Map on EC 1.5.1.8

1.5.1.8

alpha-aminoadipate

hyperlysinemia

pipecolic

dihydrodipicolinate

aminoadipic

homocitrate

medicine

Reaction

Synonyms

AasS, dehydrogenase, saccharopine (nicotinamide adenine dinucleotide phosphate, lysine-forming), L-lysine-alpha-ketoglutarate reductase, LKR, LKR/SDH, LOR, LOR-SDH, lysine 2-oxoglutarate reductase, lysine 2-oxoglutarate reductase-saccharopine dehydrogenase, lysine alpha-ketoglutarate reductase, lysine ketoglutarate reductase, lysine ketoglutarate/reductase saccharopine dehydrogenase, lysine-2-oxoglutarate reductase, lysine-alpha-ketoglutarate reductase, lysine-ketoglutarate reductase, lysine-ketoglutarate reductase/saccharopine dehydrogenase, lysine-ketoglutaric reductase, lysine:alpha-ketoglutarate:TPNH oxidoreductase (epsilon-N-[glutaryl-2]-L-lysine forming), nllkr/sdh, saccharopine (nicotinamide adenine dinucleotide phosphate, lysine-forming) dehydrogenase, saccharopine dehydrogenase, saccharopine dehydrogenase (NADP, lysine-forming), saccharopine dehydrogenase (nicotinamide adenine dinucleotide phosphate, lysine-forming)

ECTree

1 Oxidoreductases

1.5 Acting on the CH-NH group of donors

1.5.1 With NAD⁺ or NADP⁺ as acceptor

1.5.1.8 saccharopine dehydrogenase (NADP+, L-lysine-forming)

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Results	in table
16	Activating Compound
73	AA Sequence
5	Application
1	CAS Registry Number
9	Cloned(Commentary)
67	Cofactor
39	Disease/ Diagnostics
6	Expression
19	General Information
8	General Stability
41	Inhibitors
1	Ki Value [mM]
19	KM Value [mM]
30	Localization
17	Metals/Ions
18	Molecular Weight [Da]
65	Natural Substrates/ Products (Substrates)
234	Organism
6	Pathway
17	PDB ID
14	pH Optimum
3	pH Range
3	pH Stability
6	Posttranslational Modification
4	Protein Variants
20	Purification (Commentary)
4	Reaction
3	Reaction Type
61	Reference
86	Source Tissue
27	Specific Activity [micromol/min/mg]
6	Storage Stability
178	Substrates and Products (Substrate)
19	Subunits
55	Synonyms
1	Systematic Name
19	Temperature Optimum [°C]
1	Temperature Stability [°C]
1	Turnover Number [1/s]

Molecular Weight

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Molecular Weight on EC 1.5.1.8 - saccharopine dehydrogenase (NADP+, L-lysine-forming)

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115000

2 entries

117000

Arabidopsis thaliana

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

392372, 392375

123000

Glycine max

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

392374

125000

Zea mays

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

392369

190000

Phaseolus vulgaris

bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase, gel filtration

654174

202000

Oryza sativa

non-denaturing PAGE, bifunctional protein containing lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, one band represents the holoenzyme and shows higher enzyme activities compared to a second band of 396 kDa with much lower enzyme activities indicating a multimeric structure

392370

203000

Oryza sativa

gel filtration, bifunctional protein containing lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities

230000

gel filtration

256000

gel filtration, bifunctional protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities

392374

260000

Zea mays

bifunctional enzyme with lysine-oxoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities, but domains are functionally independent of each other

392369

420000

Bos taurus

sedimentation equilibrium method, single protein with lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9 activities: aminoadipic semialdehyde synthase, but reductase and dehydrogenase domains are separately folded and functionally independent of each other

392365

467000

Papio sp.

gel filtration, single protein catalyzes both lysine-ketoglutarate reductase reaction EC 1.5.1.8 and saccharopine dehydrogenase reaction EC 1.5.1.9, bifunctional enzyme: aminoadipic semialdehyde synthase

468000

480000

gel filtration, no separation of L-lysine-ketoglutarate reductase EC 1.5.1.8 and saccharopine dehydrogenase EC 1.5.1.9

392360

52000

Rattus norvegicus

4 * 52000, enzyme clearly separated from saccharopine dehydrogenase EC 1.5.1.9, SDS-PAGE

392359