1.4.1.16: diaminopimelate dehydrogenase

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For detailed information about diaminopimelate dehydrogenase, go to the full flat file.

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

     1 Oxidoreductases

         1.4 Acting on the CH-NH₂ group of donors

             1.4.1 With NAD⁺ or NADP⁺ as acceptor

                1.4.1.16 diaminopimelate dehydrogenase

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Results	in table
3529	AA Sequence
4	Application
1	CAS Registry Number
20	Cloned(Commentary)
84	Cofactor
8	Crystallization (Commentary)
4	General Information
5	IC50 Value
77	Inhibitors
77	kcat/KM [mM/s]
10	Ki Value [mM]
133	KM Value [mM]
1	Metals/Ions
15	Molecular Weight [Da]
49	Natural Substrates/ Products (Substrates)
120	Organism
6	Pathway
38	PDB ID
21	pH Optimum
3	pH Range
4	pH Stability
52	Protein Variants
18	Purification (Commentary)
5	Reaction
3	Reaction Type
111	Reference
34	Specific Activity [micromol/min/mg]
5	Storage Stability
211	Substrates and Products (Substrate)
17	Subunits
42	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
12	Temperature Stability [°C]
102	Turnover Number [1/s]

Application

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Application on EC 1.4.1.16 - diaminopimelate dehydrogenase

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

biotechnology

Symbiobacterium thermophilum

Q67PI3

high thermostability and relaxed substrate profile of Symbiobacterium thermophilum meso-DAPDH warrant it as an excellent starting enzyme for creating effective D-amino acid dehydrogenases by protein engineering

724026

synthesis

3 entries

synthesis

Symbiobacterium thermophilum

Q67PI3

expression of DapDH in Escherichia coli significantly enhances carbon flux into the pentose phosphate pathway and L-lysine biosynthetic pathway, thus increasing the levels of NADPH and precursors for L-lysine biosynthesis. The coexistence of two DAP-pathways and sufficient ammonium availability are good for increasing the final titer of L-lysine with a high carbon yield and productivity in Escherichia coli. Fed-batch fermentation of the target strain results in 119.5 g/l of L-lysine with a carbon yield of 49.1% and productivity of 2.99 g per l and h

763734

synthesis

Pseudothermotoga thermarum

F7YTT4

individual overexpression of ASPDH, aspartate-semialdehyde dehydrogenase from Tistrella mobilis, dihydrodipicolinate reductase from Escherichia coli, and diaminopimelate dehydrogenase from Pseudothermotoga thermarum in Corynebacterium glutamicum LC298, a basic lysine producer, increases the production of lysine by 30.7%, 32.4%, 17.4%, and 36.8%, respectively. The highest increase of lysine production (30.7%) is observed for a triple-mutant strain (27.7 g/L, 0.35 g/g glucose) expressing ASPDH, aspartate-semialdehyde dehydrogenase from Tistrella mobilis, dihydrodipicolinate reductase from Escherichia coli. A quadruple-mutant strain expressing all of the four NADH-utilizing enzymes allows high lysine production (24.1 g/l, 0.30 g/g glucose) almost independent of the oxidative pentose phosphate pathway

763424

synthesis

Pseudothermotoga thermarum DSM 5069

-

individual overexpression of ASPDH, aspartate-semialdehyde dehydrogenase from Tistrella mobilis, dihydrodipicolinate reductase from Escherichia coli, and diaminopimelate dehydrogenase from Pseudothermotoga thermarum in Corynebacterium glutamicum LC298, a basic lysine producer, increases the production of lysine by 30.7%, 32.4%, 17.4%, and 36.8%, respectively. The highest increase of lysine production (30.7%) is observed for a triple-mutant strain (27.7 g/L, 0.35 g/g glucose) expressing ASPDH, aspartate-semialdehyde dehydrogenase from Tistrella mobilis, dihydrodipicolinate reductase from Escherichia coli. A quadruple-mutant strain expressing all of the four NADH-utilizing enzymes allows high lysine production (24.1 g/l, 0.30 g/g glucose) almost independent of the oxidative pentose phosphate pathway

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