1.4.1.B2: L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+)

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For detailed information about L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+), go to the full flat file.

Reaction

Synonyms

3,5-DAHDH, Kdd

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.B2 L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+)

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Results	in table
2	AA Sequence
2	Cloned(Commentary)
7	Cofactor
1	Crystallization (Commentary)
2	General Information
32	Inhibitors
12	Ki Value [mM]
14	KM Value [mM]
4	Metals/Ions
4	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
5	Organism
2	pH Optimum
3	pH Range
1	pH Stability
27	Protein Variants
2	Purification (Commentary)
1	Reaction
5	Reference
1	Specific Activity [micromol/min/mg]
3	Storage Stability
14	Substrates and Products (Substrate)
3	Subunits
2	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Range [°C]
4	Temperature Stability [°C]

Crystallization

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Crystallization on EC 1.4.1.B2 - L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+)

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structures of 3,5-DAHDH in apo form, complexed with cofactor NADPH, and of variant E310G/A314Y in complex with NADPH. The overall monomeric structure of 3,5-DAHDH is composed of an N-terminal catalytic domain (Domain I) and a C-terminal cofactor-binding domain (Domain II) separating by a deep cleft

Candidatus Cloacimonas acidaminovorans

B0VJ11

762604