1.1.1.387: L-serine 3-dehydrogenase (NAD+)

This is an abbreviated version!
For detailed information about L-serine 3-dehydrogenase (NAD+), go to the full flat file.

L-SerDH, L-serine 3-dehydrogenase, L-serine dehydrogenase, NAD+-dependent L-serine dehydrogenase, PA0743

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Results	in table
1	Activating Compound
1	AA Sequence
2	Cloned(Commentary)
7	Cofactor
2	Crystallization (Commentary)
3	General Information
6	Inhibitors
9	kcat/KM [mM/s]
17	KM Value [mM]
1	Metals/Ions
1	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
2	Organism
2	pH Optimum
9	Protein Variants
2	Purification (Commentary)
6	Reaction
2	Reference
1	Specific Activity [micromol/min/mg]
14	Substrates and Products (Substrate)
1	Subunits
5	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Stability [°C]
9	Turnover Number [1/s]

Reference on EC 1.1.1.387 - L-serine 3-dehydrogenase (NAD+)

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Tchigvintsev, A.; Singer, A.; Brown, G.; Flick, R.; Evdokimova, E.; Tan, K.; Gonzalez, C.F.; Savchenko, A.; Yakunin, A.F.

Biochemical and structural studies of uncharacterized protein PA0743 from Pseudomonas aeruginosa revealed NAD+-dependent L-serine dehydrogenase

J. Biol. Chem.

287

1874-1883

2012

Pseudomonas aeruginosa (Q9I5I6), Pseudomonas aeruginosa

Yoneda, K.; Sakuraba, H.; Araki, T.; Ohshima, T.

Crystal structure of the NADP+ and tartrate-bound complex of L-serine 3-dehydrogenase from the hyperthermophilic archaeon Pyrobaculum calidifontis

Extremophiles

395-405

2018

Pyrobaculum calidifontis