Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-alanine | uncompetitive substrate inhibition | Arenicola marina |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics, thermodynamics and kinetics of substrate binding | Arenicola marina | |
14.8 | - |
L-alanine | pH and temperature not specified in the publication | Arenicola marina | |
655.1 | - |
glycine | pH and temperature not specified in the publication | Arenicola marina |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-alanine + pyruvate + NADH + H+ | Arenicola marina | reductive condensation, the enzyme is highy specific for L-alanine | 2,2'-iminodipropanoate + NAD+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arenicola marina | B5D5P2 | - |
- |
Purification (Comment) | Organism |
---|---|
native enzyme to homogeneity | Arenicola marina |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycine + pyruvate + NADH + H+ | reductive condensation, low activity | Arenicola marina | ? + NAD+ + H2O | - |
? | |
L-alanine + pyruvate + NADH + H+ | reductive condensation, the enzyme is highy specific for L-alanine | Arenicola marina | 2,2'-iminodipropanoate + NAD+ + H2O | - |
? | |
additional information | L-alanine binding region of alanopine dehydrogenase near a distinct helix-link-helix motif predicted by unbiased molecular dynamics simulations of ligand diffusion using a homology model of alanopine dehydrogenase, overview | Arenicola marina | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 45000, SDS-PAGE | Arenicola marina |
Synonyms | Comment | Organism |
---|---|---|
ALADH | - |
Arenicola marina |
AlaDHAm | - |
Arenicola marina |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
176.4 | - |
glycine | pH and temperature not specified in the publication | Arenicola marina | |
1084.6 | - |
L-alanine | pH and temperature not specified in the publication | Arenicola marina |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | cofactor binding region determination predicted by unbiased molecular dynamics simulations of ligand diffusion | Arenicola marina | |
NAD+ | - |
Arenicola marina | |
NADH | - |
Arenicola marina |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
58 | - |
L-alanine | pH and temperature not specified in the publication | Arenicola marina |
General Information | Comment | Organism |
---|---|---|
evolution | AlaDHAm is a member of the family of opine dehydrogenases (OpDHs), which catalyze the reductive condensation of pyruvate with an L-amino acid in the presence of NADH to so-called opines during anaerobic glycolysis. Residue E141 of domain I and W279 of domain II are conserved in OpDHs and are present in AlaDHAm, stucture comparisons, overview | Arenicola marina |
metabolism | AlaDHAm is a member of the family of opine dehydrogenases (OpDHs), which catalyze the reductive condensation of pyruvate with an L-amino acid in the presence of NADH to so-called opines during anaerobic glycolysis | Arenicola marina |
additional information | L-alanine binding region of alanopine dehydrogenase near a distinct helix-link-helix motif predicted by unbiased molecular dynamics simulations of ligand diffusion using a homology model of alanopine dehydrogenase, overview. L-Alanine is accommodated in a pocket mainly formed by residues Y236, V276, W279, Y280, Y284, L294, N301, and Y304 of domain II, five of which are strictly conserved | Arenicola marina |