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Literature summary for 1.5.1.17 extracted from

  • Gohlke, H.; Hergert, U.; Meyer, T.; Mulnaes, D.; Grieshaber, M.K.; Smits, S.H.; Schmitt, L.
    Binding region of alanopine dehydrogenase predicted by unbiased molecular dynamics simulations of ligand diffusion (2013), J. Chem. Inf. Model., 53, 2493-2498 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
L-alanine uncompetitive substrate inhibition Arenicola marina

KM Value [mM]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Arenicola marina B5D5P2
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme to homogeneity Arenicola marina

Substrates and Products (Substrate)

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

Subunits Comment Organism
? x * 45000, SDS-PAGE Arenicola marina

Synonyms

Synonyms Comment Organism
ALADH
-
Arenicola marina
AlaDHAm
-
Arenicola marina

Turnover Number [1/s]

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

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 [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
58
-
L-alanine pH and temperature not specified in the publication Arenicola marina

General Information

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