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Literature summary extracted from

  • Valenzuela-Soto, E.M.; Munoz-Clares, R.A.
    Betaine-aldehyde dehydrogenase from leaves of Amaranthus hypochondriacus L. exhibits an Iso Ordered Bi Bi steady state mechanism (1993), J. Biol. Chem., 268, 23818-23823.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.8 AMP competitive with respect to NAD+ and mixed with betaine aldehyde and uncompetitive with respect to NAD+ Amaranthus hypochondriacus
1.2.1.8 choline
-
Amaranthus hypochondriacus
1.2.1.8 glycine betaine no inhibition up to 10 mM Amaranthus hypochondriacus
1.2.1.8 NADH mixed inhibitor against NAD+ and betaine aldehyde Amaranthus hypochondriacus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.8 0.0395
-
NAD+
-
Amaranthus hypochondriacus
1.2.1.8 0.0561
-
Betaine aldehyde
-
Amaranthus hypochondriacus

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.8 Amaranthus hypochondriacus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.1.8 betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+ iso-ordered bi-bi steady state mechanism Amaranthus hypochondriacus
1.2.1.8 betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+ NAD+ is the first substrate to bind to the enzyme and NADH is the last product to dissociate from it Amaranthus hypochondriacus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.8 leaf
-
Amaranthus hypochondriacus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.8 betaine aldehyde + NAD+ + H2O
-
Amaranthus hypochondriacus betaine + NADH
-
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Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.8 0.896
-
AMP with respect to NAD+ Amaranthus hypochondriacus
1.2.1.8 4.1
-
choline with respect to betaine aldehyde Amaranthus hypochondriacus