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Literature summary extracted from

  • Munoz-Bacasehua, C.; Rosas-Rodriguez, J.A.; Lopez-Zavala, A.A.; Valenzuela-Soto, E.M.
    Spectroscopic analysis of coenzyme binding to betaine aldehyde dehydrogenase dependent on potassium (2021), Luminescence, 2021, 1-10 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.8 K+ thermal stability of the pkBADH-NAD+ complex in the presence of K+ shows a complete loss of the ellipticity signal and highly cooperative thermal transitions in each thermogram in the presence of each K+ concentration tested. In all tested conditions, the thermal denaturation is irreversible Sus scrofa
1.2.1.8 NADH a mixed-type inhibitor of the enzyme. After NADH release, the enzyme cannot start a new catalytic cycle, possibly because of the catalytic residue protonation state Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.8 additional information
-
 additional information pkBADH kinetic analysis Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.1.8 K+ required for binding of cofactor NAD+. K+ causes small changes in secondary and tertiary structures that influences the active site conformation, binding of K+ to the enzyme caused changes in the alpha-helix content of 4% and 12% in the presence of 25 mM and 100 mM K+, respectively Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.8 betaine aldehyde + NAD+ + H2O Sus scrofa
-
 betaine + NADH + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.8 Sus scrofa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.1.8 betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+ porcine kidney BADH follows an iso bi-bi ordered mechanism in which NAD+ is the first substrate to bind to pkBADH and NADH is the last product released Sus scrofa
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.8 kidney
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.8 betaine aldehyde + NAD+ + H2O
-
 Sus scrofa betaine + NADH + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.8 More secondary and tertiary structure of pkBADH in presence or absence of NAD+, fluorescence quenching spectra of pkBADH titrated with variable NAD+ concentrations in presence of potassium, overview. The deconvolution data analysis shows a 13% increase in the pkBADH helical structure, a decrease of 7% in beta-sheet content and 6% in turns content during the pkBADH-NAD+ complex formation Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
1.2.1.8 BADH
-
 Sus scrofa
1.2.1.8 betaine aldehyde dehydrogenase
-
 Sus scrofa
1.2.1.8 pkBADH
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.8 25
-
 assay at Sus scrofa

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.1.8 47.2 59.9 thermal stability of the pkBADH-NAD+ complex in the presence of K+ shows a complete loss of the ellipticity signal and highly cooperative thermal transitions in each thermogram in the presence of each K+ concentration tested. In all tested conditions, the thermal denaturation is irreversible. The first derivative analysis from the pkBADH-NAD+ complex shows a peak with a (Tm)app value of 47.2°C, the addition of 25 mM K+ increased the (Tm)app to 59.9°C, while the addition of 50 mM or 100 mM K+ provokes changes in the (Tm)app to 55.9°C or 54.9°C, respectively. Binding of NAD+ to pkBADH causes a lower thermal stability of the enzyme Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.8 8
-
 assay at Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.8 NAD+ porcine kidney betaine aldehyde dehydrogenase (pkBADH) binds NAD+ with different affinities at each active site and the binding is K+ dependent Sus scrofa

General Information

EC Number General Information Comment Organism
1.2.1.8 physiological function porcine kidney betaine aldehyde dehydrogenase (pkBADH) binds NAD+ with different affinities at each active site and the binding is K+ dependent Sus scrofa