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Literature summary for 1.1.1.39 extracted from

  • Rao, G.S.J.; Coleman, D.E.; Karsten, W.E.; Cook, P.F.; Harris, B.G.
    Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site (2003), J. Biol. Chem., 278, 38051-38058.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
quarternary complex of purified enzyme with NADH, tartronate, and Mg2+, hanging drop vapour diffusion method, from 100 mM Tris-SO4, pH 7.3, 100 mM sodium acetate, 15% PEG 4000, 5 mM NADH, 10 mM tartronate, 20 mM MgSO4, 10 mM 2-mercaptoethanol, and 0.02% sodium azide, for cryoprotection the crystals are soaked in 25% PEG 4000, 15 mM NAD+, 10 mM 2-mercaptoethanol, and 100 mM Tris-SO4, pH 7.5, for 2 h, then 24 h in the crystallization buffer plus 20% EG v/v, X-ray diffraction structure determination and analysis at 2.0 A resolution, structure modeling Ascaris suum

Inhibitors

Inhibitors Comment Organism Structure
Tartronate binding site structure at the active site, competitive Ascaris suum

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Ascaris suum 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Ascaris suum

Organism

Organism UniProt Comment Textmining
Ascaris suum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ reaction mechanism, active site structure, enzyme-cofactor interactions, overview Ascaris suum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
Ascaris suum pyruvate + CO2 + NADH
-
?

Synonyms

Synonyms Comment Organism
ME
-
Ascaris suum
NAD-malic enzyme
-
Ascaris suum

Cofactor

Cofactor Comment Organism Structure
additional information binding site structure of NADH Ascaris suum
NAD+ conformational change upon binding Ascaris suum