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Literature summary for 1.1.1.40 extracted from

  • Hsu, R.Y.; Glynias, M.J.; Satterlee, J.; Feeney, R.; Clarke, A.R.; Emery, D.C.; Roe, B.A.; Wilson, R.K.; Goodridge, A.G.; Holbrook, J.J.
    Duck liver 'malic' enzyme. Expression in Escherichia coli and characterization of the wild-type enzyme and site-directed mutants (1992), Biochem. J., 284, 869-876.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli TH-2 cells as a fusion protein including a 15-residue N-terminal leader from beta-galactosidase coded by the lacZ gene Anas platyrhynchos

Protein Variants

Protein Variants Comment Organism
C99S turnover number decreases 3fold and Km for malate increases 4fold Anas platyrhynchos
R70Q kinetic parameters are similar except for a slightly lower turnover number and higher Km for L-malate Anas platyrhynchos

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0046
-
 NADP+
-
 Anas platyrhynchos
0.073
-
 L-malate
-
 Anas platyrhynchos

Organism

Organism UniProt Comment Textmining
Anas platyrhynchos
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Anas platyrhynchos

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Anas platyrhynchos
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NADP+
-
 Anas platyrhynchos pyruvate + CO2 + NADPH
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
160
-
 L-malate
-
 Anas platyrhynchos

Cofactor

Cofactor Comment Organism Structure
NADP+ cofactor Anas platyrhynchos