Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.26 extracted from

  • Shinoda, T.; Arai, K.; Taguchi, H.
    A highly specific glyoxylate reductase derived from a formate dehydrogenase (2007), Biochem. Biophys. Res. Commun., 355, 782-787.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information construction of a E141N/Q313E mutant formate dehydrogenase which gains glyoxylate reductase activity improved through enhancement of the hydrogen transfer step in the catalytic process, while the replacement induces no marked activity toward other 2-koxoacid substrates, and diminishes the enzyme's activity as to formate oxidation, substrate specificity and kinetic switch of the mutant, overview Paracoccus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.4
-
glyoxylate pH 7.0, 30°C, recombinant E141N/Q313E mutant formate dehydrogenase Paracoccus sp.

Organism

Organism UniProt Comment Textmining
Paracoccus sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glyoxylate + NADH a E141N/Q313E mutant formate dehydrogenase shows glyoxylate reductase activity improved through enhancement of the hydrogen transfer step in the catalytic process, overview Paracoccus sp. glycolate + NAD+
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at, E141N/Q313E mutant formate dehydrogenase Paracoccus sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3
-
glyoxylate pH 7.0, 30°C, recombinant E141N/Q313E mutant formate dehydrogenase Paracoccus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at, E141N/Q313E mutant formate dehydrogenase Paracoccus sp.

Cofactor

Cofactor Comment Organism Structure
NADH
-
Paracoccus sp.