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Literature summary for 1.1.1.79 extracted from

  • Husic, D.W.; Tolbert, N.E.
    NADH:hydroxypyruvate reductase and NADPH:glyoxylate reductase in algae: partial purification and characterization from Chlamydomonas reinhardtii (1987), Arch. Biochem. Biophys., 252, 396-408.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
glyoxylate
-
Chlamydomonas reinhardtii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glyoxylate + NAD(P)H Chlamydomonas reinhardtii enzyme prefers NADPH glycolate + NAD(P)+
-
?

Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glyoxylate + NAD(P)H enzyme prefers NADPH Chlamydomonas reinhardtii glycolate + NAD(P)+
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 9.5
-
Chlamydomonas reinhardtii

Cofactor

Cofactor Comment Organism Structure
NAD(P)H NADPH is preferred Chlamydomonas reinhardtii
NADPH NADPH is preferred Chlamydomonas reinhardtii