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Literature summary for 1.1.1.169 extracted from

  • Miyanaga, A.; Fujisawa, S.; Furukawa, N.; Arai, K.; Nakajima, M.; Taguchi, H.
    The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase (2013), Biochem. Biophys. Res. Commun., 439, 109-114.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-4-dehydropantoate + NADPH + H+ Enterococcus faecalis
-
(R)-pantoate + NADP+
-
?
(R)-4-dehydropantoate + NADPH + H+ Enterococcus faecalis IAM10071
-
(R)-pantoate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis E3USM3
-
-
Enterococcus faecalis IAM10071 E3USM3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-4-dehydropantoate + NADPH + H+
-
Enterococcus faecalis (R)-pantoate + NADP+
-
?
(R)-4-dehydropantoate + NADPH + H+
-
Enterococcus faecalis IAM10071 (R)-pantoate + NADP+
-
?

Synonyms

Synonyms Comment Organism
2-ketopantoate reductase
-
Enterococcus faecalis
KPR
-
Enterococcus faecalis

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Enterococcus faecalis