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Results 1 - 10 of 10
EC Number General Information Commentary Reference
Show all pathways known for 1.1.1.169Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.169evolution the enzyme is a member of the family of 2-hydroxyacid dehydrogenases 740065
Show all pathways known for 1.1.1.169Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.169malfunction both the homologous gene from Enterococcus faecalis V583 (EF1861) and Escherichia coli panE functionally complement Francisella novicida lacking any KPR. Furthermore, panG from Francisella novicida can complement an Escherichia coli KPR double mutant. A panG deletion mutant is a pantothenate auxotroph and is genetically and chemically complemented with pang in trans or with the addition of pantolactone 725293
Show all pathways known for 1.1.1.169Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.169malfunction enzyme mutation A181L causes substitution of Ser239 and increases the Km for ketopantoate 844fold, without affecting kcat. The decrease in 2-dehydropantoate affinity enhances the already kinetically preferred NADPH binding path, making the random mechanism appear to be sequentially ordered and reducing the kinetic cooperativity 740065
Show all pathways known for 1.1.1.169Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.169malfunction gene disruption of gene TK1968results in a strain with growth defects that are complemented by addition of pantoate -, 736827
Show all pathways known for 1.1.1.169Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.169metabolism ketopantoate reductase from the hyperthermophilic archaeon Thermococcus kodakarensis catalyses the second step in CoA biosynthesis, the reduction of 2-oxopantoate to pantoate. CoA biosynthesis in the archaeon is regulated by feedback inhibition of enzyme ketopantoate reductase -, 736827
Show all pathways known for 1.1.1.169Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.169more CoA and 2-oxopantoate cooperatively trigger a conformational change from an open form to a closed enzyme form, structure analysis, overview -, 741385
Show all pathways known for 1.1.1.169Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.169more residue Ser239 is known to be important for the binding affinity of 2-dehydropantoate 740065
Show all pathways known for 1.1.1.169Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.169physiological function ketopantoate reductase (KPR) catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate to pantoate, and is a target of the feedback inhibition by CoA in archaea. Coenzyme A (CoA) plays essential roles in a variety of metabolic pathways in all three domains of life. The biosynthesis pathway of CoA is strictly regulated by feedback inhibition. In bacteria and eukaryotes, pantothenate kinase is the target of feedback inhibition by CoA -, 741385
Show all pathways known for 1.1.1.169Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.169physiological function ketopantoate reductase (KPR) catalyzes the NADPH-dependent production of pantoate, an essential precursor in the biosynthesis of coenzyme A 740065
Show all pathways known for 1.1.1.169Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.169physiological function ketopantoate reductase catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate which is a step in the biosynthesis of coenzyme A -, 739822
Results 1 - 10 of 10