EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.79 | additional information | invertion of the cofactor specificity of the NADP+-dependent enzyme glyoxylate reductase by a structure-guided, semirational strategy, overview. The heuristic-based approach leverages the diversity and sensitivity of catalytically productive cofactor binding geometries to limit the problem to an experimentally tractable scale. Experimental validation of the CSR-SALAD method for switching cofactor preference to NAD while retaining catalytic activity | Arabidopsis thaliana |
1.1.1.79 | R31L/T32K/K35D/C68R | site-directed mutagenesis of Rosmann fold (c.2.1.6) residues leading to a switch of cofactor preference of the enzyme from NADP(H) to NAD(H), altered cofactor kinetics of the mutant enzyme R31L/T32K/ K35D/C68R compared to the wild-type, overview | Arabidopsis thaliana |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.79 | additional information | - |
additional information | Michaelis-Menten kinetics, altered cofactor kinetics of the mutant enzyme R31L/T32K/K35D/C68R compared to the wild-type | Arabidopsis thaliana |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.79 | glycolate + NADP+ | Arabidopsis thaliana | - |
glyoxylate + NADPH + H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.79 | Arabidopsis thaliana | Q9LSV0 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.79 | glycolate + NADP+ | - |
Arabidopsis thaliana | glyoxylate + NADPH + H+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.79 | glyoxylate reductase | - |
Arabidopsis thaliana |
1.1.1.79 | GLYR1 | - |
Arabidopsis thaliana |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.79 | 24 | - |
assay at | Arabidopsis thaliana |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.79 | 7.8 | - |
assay at | Arabidopsis thaliana |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.79 | NADP+ | the wild-type enzyme is specific for NADPH/NADP+ | Arabidopsis thaliana | |
1.1.1.79 | NADPH | the wild-type enzyme is specific for NADPH/NADP+ | Arabidopsis thaliana |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.79 | evolution | the enzyme belongs to the group of enzymes with the most common NAD(P)-binding fold, the Rossmann fold, as well as other, less common cofactor binding folds (TIM barrel and dihydroquinoate synthase-like folds) | Arabidopsis thaliana |