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Literature summary for 1.1.1.79 extracted from

  • Cahn, J.K.; Werlang, C.A.; Baumschlager, A.; Brinkmann-Chen, S.; Mayo, S.L.; Arnold, F.H.
    A general tool for engineering the NAD/NADP cofactor preference of oxidoreductases (2016), ACS Synth. Biol., 6, 326-333.
    View publication on PubMed
Search for more literature for 1.1.1.79

Protein Variants

Protein Variants Comment Organism
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
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycolate + NADP+ Arabidopsis thaliana
-
 glyoxylate + NADPH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9LSV0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycolate + NADP+
-
 Arabidopsis thaliana glyoxylate + NADPH + H+
-
 ?

Synonyms

Synonyms Comment Organism
glyoxylate reductase
-
 Arabidopsis thaliana
GLYR1
-
 Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
24
-
 assay at Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
NADP+ the wild-type enzyme is specific for NADPH/NADP+ Arabidopsis thaliana
NADPH the wild-type enzyme is specific for NADPH/NADP+ Arabidopsis thaliana

General Information

General Information Comment Organism
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