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Literature summary extracted from

  • Singh, P.; Sarin, N.B.
    Structural characterization and functional validation of aldose reductase from the resurrection plant Xerophyta viscosa (2014), Mol. Biotechnol., 56, 971-978.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.1.21 biotechnology ALDRXV4 gene from Xerophyta viscosa is a potential candidate for developing stress-tolerant crop plants Xerophyta viscosa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.21 gene ALDRXV4, cDNA expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) using pET28a expression vector. Overexpression of enzyme ALDRXV4 improves growth and tolerance against diverse abiotic stresses induced by high salt (500 mM NaCl), osmoticum (10% PEG 6000), heavy metal (20 mM CdCl2), and methylglyoxal (5 mM) in Escherichia coli cells. Recombinant expression of ALDRXV4-GFP fusion enzyme in onion epidermal peel via Agrobacterium tumefaciens transfection method Xerophyta viscosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.21 additional information
-
additional information Michaelis-Menten kinetics Xerophyta viscosa
1.1.1.21 1.1
-
DL-glyceraldehyde pH 6.2, temperature not specified in the publication, recombinant His-tagged enzyme Xerophyta viscosa
1.1.1.21 1.2
-
methylglyoxal pH 6.2, temperature not specified in the publication, recombinant His-tagged enzyme Xerophyta viscosa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.21 cytoplasm
-
Xerophyta viscosa 5737
-
1.1.1.21 nucleus
-
Xerophyta viscosa 5634
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.21 36000
-
-
Xerophyta viscosa

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.21 Xerophyta viscosa Q9XF81
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.21 recombinant His-tagged enzyme several fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Xerophyta viscosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.21 DL-glyceraldehyde + NADPH + H+
-
Xerophyta viscosa glycerol + NADP+
-
?
1.1.1.21 malondialdehyde + NADPH + H+
-
Xerophyta viscosa ?
-
?
1.1.1.21 methylglyoxal + NADPH + H+
-
Xerophyta viscosa ?
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.21 ? x * 36000, about, recombinant enzyme, SDS-PAGE Xerophyta viscosa
1.1.1.21 More three-dimensional structure prediction based on homology modeling using the the structure of the Hordeum vulgare enzyme, PDB ID 2bgs, and circular dichroism spectroscopy structure analysis, overview Xerophyta viscosa

Synonyms

EC Number Synonyms Comment Organism
1.1.1.21 aldose reductase
-
Xerophyta viscosa
1.1.1.21 ALDRXV4
-
Xerophyta viscosa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.21 5.8
-
DL-glyceraldehyde pH 6.2, temperature not specified in the publication, recombinant His-tagged enzyme Xerophyta viscosa
1.1.1.21 14.5
-
methylglyoxal pH 6.2, temperature not specified in the publication, recombinant His-tagged enzyme Xerophyta viscosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.21 6.2
-
assay at Xerophyta viscosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.21 NADPH
-
Xerophyta viscosa

General Information

EC Number General Information Comment Organism
1.1.1.21 physiological function aldose reductases are key enzymes in the detoxification of reactive aldehyde compounds like methylglyoxal and malondialdehyde Xerophyta viscosa

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.21 5.3
-
DL-glyceraldehyde pH 6.2, temperature not specified in the publication, recombinant His-tagged enzyme Xerophyta viscosa
1.1.1.21 9.3
-
methylglyoxal pH 6.2, temperature not specified in the publication, recombinant His-tagged enzyme Xerophyta viscosa