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Literature summary for 1.11.1.11 extracted from

  • Ma, W.; Yang, Y.
    Cloning, expression and purification of an ascorbate peroxidase gene from Rhus chinensis (2019), J. Plant Biochem. Biotechnol., 28, 223-229 .
No PubMed abstract available
Search for more literature for 1.11.1.11

Cloned(Commentary)

Cloned (Comment) Organism
gene APX, DNA and amino acid sequence determination and analysis. The 1938 bp RcAPX gene encompasses 6 introns and 7 exons. The open reading frame of RcAPX is 750 bp long and encodes a 249-amino acid peptide, sequence comparisons and phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis. Recombinant expression in Escherichia coli Rhus chinensis

Protein Variants

Protein Variants Comment Organism
D207A site-directed mutagenesis, the mutant retains 18.5% activity of the wild-type activity Rhus chinensis
H162L site-directed mutagenesis, the mutant retains 24.2% activity of the wild-type activity Rhus chinensis
H42L site-directed mutagenesis, the mutant retains 23.5% activity of the wild-type activity Rhus chinensis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Rhus chinensis 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in the heme group Rhus chinensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 L-ascorbate + H2O2 + 2 H+ Rhus chinensis
-
 L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Rhus chinensis
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Rhus chinensis
-
additional information RcAPX is found in all tested tissues with highest amounts in young petioles. Enzyme RcAPX shows differential expression in different tissues at various developmental stages. RcAPX expression is significantly suppressed by galls, Galla chinensis, resulting from the galling aphid Schlechtendalia chinensis parasitizing the vein or compound leaves of Rhus chinensis Rhus chinensis
-
petiole
-
 Rhus chinensis
-
root
-
 Rhus chinensis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-ascorbate + H2O2 + 2 H+
-
 Rhus chinensis L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?

Subunits

Subunits Comment Organism
? x * 27189, sequence calculation Rhus chinensis
More RcAPX consists of 32.13% alpha-helixes, 9.24% beta-sheets, and 58.63% random coil regions Rhus chinensis

Synonyms

Synonyms Comment Organism
APX
-
 Rhus chinensis
ascorbate peroxidase
-
 Rhus chinensis
RcAPX
-
 Rhus chinensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 recombinant enzyme Rhus chinensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 recombinant enzyme Rhus chinensis

Cofactor

Cofactor Comment Organism Structure
heme
-
 Rhus chinensis

pI Value

Organism Comment pI Value Maximum pI Value
Rhus chinensis sequence calculation
-
 5.43

Expression

Organism Comment Expression
Rhus chinensis RcAPX expression is significantly suppressed by galls, Galla chinensis, resulting from the galling aphid Schlechtendalia chinensis parasitizing the vein or compound leaves of Rhus chinensis down

General Information

General Information Comment Organism
additional information possible substrate binding sites include His42, His162 and Asp20, substrate docking study Rhus chinensis
physiological function ascorbate peroxidase (APX) is the key enzyme in hydrogen peroxide degradation, and may have a critical function in plant-aphid interactions. The enzyme has an essential function in the scavenging of H2O2 produced in normal metabolic conditions or under environmental stress due to drought Rhus chinensis