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Literature summary for 4.2.1.92 extracted from

  • Deng, W.W.; Wu, Y.L.; Li, Y.Y.; Tan, Z.; Wei, C.L.
    Molecular Cloning and characterization of hydroperoxide lyase gene in the leaves of tea plant (Camellia sinensis) (2016), J. Agric. Food Chem., 64, 1770-1776 .
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
a unique cDNA fragment is isolated by suppressive subtractive hybridization (SSH) from a tea plant subjected to herbivory by tea geometrid Ectropis obliqua, a full-length cDNA is acquired by RACE, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3), quantitative RT-PCR expression analysis Camellia sinensis

Organism

Organism UniProt Comment Textmining
Camellia sinensis
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Camellia sinensis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.2
-
 purified recombinant enzyme, pH and temperature not specified in the publication Camellia sinensis

Subunits

Subunits Comment Organism
? x * 60000, recombinant His-tagged enzyme, SDS-PAGE Camellia sinensis

Synonyms

Synonyms Comment Organism
CsHPL
-
 Camellia sinensis
HPL
-
 Camellia sinensis
hydroperoxide lyase
-
 Camellia sinensis

Expression

Organism Comment Expression
Camellia sinensis CsHPL is strongly upregulated in tea plants after Ectropis obliqua pathogen attack up

General Information

General Information Comment Organism
physiological function hydroperoxide lyase (HPL) is the major enzyme in the biosynthesis of natural volatile aldehydes and alcohols in plants. The enzyme is important for defense against insects in tea plants Camellia sinensis