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Literature summary extracted from

  • Pfaff, C.; Glindemann, N.; Gruber, J.; Frentzen, M.; Sadre, R.
    Chorismate pyruvate-lyase and 4-hydroxy-3-solanesylbenzoate decarboxylase are required for plastoquinone biosynthesis in the cyanobacterium Synechocystis sp. PCC6803 (2014), J. Biol. Chem., 289, 2675-2686.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.98 expressed in Escherichia coli ubiX and ubiD deletion mutant Synechocystis sp.
4.1.3.40 gene sll1797, phylogenetic analysis and tree, expression in Escherichia coli strain BL21AI as GST-tagged protein, and in Escherichia coli strain BW25113 for quantitative expression analysis by real time quantitative PCR. Complementation of ubiquinone-deficient Escherichia coli mutants by catalytic activity of heterologous Sll1797 Synechocystis sp.

Protein Variants

EC Number Protein Variants Comment Organism
4.1.3.40 additional information generation of a Synechocystis sp. single-gene knockout mutant lacking the chorismate pyruvate-lyase Sll1797 Synechocystis sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.1.98 membrane
-
 Synechocystis sp. 16020
-
4.1.3.40 membrane the recombinant enzyme shows severalfold higher specific activities in membrane than in soluble protein fractions Synechocystis sp. 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.98 additional information the addition of divalent cations does not stimulate the enzyme activity Synechocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.98 a 4-hydroxy-3-polyprenylbenzoate Synechocystis sp.
-
 a 2-polyprenylphenol + CO2
-
 ?
4.1.3.40 chorismate Synechocystis sp.
-
 4-hydroxybenzoate + pyruvate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.98 Synechocystis sp.
-
-
-
4.1.3.40 Synechocystis sp. P73322 gene sll1797
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.40 recombinant GST-tagged enzyme from Escherichia coli strain BL21AI by glutathione affinity chromatography Synechocystis sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.98 4-hydroxy-3-farnesylbenzoate highest activity with 4-hydroxy-3-farnesylbenzoate Synechocystis sp. ? + CO2
-
 ?
4.1.1.98 4-hydroxy-3-geranylgeranylbenzoate
-
 Synechocystis sp. ? + CO2
-
 ?
4.1.1.98 a 4-hydroxy-3-polyprenylbenzoate
-
 Synechocystis sp. a 2-polyprenylphenol + CO2
-
 ?
4.1.1.98 additional information very low specific activity with 4-hydroxy-3-octaprenylbenzoate Synechocystis sp. ?
-
 ?
4.1.3.40 chorismate
-
 Synechocystis sp. 4-hydroxybenzoate + pyruvate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.98 4-hydroxy-3-solanesylbenzoate decarboxylase
-
 Synechocystis sp.
4.1.1.98 slr1099
-
 Synechocystis sp.
4.1.3.40 chorismate pyruvate-lyase
-
 Synechocystis sp.
4.1.3.40 Sll1797
-
 Synechocystis sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.98 30
-
-
 Synechocystis sp.
4.1.3.40 30
-
-
 Synechocystis sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.98 8.5
-
-
 Synechocystis sp.
4.1.3.40 8
-
-
 Synechocystis sp.

General Information

EC Number General Information Comment Organism
4.1.1.98 malfunction disruption of the slr1099 gene results in reduced growth rates and plastoquinone contents Synechocystis sp.
4.1.3.40 malfunction a knockout mutant shows highyl reduced plastoquinone content, and the mutant requires 4-hydroxybenzoate for growth Synechocystis sp.
4.1.3.40 metabolism the enzyme is required for initiation of cyanobacterial plastoquinone biosynthesis, together with two 4-hydroxy-3-solanesylbenzoate decarboxylases. The chorismate pyruvate-lyase Sll1797 catalyzes the conversion of chorismate to 4-hydroxybenzoate that is prenylated by Slr0926. Slr1099 and Sll0936 are both involved in the decarboxylation of 4-hydroxy-3-solanesylbenzoate Synechocystis sp.