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Literature summary for 1.14.99.1 extracted from

  • Varvas, K.; Kasvandik, S.; Hansen, K.; Jaerving, I.; Morell, I.; Samel, N.
    Structural and catalytic insights into the algal prostaglandin H synthase reveal atypical features of the first non-animal cyclooxygenase (2013), Biochim. Biophys. Acta, 1831, 863-871.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
PGHS DNA and amiino acid sequence determination and analysis, sequence comparisons Coccotylus truncatus
PGHS DNA and amino acid sequence determination and analysis, sequence comparisons, functional expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)RP Agarophyton vermiculophyllum

Inhibitors

Inhibitors Comment Organism Structure
additional information algal PGHS is not inhibited by non-steroidal anti-inflammatory drugs that inhibit the mammalian enzymes Agarophyton vermiculophyllum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Agarophyton vermiculophyllum

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane bound Agarophyton vermiculophyllum 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ ferric heme enzyme Agarophyton vermiculophyllum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63500
-
4 * 63500, recombinant His-tagged enzyme, SDS-PAGE Agarophyton vermiculophyllum
330000
-
about, recombinant His-tagged enzyme, gel filtration Agarophyton vermiculophyllum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
arachidonate + AH2 + 2 O2 Agarophyton vermiculophyllum
-
prostaglandin G2 + A + ?
-
?
arachidonate + AH2 + 2 O2 Agarophyton vermiculophyllum
-
prostaglandin H2 + A + H2O
-
?

Organism

Organism UniProt Comment Textmining
Agarophyton vermiculophyllum I6VVK9 collected from the coast of Kanagawa Prefecture in Tokyo Bay
-
Coccotylus truncatus I6VCP8 collected on the coast of the Baltic Sea in Kassari Bay
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme 138fold from Escherichia coli strain BL21(DE3)RP membranes by nickel affinity chromatography, and anion exchange chromatography Agarophyton vermiculophyllum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arachidonate + AH2 + 2 O2
-
Agarophyton vermiculophyllum prostaglandin G2 + A + ?
-
?
arachidonate + AH2 + 2 O2
-
Agarophyton vermiculophyllum prostaglandin H2 + A + H2O
-
?
arachidonate + reduced N,N,N',N'-tetramethylphenylenediamine + 2 O2
-
Agarophyton vermiculophyllum prostaglandin G2 + oxidized N,N,N',N'-tetramethylphenylenediamine + ?
-
?
arachidonate + reduced N,N,N',N'-tetramethylphenylenediamine + 2 O2
-
Agarophyton vermiculophyllum prostaglandin H2 + oxidized N,N,N',N'-tetramethylphenylenediamine + H2O
-
?

Subunits

Subunits Comment Organism
More structure comparisons, overview Agarophyton vermiculophyllum
tetramer 4 * 63500, recombinant His-tagged enzyme, SDS-PAGE Agarophyton vermiculophyllum

Synonyms

Synonyms Comment Organism
PGHS
-
Agarophyton vermiculophyllum
PGHS
-
Coccotylus truncatus
prostaglandin H synthase
-
Agarophyton vermiculophyllum
prostaglandin H synthase
-
Coccotylus truncatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
cyclooxygenase activity assay at Agarophyton vermiculophyllum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
cyclooxygenase activity assay at Agarophyton vermiculophyllum

Cofactor

Cofactor Comment Organism Structure
heme ferric heme, heme content of the purified recombinant GvPGHS determined by a pyridine-hemochromogen assay is 0.39 mol of heme/mol of GvPGHS monomer Agarophyton vermiculophyllum

General Information

General Information Comment Organism
evolution the algal PGHS lacks structural elements identified in all known animal PGHSs, such as epidermal growth factor-like domain and helix B in the membrane binding domain. The key residues of animal PGHS, like catalytic Tyr385 and heme liganding His388 are conserved in the algal enzyme, but the amino acid residues shown to be important for substrate binding and coordination, and the target residues for nonsteroidal anti-inflammatory drugs, Arg120, Tyr355, and Ser530, are not found at the appropriate positions in the algal sequences. The preferred substrate for the algal PGHS is arachidonic acid with cyclooxygenase reaction rate remarkably higher than values reported for mammalian PGHS isoforms Agarophyton vermiculophyllum