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 | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Agarophyton vermiculophyllum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | bound | Agarophyton vermiculophyllum | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | ferric heme enzyme | Agarophyton vermiculophyllum |
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 | 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 | 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 (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 | 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 | Comment | Organism |
---|---|---|
More | structure comparisons, overview | Agarophyton vermiculophyllum |
tetramer | 4 * 63500, recombinant His-tagged enzyme, SDS-PAGE | Agarophyton vermiculophyllum |
Synonyms | Comment | Organism |
---|---|---|
PGHS | - |
Agarophyton vermiculophyllum |
PGHS | - |
Coccotylus truncatus |
prostaglandin H synthase | - |
Agarophyton vermiculophyllum |
prostaglandin H synthase | - |
Coccotylus truncatus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
cyclooxygenase activity assay at | Agarophyton vermiculophyllum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
cyclooxygenase activity assay at | Agarophyton vermiculophyllum |
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 | 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 |