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Literature summary for 5.3.99.3 extracted from

  • Yamada, T.; Takusagawa, F.
    PGH2 degradation pathway catalyzed by GSH-heme complex bound microsomal prostaglandin E2 synthase type 2: the first example of a dual-function enzyme (2007), Biochemistry, 46, 8414-8424.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-terminally truncated enzyme in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
red-coloured protein purified after growth of Escherichia coli in LB medium containing delta-aminolevulinate and Fe(NO3)3. Enzyme contains bound glutathione and heme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isoform mPGES-2
-

Purification (Commentary)

Purification (Comment) Organism
purification after expression of N-terminally truncated enzyme in recombinant Escherichia coli growing in LB medium containing delta-aminolevulinate and Fe(NO3)3 gives a protein of red colour. Purification after growth of Escherichia coli on minimal medium gives a colourless protein Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information glutathione-heme-complex bound enzyme catalyzes formation of 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid and malonaldehyde from prostaglandin H2, i.e. shows lyase activity Homo sapiens ?
-
?

Cofactor

Cofactor Comment Organism Structure
heme crystallization data of red-coloured protein purified after growth of recombinant Escherichia coli in LB medium containing delta-aminolevulinate and Fe(NO3)3. Heme is complexed with bound glutathione forming a S-Fe coordination bond with no polar interaction with enzyme. Heme dissociation constant is 0.00053 mM Homo sapiens