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Literature summary for 5.3.99.6 extracted from

  • Neumann, P.; Brodhun, F.; Sauer, K.; Herrfurth, C.; Hamberg, M.; Brinkmann, J.; Scholz, J.; Dickmanns, A.; Feussner, I.; Ficner, R.
    Crystal structures of Physcomitrella patens AOC1 and AOC2: insights into the enzyme mechanism and differences in substrate specificity (2012), Plant Physiol., 160, 1251-1266.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.99.6

Cloned(Commentary)

Cloned (Comment) Organism
AOC1, expression as N-terminally GST-tagged enzyme in Escherichia coli Physcomitrium patens
AOC2, expression as N-terminally GST-tagged enzyme in Escherichia coli Physcomitrium patens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant free isozyme AOC2, X-ray diffraction structure determination and analysis at 1.95 A resolution Physcomitrium patens
purified recombinant isozyme AOC1, free or in complex with substrate analogue 12,13S-epoxy-9Z,15Z-octadecadienoic acid, X-ray diffraction structure determination and analysis at 1.35-2.0 A resolution Physcomitrium patens

Protein Variants

Protein Variants Comment Organism
F140V site-directed mutagenesis, the mutant variant is active with the 13-hydroperoxy octadecatrienoic acid-derived allene oxide, but inactive with 20:4(n-6)-derived (12S)-hydroperoxy eicosatetraenoic acid and (12S)-hydroperoxy eicosatetraenoic acid-derived allene oxide Physcomitrium patens
F29I/F140V site-directed mutagenesis, the mutant variant is active with the 13-hydroperoxy octadecatrienoic acid-derived allene oxide, but inactive with 20:4(n-6)-derived (12S)-hydroperoxy eicosatetraenoic acid and (12S)-hydroperoxy eicosatetraenoic acid-derived allene oxide Physcomitrium patens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Physcomitrium patens the plant contains two isozymes, PpAOC1 and PpAOC2, with different substrate specificities for C18- and C20-derived substrates, respectively. Comparison of complex structures of the C18 substrate analogue with in silico modeling of the C20 substrate analogue bound to the enzyme allows identification of the three major molecular determinants responsible for the different substrate specificities, i.e. larger active site diameter, an elongated cavity of PpAOC2, and two nonidentical residues at the entrance of the active site ?
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 ?

Organism

Organism UniProt Comment Textmining
Physcomitrium patens Q8GS38 isozyme AOC1; isozyme AOC1
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Physcomitrium patens Q8H0N6 isozyme AOC2; isozyme AOC2
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Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally GST-tagged isozyme AOC1 from Escherichia coli by glutathione affinity chromatography and gel filtration Physcomitrium patens

Reaction

Reaction Comment Organism Reaction ID
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate = (15Z)-12-oxophyto-10,15-dienoate catalytic mechanism of AOC isozymes: (1) a resting state of the apo enzyme with a closed conformation, (2) a first shallow binding mode, followed by (3) a tight binding of the substrate accompanied by conformational changes in the binding pocket, and (4) initiation of the catalytic cycle by opening of the epoxide ring. Cyclization of the allene oxide seems to be initiated by one particular Glu residue in the active site of AOC that leads to an opening of the epoxy ring, conformational changes, and a concerted pericyclic ring closure Physcomitrium patens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(12S)-hydroperoxy eicosatetraenoic acid 20:4(n-6)-derived (12S)-hydroperoxy eicosatetraenoic acid Physcomitrium patens 11-oxoprostatrienoic acid
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 ?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
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 Physcomitrium patens (15Z)-12-oxophyto-10,15-dienoate
-
 ?
additional information the plant contains two isozymes, PpAOC1 and PpAOC2, with different substrate specificities for C18- and C20-derived substrates, respectively. Comparison of complex structures of the C18 substrate analogue with in silico modeling of the C20 substrate analogue bound to the enzyme allows identification of the three major molecular determinants responsible for the different substrate specificities, i.e. larger active site diameter, an elongated cavity of PpAOC2, and two nonidentical residues at the entrance of the active site Physcomitrium patens ?
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 ?
additional information substrate specificity of isozyme AOC2, overview Physcomitrium patens ?
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 ?
additional information substrate specificity of wild-type and mutant isozymes AOC1, overview. The substrate dihydro analogue cis-12,13S-epoxy-9Z,15Z-octadecadienoic acid does not cyclize in the presence of PpAOC1, but when bound to the enzyme, it undergoes isomerization into the corresponding trans-epoxide. AOc1 shows no activity with 20:4(n-6)-derived (12S)-hydroperoxy eicosatetraenoic acid Physcomitrium patens ?
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 ?

Synonyms

Synonyms Comment Organism
Allene oxide cyclase
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 Physcomitrium patens
AOC
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 Physcomitrium patens
AOC1
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 Physcomitrium patens
AOC2
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 Physcomitrium patens

Cofactor

Cofactor Comment Organism Structure
heme
-
 Physcomitrium patens

General Information

General Information Comment Organism
metabolism the first specific step in the biosynthesis of the cyclopentanone class of oxylipins is catalyzed by allene oxide cyclase that forms cis(+)-12-oxo-phytodienoic acid. After reduction of the cyclopentenone by cis(+)-12-oxo-phytodienoic acid reductase isoform 3, the octanoic or hexanoic side chain is shortened by beta-oxidation cycles, pathway overview Physcomitrium patens
additional information comparison of active site structures of isozymes AOC1 and AOC2 and structure-function relationship, detailed overview Physcomitrium patens
additional information structural changes of the catalytic center lead to an open and closed conformation of PpAOC2. Comparison of active site structures of isozymes AOC1 and AOC2 and structure-function relationship, detailed overview Physcomitrium patens