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Literature summary for 4.2.3.9 extracted from

  • Miller, D.J.; Gao, J.; Truhlar, D.G.; Young, N.J.; Gonzalez, V.; Allemann, R.K.
    Stereochemistry of eudesmane cation formation during catalysis by aristolochene synthase from Penicillium roqueforti (2008), Org. Biomol. Chem., 6, 2346-2354.
    View publication on PubMed
Search for more literature for 4.2.3.9

Cloned(Commentary)

Cloned (Comment) Organism
expression of AS and AS-F112A in Escherichia coli Penicillium roqueforti

Protein Variants

Protein Variants Comment Organism
F112A expression of AS-F112A in Escherichia coli Penicillium roqueforti

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0008
-
 farnesyl diphosphate assay under normal conditions and in D2O, 20 mM Tris, 5 mM MgCl2, 5 mM 2-mercaptoethanol and 15% glycerol Penicillium roqueforti

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Penicillium roqueforti

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
farnesyl diphosphate Penicillium roqueforti biogenetic precursor of more than 300 different sesquiterpene hydrocarbon scaffolds in plants, bacteria and fungi (+)-aristolochene + diphosphate
-
 ?
additional information Penicillium roqueforti reaction is a a cyclisation cascade that leads to the generation of two 6-membered rings, three chiral centres, and two double bonds with high regio- and stereospecificity. Concurrent to diphosphate expulsion enzyme facilitates attack of C1 in farnesyl diphosphate by the C10, C11-double bond to produce germacryl cation. Proton loss from C12 leads to the production of (S)-germacrene A which is then postulated to undergo reprotonation of the C6, C7-double bond and a further cyclisation to form the bicyclic eudesmane cation. Successive 1,2-hydride shift and methyl migration followed by loss of H on C8 completes the generation of (+)-aristolochene ?
-
 ?

Organism

Organism UniProt Comment Textmining
Penicillium roqueforti
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Proteins are extracted from the inclusion bodies and purified following established protocols, each enzyme is pure as judged by SDS-gel electrophoresis Penicillium roqueforti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
farnesyl diphosphate biogenetic precursor of more than 300 different sesquiterpene hydrocarbon scaffolds in plants, bacteria and fungi Penicillium roqueforti (+)-aristolochene + diphosphate
-
 ?
additional information reaction is a a cyclisation cascade that leads to the generation of two 6-membered rings, three chiral centres, and two double bonds with high regio- and stereospecificity. Concurrent to diphosphate expulsion enzyme facilitates attack of C1 in farnesyl diphosphate by the C10, C11-double bond to produce germacryl cation. Proton loss from C12 leads to the production of (S)-germacrene A which is then postulated to undergo reprotonation of the C6, C7-double bond and a further cyclisation to form the bicyclic eudesmane cation. Successive 1,2-hydride shift and methyl migration followed by loss of H on C8 completes the generation of (+)-aristolochene Penicillium roqueforti ?
-
 ?

Synonyms

Synonyms Comment Organism
aristolochene synthase
-
 Penicillium roqueforti
AS
-
 Penicillium roqueforti

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Penicillium roqueforti

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.02
-
 farnesyl diphosphate assay under normal conditions and in D2O, 20 mM Tris, 5 mM MgCl2, 5 mM 2-mercaptoethanol and 15% glycerol Penicillium roqueforti

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Penicillium roqueforti