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Literature summary for 4.2.3.9 extracted from

  • Deligeorgopoulou, A.; Allemann, R.K.
    Evidence for differential folding of farnesyl pyrophosphate in the active site of aristolochene synthase: a single-point mutation converts aristolochene synthase into an (E)-b-farnesene synthase (2003), Biochemistry, 42, 7741-7747.
    View publication on PubMed
Search for more literature for 4.2.3.9

Cloned(Commentary)

Cloned (Comment) Organism
mutant enzymes Y92C and Y92A Penicillium roqueforti

Protein Variants

Protein Variants Comment Organism
Y92A turnover number is approximately 2 orders of magnitude lower than the value observed for the wild-type enzyme,the mutant enzyme produces almost 80% of the alicyclic sesquiterpenes (E)-beta-farnesene and (E,E)-alpha-farnesene. The mutant also produces small amounts of additional hydrocarbons with a molecular weight of 204: alpha-selinene, beta-selinene, selina-4,11-diene, (E,Z)-alpha-farnesene, and beta-bisabolene. Km-value for trans, trans-farnesyl diphosphate is 0.0834 mM compared to 0.0023 mM for the wild-type enzyme Penicillium roqueforti
Y92A reduction of the size of the side chain of residue 92 leads to the production of the alicyclic sesquiterpenes (E)-beta- and (E,E)-alpha-farnesene. The relative amounts of linear products formed depend linearly on the size of the residues at position 92. ASY92A produces almost 80% of alicyclic sesquiterpenes and no aristolochene Penicillium roqueforti
Y92C turnover number is approximately 2 orders of magnitude lower than the value observed for the wild-type enzyme. Km-value for trans, trans-farnesyl diphosphate is 0.05027 mM compared to 0.0023 mM for the wild-type enzyme Penicillium roqueforti
Y92C reduction of the size of the side chain of residue 92 leads to the production of the alicyclic sesquiterpenes (E)-beta- and (E,E)-alpha-farnesene. Mutant ASY92C still produces about 6.8% of aristolochene Penicillium roqueforti
Y92F reduction of the size of the side chain of residue 92 leads to the production of the alicyclic sesquiterpenes (E)-beta- and (E,E)-alpha-farnesene Penicillium roqueforti
Y92V reduction of the size of the side chain of residue 92 leads to the production of the alicyclic sesquiterpenes (E)-beta- and (E,E)-alpha-farnesene Penicillium roqueforti

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0023
-
 (2E,6E)-farnesyl diphosphate wild-type, pH 7.5, temperature not specified in the publication Penicillium roqueforti
0.0502
-
 (2E,6E)-farnesyl diphosphate mutant Y92C, pH 7.5, temperature not specified in the publication Penicillium roqueforti
0.05027
-
 trans,trans-farnesyl diphosphate pH 7.5, mutant enzyme Y92C Penicillium roqueforti
0.0834
-
 trans,trans-farnesyl diphosphate pH 7.5, mutant enzyme Y92A Penicillium roqueforti
0.0834
-
 (2E,6E)-farnesyl diphosphate mutant Y92A, pH 7.5, temperature not specified in the publication Penicillium roqueforti

Organism

Organism UniProt Comment Textmining
Penicillium roqueforti
-
-
-
Penicillium roqueforti Q03471
-
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzyme Y92C and Y92A Penicillium roqueforti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate
-
 Penicillium roqueforti (+)-5-epi-aristolochene + diphosphate the steric bulk of residue 92 is central in binding of farnesyl diphosphate to the active site of aristolochene synthase in a quasi-cyclic conformation, thereby facilitating attack of C1 by the C10-C11 double bond to produce the cis-fused decalin S-germacrene A. Reduction of the size of the side chain of residue 92 leads to the production of the alicyclic sesquiterpenes (E)-beta- and (E,E)-alpha-farnesene. The relative amounts of linear products formed depend linearly on the size of the residues at position 92 ?
trans,trans-farnesyl diphosphate the steric bulk of residue 92 is central in binding of farnesyl diphosphate to the active site of the enzyme in a quasi-cyclic conformation, thereby facilitating attack of C1 by the C10-C11 double bond to produce the cis-fused decalin S-germacrene A. The cyclization of farnesyl diphosphate to germacrene A in aristolochene synthase proceeds in a stepwise fashion through farnesyl cation Penicillium roqueforti aristolochene + diphosphate the mutant Y92A produces almost 80% of the alicyclic sesquiterpenes (E)-beta-farnesene and (E,E)-alpha-farnesene. The mutant also produces small amounts of additional hydrocarbons with a molecular weight of 204: alpha-selinene, beta-selinene, selina-4,11-diene, (E,Z)-alpha-farnesene, and beta-bisabolene ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00049
-
 (2E,6E)-farnesyl diphosphate mutant Y92C, pH 7.5, temperature not specified in the publication Penicillium roqueforti
0.000491
-
 trans,trans-farnesyl diphosphate pH 7.5, mutant enzyme Y92C Penicillium roqueforti
0.00137
-
 trans,trans-farnesyl diphosphate pH 7.5, mutant enzyme Y92A Penicillium roqueforti
0.0014
-
 (2E,6E)-farnesyl diphosphate mutant Y92A, pH 7.5, temperature not specified in the publication Penicillium roqueforti
0.03
-
 (2E,6E)-farnesyl diphosphate wild-type, pH 7.5, temperature not specified in the publication Penicillium roqueforti

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.01
-
 (2E,6E)-farnesyl diphosphate mutant Y92C, pH 7.5, temperature not specified in the publication Penicillium roqueforti
0.016
-
 (2E,6E)-farnesyl diphosphate mutant Y92A, pH 7.5, temperature not specified in the publication Penicillium roqueforti
13.04
-
 (2E,6E)-farnesyl diphosphate wild-type, pH 7.5, temperature not specified in the publication Penicillium roqueforti