EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.3.9 | mutant enzymes Y92C and Y92A | Penicillium roqueforti |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.2.3.9 | 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 |
4.2.3.9 | 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 |
4.2.3.9 | 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 |
4.2.3.9 | 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 |
4.2.3.9 | 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 |
4.2.3.9 | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.3.9 | 0.0023 | - |
(2E,6E)-farnesyl diphosphate | wild-type, pH 7.5, temperature not specified in the publication | Penicillium roqueforti | |
4.2.3.9 | 0.0502 | - |
(2E,6E)-farnesyl diphosphate | mutant Y92C, pH 7.5, temperature not specified in the publication | Penicillium roqueforti | |
4.2.3.9 | 0.05027 | - |
trans,trans-farnesyl diphosphate | pH 7.5, mutant enzyme Y92C | Penicillium roqueforti | |
4.2.3.9 | 0.0834 | - |
trans,trans-farnesyl diphosphate | pH 7.5, mutant enzyme Y92A | Penicillium roqueforti | |
4.2.3.9 | 0.0834 | - |
(2E,6E)-farnesyl diphosphate | mutant Y92A, pH 7.5, temperature not specified in the publication | Penicillium roqueforti |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.3.9 | Penicillium roqueforti | - |
- |
- |
4.2.3.9 | Penicillium roqueforti | Q03471 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.2.3.9 | mutant enzyme Y92C and Y92A | Penicillium roqueforti |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.3.9 | (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 | ? | |
4.2.3.9 | 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 | ? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.3.9 | 0.00049 | - |
(2E,6E)-farnesyl diphosphate | mutant Y92C, pH 7.5, temperature not specified in the publication | Penicillium roqueforti | |
4.2.3.9 | 0.000491 | - |
trans,trans-farnesyl diphosphate | pH 7.5, mutant enzyme Y92C | Penicillium roqueforti | |
4.2.3.9 | 0.00137 | - |
trans,trans-farnesyl diphosphate | pH 7.5, mutant enzyme Y92A | Penicillium roqueforti | |
4.2.3.9 | 0.0014 | - |
(2E,6E)-farnesyl diphosphate | mutant Y92A, pH 7.5, temperature not specified in the publication | Penicillium roqueforti | |
4.2.3.9 | 0.03 | - |
(2E,6E)-farnesyl diphosphate | wild-type, pH 7.5, temperature not specified in the publication | Penicillium roqueforti |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.3.9 | 0.01 | - |
(2E,6E)-farnesyl diphosphate | mutant Y92C, pH 7.5, temperature not specified in the publication | Penicillium roqueforti | |
4.2.3.9 | 0.016 | - |
(2E,6E)-farnesyl diphosphate | mutant Y92A, pH 7.5, temperature not specified in the publication | Penicillium roqueforti | |
4.2.3.9 | 13.04 | - |
(2E,6E)-farnesyl diphosphate | wild-type, pH 7.5, temperature not specified in the publication | Penicillium roqueforti |