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The two reactions compared are done so using a Tanimoto similarity score (for more information, please see the MACiE FAQ) for the bond changes only. The score maay range from 0 to 1 where 1 indicates that the two reactions are identical at the bond change level and 0 indicates that there are no bond changes in common.


Key

1.0-0.9 0.9-0.8 0.8-0.7 0.7-0.6 0.6-0.5 0.5-0.4 0.4-0.3 0.3-0.2 0.2-0.1 0.1-0.0 =0

Results for Comparison of M0089 and M0261

These two reactions have a combined similarity of 0.75


M0089

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Comparison

M0261

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EC 4.2.3.7
pentalenene synthase
Serial Number EC 4.2.3.9
aristolochene synthase

Image of 2-trans,6-trans-farnesyl diphosphate

right arrow

Image of proton

Image of pentalenene

Image of diphosphate

2-trans,6-trans-farnesyl diphosphate
C00448
CHEBI:175763
proton
C00080
CHEBI:24636
pentalenene
C01841
CHEBI:17251
diphosphate
C00013
CHEBI:18361
0.86

Image of 2-trans,6-trans-farnesyl diphosphate

right arrow

Image of aristolochene

Image of diphosphate

2-trans,6-trans-farnesyl diphosphate
C00448
CHEBI:175763
aristolochene
C02004
CHEBI:43445
diphosphate
C00013
CHEBI:33019

Catalytic CATH Codes

1.10.600.10

Catalytic CATH Codes

1.10.600.10

Active Site



0.52045

Active Site



Catalytic Residues

Type Number Chain Location of Function
Phe 76 A Side Chain
Phe 77 A Side Chain
Asn 219 A Side Chain
Trp 308 A Side Chain
His 309 A Side Chain
0.5555

Catalytic Residues

Type Number Chain Location of Function
Tyr 92 A Side Chain
Phe 112 A Side Chain
Phe 178 A Side Chain
Lys 206 A Side Chain
Trp 333 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
magnesium MG(not in PDB) 1 x

Metal Cofactors

Type Het group Number Chain
magnesium none1 0 none
magnesium none2 0 none
magnesium none3 0 none

Reaction occurs across 7 steps

0.8367

Reaction occurs across 5 steps

Step 1
GIF of Reaction Step M0089.stg01

The substrate undergoes heterolysis. The diphosphate product remains associated with the active site, and the cabocation is delocalised over the three terminal carbon atoms of the intermediate.
0.33 Step 1
GIF of Reaction Step M0261.stg01

The C10-C11 double bond initiates an electrophilic substitution at the C1, eliminating the diphosphate product.
Step 2
GIF of Reaction Step M0089.stg02

The terminal double bond adds to the terminal carbocation in an intramolecular electrophilic addition resulting in a cyclic intermediate.
0 Step 2
GIF of Reaction Step M0261.stg02

Lys206 deprotonates the C12, producing the neutral Germacrene A intermediate.
Step 3
GIF of Reaction Step M0089.stg03

His309 deprotonates the carbon adjacent to the newly formed carbocation, forming a new double bond in the humulene intermediate.
0 Step 3
GIF of Reaction Step M0261.stg03

The C2-C3 double bond initiates an electrophilic attack on the C7, which causes the protonation of C6 from Lys206 to form the Eudesmane cation intermediate.
Step 4
GIF of Reaction Step M0089.stg04

In a second intramolecular electrophilic addition, a double bond adds across the cycle forming a five membered ring and a new carbocation.
0.14 Step 4
GIF of Reaction Step M0261.stg04

Lys206 deprotonates the C8 carbon, which forms a double bond between C8 and C7. This initiates the migration of the C14 methyl from C7 to C8 and a migration of a hydride from C2 to C3 to form the Aristolochene product.
Step 5
GIF of Reaction Step M0089.stg05

In a third intramolecular electrophilic addition, the remaining double bond adds across the cycle to form the three five membered ring motif of pentalenene, this also causes a [1,2]-hydride shift and the carbocation shifting to a different carbon atom
0 Step 5
GIF of Reaction Step M0261.stg05

Bulk solvent deprotonates Lys206 in an inferred return step.
Step 6
GIF of Reaction Step M0089.stg06

His309 deprotonates the carbon adjacent to the new carbocation, forming the final double bond of pentalenene.
N/A Step 6
No Step with this number present
Step 7
GIF of Reaction Step M0089.stg07

Water deprotonates His309 in an inferred step to regenerate the enzyme active site.
N/A Step 7
No Step with this number present

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