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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 M0262 and M0265

These two reactions have a combined similarity of 0.53


M0262

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Comparison

M0265

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EC 4.2.3.6
trichodiene synthase
Serial Number EC 4.2.3.9
aristolochene synthase

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

right arrow

Image of trichodiene

Image of diphosphate

2-trans,6-trans-farnesyl diphosphate
C00448
CHEBI:175763
trichodiene
C01860
CHEBI:15861
diphosphate
C00013
CHEBI:33019
0.84

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

right arrow

Image of 5-epi-aristolochene

Image of diphosphate

2-trans,6-trans-farnesyl diphosphate
C00448
CHEBI:175763
5-epi-aristolochene
X00127
CHEBI:23925
diphosphate
C00013
CHEBI:33019

Catalytic CATH Codes

1.10.600.10

Catalytic CATH Codes

1.10.600.10

Active Site



0.5688

Active Site



Catalytic Residues

Type Number Chain Location of Function
Tyr 93 B Side Chain
Arg 182 B Side Chain
Lys 232 B Side Chain
Arg 304 B Side Chain
Tyr 305 B Side Chain
Thr 96 B Side Chain
Leu 97 B Side Chain
Asp 100 B Side Chain
0.619

Catalytic Residues

Type Number Chain Location of Function
Arg 264 A Side Chain
Arg 441 A Side Chain
Thr 401 A Main Chain Carbonyl
Thr 402 A Main Chain Carbonyl
Thr 403 A Side Chain
Tyr 527 A Side Chain
Asp 525 A Side Chain
Tyr 520 A Side Chain
Asp 444 A Side Chain
Trp 273 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
magnesium MG 701 B
magnesium MG 702 B
magnesium MG 703 B

Metal Cofactors

Type Het group Number Chain
magnesium MG 851 A
magnesium MG 852 A
magnesium MG 853 A

Reaction occurs across 6 steps

0.4761

Reaction occurs across 9 steps

Step 1
GIF of Reaction Step M0262.stg01

The binding of the substrate causes a conformation change in the active site, which promotes the elimination of the pyrophosphate.
0.33 Step 1
GIF of Reaction Step M0265.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.
Step 2
GIF of Reaction Step M0262.stg02

The pyrophosphate attacks the C3 cationic carbon in a nucleophilic addition reaction.
0 Step 2
GIF of Reaction Step M0265.stg02

The C10-C11 double bond initiates an electrophilic attack on the positive carbocation, forming the first cyclic intermediate.
Step 3
GIF of Reaction Step M0262.stg03

Intramolecular elimination of the pyrophosphate.
0 Step 3
GIF of Reaction Step M0265.stg03

Asp525 deprotonates the intermediate to produce germacrene.
Step 4
GIF of Reaction Step M0262.stg04

Intramolecular electrophilic addition across the C1-C6 bond to form the six-membered ring.
0 Step 4
GIF of Reaction Step M0265.stg04

Asp444 in the Asp444-Tyr520-Asp525 triad deprotonated Tyr520, which in turn deprotonates Asp525.
Step 5
GIF of Reaction Step M0262.stg05

Intramolecular electrophilic addition across the C10-C7 bond to form the five-membered ring.
0.3 Step 5
GIF of Reaction Step M0265.stg05

The C2-C3 double bond initiates an electrophilic addition to the C6 double bond, which deprotonates Tyr520, in turn deprotonating Asp444.
Step 6
GIF of Reaction Step M0262.stg06

The Pyrophosphate deprotonates the substrate, which initiates the first methyl migration, followed by a second methyl migration and finally a 1,4-hydride shift.
0.21 Step 6
GIF of Reaction Step M0265.stg06

The C2 hydride migrates to the C3.
Step 7
No Step with this number present
N/A Step 7
GIF of Reaction Step M0265.stg07

The C14 methyl migrates to the planar C2 carbocation.
Step 8
No Step with this number present
N/A Step 8
GIF of Reaction Step M0265.stg08

Trp273 deprotonates the reactive intermediate, producing the final product.
Step 9
No Step with this number present
N/A Step 9
GIF of Reaction Step M0265.stg09

Trp273 is deprotonated in order to renegerate the active state of the enzyme.

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