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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 M0222 and M0252

These two reactions have a combined similarity of 0.40


M0222

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Comparison

M0252

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EC 4.1.2.13
fructose-bisphosphate aldolase (Class I)
Sub-SubClass EC 4.1.1.48
indole-3-glycerol-phosphate synthase

Image of D-glyceraldehyde 3- phosphate

Image of glycerone phosphate

right arrow

Image of D-fructose 1,6-bisphosphate

D-glyceraldehyde 3- phosphate
C00118
CHEBI:59776
glycerone phosphate
C00111
CHEBI:57642
D-fructose 1,6-bisphosphate
C00354
CHEBI:49299
0.26

Image of proton

Image of 1-(2-Carboxyphenylamino)-1'-deoxy-D-ribulose 5'-phosphate

right arrow

Image of carbon dioxide

Image of Indoleglycerol phosphate

Image of water

proton
C00080
CHEBI:24636
1-(2-Carboxyphenylamino)-1'-deoxy-D-ribulose 5'-phosphate
C01302
CHEBI:58613
carbon dioxide
C00011
CHEBI:16526
Indoleglycerol phosphate
C03506
CHEBI:18299
water
C00001
CHEBI:15377

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.675

Active Site



Catalytic Residues

Type Number Chain Location of Function
Lys 146 A Side Chain
Ser 300 A Side Chain
Tyr 363 A Side Chain
Asp 33 A Side Chain
Lys 229 A Side Chain
Glu 187 A Side Chain
Glu 189 A Side Chain
0.75

Catalytic Residues

Type Number Chain Location of Function
Lys 53 A Side Chain
Glu 51 A Side Chain
Lys 110 A Side Chain
Glu 159 A Side Chain
Asn 180 A Side Chain
Ser 211 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

No Associated Metal Cofactors

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 10 steps

0.3233

Reaction occurs across 5 steps

Step 1
GIF of Reaction Step M0222.stg01

Lys229 attacks the carbonyl carbon of D-glyceraldehyde 3- phosphate in a nucleophilic addition.
0.14 Step 1
GIF of Reaction Step M0252.stg01

The nitrogen in the substrate initiates a double bond rearrangement which results in the cyclisation of the intermediate, and deprotonation of Lys110.
Step 2
GIF of Reaction Step M0222.stg02

The oxyanion formed deprotonates the bound Lys229.
0 Step 2
GIF of Reaction Step M0252.stg02

The carboxylic acid group undergoes elimination from the substrate resulting indecarboxylation.
Step 3
GIF of Reaction Step M0222.stg03

Lys229 initiates an elimination of water, which gains an extra proton from Glu187.
0.2 Step 3
GIF of Reaction Step M0252.stg03

In this inferred step, Lys110 deprotonates water.
Step 4
GIF of Reaction Step M0222.stg04

The phosphate of the bound intermediate deprotonates water, which in turn deprotonates Tyr363.
0.33 Step 4
GIF of Reaction Step M0252.stg04

Glu159 deprotonates the carbon alpha to the nitrogen in the newly formed ring, initiating the elimination of water and the deprotonation of Lys110.
Step 5
GIF of Reaction Step M0222.stg05

Tyr363 deprotonates the C1-H of the bound intermediate, initiating a double bond rearrangement that leaves Lys229 with a lone pair of electrons.
0.11 Step 5
GIF of Reaction Step M0252.stg05

In this inferred return step, water deprotonates Glu159 and Lys110 deprotonates water.
Step 6
GIF of Reaction Step M0222.stg06

Glu187 deprotonates water, which deprotonates a second water which deprotonates the phosphate of the bound intermediate.
N/A Step 6
No Step with this number present
Step 7
GIF of Reaction Step M0222.stg07

Glycerone phosphate binds, displacing one of the water molecules. Lys229 initiates a nucleophilic addition of the bound intermediate to the glycerone phosphate. The formed oxyanion deprotonates Glu187.
N/A Step 7
No Step with this number present
Step 8
GIF of Reaction Step M0222.stg08

Glu187 deprotonates water, which attacks the imine carbon of the covalenlty bound intermediate in a nucleophilic addition.
N/A Step 8
No Step with this number present
Step 9
GIF of Reaction Step M0222.stg09

Lys229 deprotonates the formed hydroxyl group, which initiates an elimination of the linear form of D-fructose 1,6-bisphosphate and neutral Lys229.
N/A Step 9
No Step with this number present
Step 10
GIF of Reaction Step M0222.stg10

Phosphate deprotonates hydroxyl, and the carbonyl oxygen re-protonates from Lys229, which in turn re-protonates from the phosphate, thus catalysing the ring closure of D-fructose 1,6-bisphosphate.
N/A Step 10
No Step with this number present

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