spacer

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 M0052 and M0252

These two reactions have a combined similarity of 0.43


M0052

View
Comparison

M0252

View
EC 4.1.2.13
fructose-bisphosphate aldolase (Class II)
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-fructosefuranose 1,6-bisphosphate

D-glyceraldehyde 3-phosphate
C00118
CHEBI:59776
glycerone phosphate
C00111
CHEBI:57642
D-fructosefuranose 1,6-bisphosphate
C00354
CHEBI:49299
0.24

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



0.2822

Active Site



Catalytic Residues

Type Number Chain Location of Function
Asp 109 A Side Chain
Glu 182 A Side Chain
Asn 286 A Side Chain
0.3

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

Type Het group Number Chain
zinc ZN 360 A
sodium NA 364 A

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 4 steps

0.5185

Reaction occurs across 5 steps

Step 1
GIF of Reaction Step M0052.stg01

Glu182 deprotonates the C1 carbon of the substrate, which initiates double bond rearrangement to form the enol-intermediate.
0.25 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 M0052.stg02

The oxyanion collapses, initiating nucleophilic addition of the intermediate to the glyceraldehyde-3-phosphate at the carbonyl carbon. The oxyanion formed deprotonates Asp109.
0.11 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 M0052.stg03

Asp109 deprotonates water which deprotonates Glu182 in an inferred step.
0.25 Step 3
GIF of Reaction Step M0252.stg03

In this inferred step, Lys110 deprotonates water.
Step 4
GIF of Reaction Step M0052.stg04

The sugar cyclises outside the enzyme active site.
0.09 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
No Step with this number present
N/A Step 5
GIF of Reaction Step M0252.stg05

In this inferred return step, water deprotonates Glu159 and Lys110 deprotonates water.

spacer
spacer