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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 M0243

These two reactions have a combined similarity of 0.52


M0222

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Comparison

M0243

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EC 4.1.2.13
fructose-bisphosphate aldolase (Class I)
Class EC 2.6.99.2
pyridoxine 5'-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
0.19

Image of 3-amino-2-oxopropyl phosphate

Image of 1-deoxy-D-xylulose 5-phosphate

right arrow

Image of pyridoxine 5'-phosphate

Image of phosphate

Image of water

3-amino-2-oxopropyl phosphate
C11638
1-deoxy-D-xylulose 5-phosphate
C11437
CHEBI:57792
pyridoxine 5'-phosphate
C00627
CHEBI:28803
phosphate
C00009
CHEBI:18367
2 water
C00001
CHEBI:15377

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.14542

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
0.1538

Catalytic Residues

Type Number Chain Location of Function
His 12 A Side Chain
Arg 51 A Side Chain
Thr 103 A Side Chain
His 45 A Side Chain
Arg 47 A Side Chain
Glu 72 A Side Chain
Glu 153 A Side Chain
Asn 9 A Side Chain
His 193 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

0.7252

Reaction occurs across 8 steps

Step 1
GIF of Reaction Step M0222.stg01

Lys229 attacks the carbonyl carbon of D-glyceraldehyde 3- phosphate in a nucleophilic addition.
0.5 Step 1
GIF of Reaction Step M0243.stg01

The 3-amino-2-oxopropyl phosphate substrate initiates a nucleophilic attack upon the 1-deoxy-D-xylulose 5-phosphate in the first step of a Schiff base formation. The carbonyl oxygen is assumed to deprotonate the amine.
Step 2
GIF of Reaction Step M0222.stg02

The oxyanion formed deprotonates the bound Lys229.
0.6 Step 2
GIF of Reaction Step M0243.stg02

The newly formed secondary amine initiates a intramolecular elimination of water, which obtains its proton first from Glu72, and then from water.
Step 3
GIF of Reaction Step M0222.stg03

Lys229 initiates an elimination of water, which gains an extra proton from Glu187.
0 Step 3
GIF of Reaction Step M0243.stg03

His45 deprotonates the C3 of the intermediate, which initiates double bond rearrangement, with the Schiff base acting as an electron sink.
Step 4
GIF of Reaction Step M0222.stg04

The phosphate of the bound intermediate deprotonates water, which in turn deprotonates Tyr363.
0.4 Step 4
GIF of Reaction Step M0243.stg04

The Schiff base reforms, initiating a double bond rearrangement and resulting in the elimination of water, which obtains it's proton from Glu72.
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.
0.25 Step 5
GIF of Reaction Step M0243.stg05

Glu72 deprotonates the remaining hydroxide, which initiates a double bond rearrangement and eliminates phosphate.
Step 6
GIF of Reaction Step M0222.stg06

Glu187 deprotonates water, which deprotonates a second water which deprotonates the phosphate of the bound intermediate.
0.6 Step 6
GIF of Reaction Step M0243.stg06

His12 activates water, which initiates a nucleophilic addition to the newly formed C=C. This causes ring closure, and the resulting oxyanion is protonated by His193. Glu72 is activated by a water molecule.
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.
0.16 Step 7
GIF of Reaction Step M0243.stg07

Glu72 deprotonates the C4 carbon, initiating the elimination of hydroxide, which obtains a proton from His12.
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.
0.2 Step 8
GIF of Reaction Step M0243.stg08

His193 deprotonates C6, initiating a double bond rearrangement that results in the protonation of O3' by His45.
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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