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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 M0148

These two reactions have a combined similarity of 0.75


M0222

View
Comparison

M0148

View
EC 4.1.2.13
fructose-bisphosphate aldolase (Class I)
Class EC 2.2.1.2
transaldolase

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
0.36

Image of D-erythrose 4-phosphate

Image of D-fructose 6-phosphate

right arrow

Image of D-glyceraldehyde 3-phosphate

Image of D-sedoheptulose 7-phosphate

D-erythrose 4-phosphate
C00279
CHEBI:16897
D-fructose 6-phosphate
C00085
CHEBI:57579
D-glyceraldehyde 3-phosphate
C00118
CHEBI:59776
D-sedoheptulose 7-phosphate
C05382
CHEBI:57483

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.4762

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
0.5

Catalytic Residues

Type Number Chain Location of Function
Asp 17 A Side Chain
Glu 96 A Side Chain
Lys 132 A Side Chain
Thr 156 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

0.9281

Reaction occurs across 9 steps

Step 1
GIF of Reaction Step M0222.stg01

Lys229 attacks the carbonyl carbon of D-glyceraldehyde 3- phosphate in a nucleophilic addition.
0 Step 1
GIF of Reaction Step M0148.stg01

Initial activation of Lys132 in which Glu96 deprotonates a bound water that in turn deprotonates Lys132.
Step 2
GIF of Reaction Step M0222.stg02

The oxyanion formed deprotonates the bound Lys229.
0.75 Step 2
GIF of Reaction Step M0148.stg02

Lys132 attacks the carbonyl carbon of D-fructose 6-phosphate in a nucleophilic addition. The generated oxyanion is reprotonated from water, which in turn deprotonates the now bound lysine
Step 3
GIF of Reaction Step M0222.stg03

Lys229 initiates an elimination of water, which gains an extra proton from Glu187.
0.75 Step 3
GIF of Reaction Step M0148.stg03

Lys132 initiates an elimination of the hydroxide group, which deprotonates the Glu96 to form water.
Step 4
GIF of Reaction Step M0222.stg04

The phosphate of the bound intermediate deprotonates water, which in turn deprotonates Tyr363.
0.5 Step 4
GIF of Reaction Step M0148.stg04

Asp17 deprotonates the hydroxide group gamma to the carbamylated carbon, initiating a bimolecular elimination of the product D-glyceraldehyde 3-phosphate from the covalently bound intermediate and resulting in a carbanion.
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.
0.5 Step 5
GIF of Reaction Step M0148.stg05

The carbanion undergoes an isomerisation in which the lone pair of electrons migrate to the nitrogen of Lys132.
Step 6
GIF of Reaction Step M0222.stg06

Glu187 deprotonates water, which deprotonates a second water which deprotonates the phosphate of the bound intermediate.
0.33 Step 6
GIF of Reaction Step M0148.stg06

The lysine-bound intermediate attacks the carbonyl carbon of the D-erythrose 4-phosphate substrate in a 1,4-nucleophilic addition. The formed oxyanion deprotonates Asp17.
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.
0.33 Step 7
GIF of Reaction Step M0148.stg07

Glu96 deprotonates a water molecule, which attacks the carbamylated carbon of the intermediate in a nucleophilic addition.
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.
0.33 Step 8
GIF of Reaction Step M0148.stg08

Lys132 deprotonates the bound water, initiating an elimination reaction that releases the D-sedoheptulose 7-phosphate product from the enzyme.
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.
0.75 Step 9
GIF of Reaction Step M0148.stg09

Regeneration of the active site in which the Lys132 deprotonates a bound water that in turn deprotonates Glu96.
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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