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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 M0267

These two reactions have a combined similarity of 0.28


M0222

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Comparison

M0267

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EC 4.1.2.13
fructose-bisphosphate aldolase (Class I)
Sub-Class EC 4.2.1.52
dihydrodipicolinate 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
0.3

Image of L-aspartate beta semi aldehyde (hydrate)

Image of Pyruvate

right arrow

Image of (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid

Image of water

L-aspartate beta semi aldehyde (hydrate)
X00125
Pyruvate
C00022
CHEBI:15361
(4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid
X00126
2 water
C00001
CHEBI:15377

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.26693

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
0.2727

Catalytic Residues

Type Number Chain Location of Function
Lys 161 A Side Chain
Tyr 133 A Side Chain
Ile 203 A Main Chain Carbonyl

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

0.2869

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.
1 Step 1
GIF of Reaction Step M0267.stg01

Lys161 acts as a nucleophile towards the keto group of the pyruvate substrate, forming a covalently bound enzyme-substrate intermediate. The pyruvate is polarised by the presence of the main chain carbonyl of Ile203, increasing its electrophilicity.
Step 2
GIF of Reaction Step M0222.stg02

The oxyanion formed deprotonates the bound Lys229.
0.6 Step 2
GIF of Reaction Step M0267.stg02

Proton transfer activates Schiff base formation in the next reaction step.
Step 3
GIF of Reaction Step M0222.stg03

Lys229 initiates an elimination of water, which gains an extra proton from Glu187.
0.6 Step 3
GIF of Reaction Step M0267.stg03

Elimination of water results in Schiff base formation.
Step 4
GIF of Reaction Step M0222.stg04

The phosphate of the bound intermediate deprotonates water, which in turn deprotonates Tyr363.
0 Step 4
GIF of Reaction Step M0267.stg04

The covalently bound lysine abstracts a proton from the terminal carbon to form the ene tautomer.
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.
0.14 Step 5
GIF of Reaction Step M0267.stg05

L-aspartate semi aldehyde is thought to enter the active site in the hydrate form. It then undergoes reversible dehydration to form the protonated aldehyde form.
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 Step 6
GIF of Reaction Step M0267.stg06

The enamine tautomer of the Schiff base adds to the dehydrated L-aspartate semi aldehyde in a conjugate nucleophilic attack.
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 Step 7
GIF of Reaction Step M0267.stg07

A 6-exo-tet cyclisation (Baldwin's classification) occurs in the enzyme-substrate intermediate.
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 M0267.stg08

Proton transfer is mediated through Tyr133.
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.
0.11 Step 9
GIF of Reaction Step M0267.stg09

The product is formed and the active site is regenerated for further catalysis.
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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