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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 M0054

These two reactions have a combined similarity of 0.42


M0222

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Comparison

M0054

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EC 4.1.2.13
fructose-bisphosphate aldolase (Class I)
Sub-Class EC 4.2.1.10
3-dehydroquinate dehydratase (type I)

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
0.27

Image of 3-dehydroquinic acid

right arrow

Image of 3-dehydroshikimate

Image of water

3-dehydroquinic acid
C00944
CHEBI:17947
3-dehydroshikimate
C02637
CHEBI:30918
water
C00001
CHEBI:15377

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.3764

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
0.4

Catalytic Residues

Type Number Chain Location of Function
Glu 86 A Side Chain
His 143 A Side Chain
Lys 170 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

0.4695

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 M0054.stg01

Glu86 deprotonates His143, which deprotonates Lys170, activating it.
Step 2
GIF of Reaction Step M0222.stg02

The oxyanion formed deprotonates the bound Lys229.
0 Step 2
GIF of Reaction Step M0054.stg02

Lys170 attacks the carbonyl carbon of the substrate in a nucleophilic addition.
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 M0054.stg03

A proton is transferred from the covalently attached lysine to the newly formed hydroxide.
Step 4
GIF of Reaction Step M0222.stg04

The phosphate of the bound intermediate deprotonates water, which in turn deprotonates Tyr363.
0.28 Step 4
GIF of Reaction Step M0054.stg04

Lys170 initiates an elimination of water (which obtains its proton from His143, which deprotonates Glu86) forming the Schiff base intermediate.
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.
0.55 Step 5
GIF of Reaction Step M0054.stg05

Glu86 deprotonates His143, which deprotonates the intermediate at the carbon adjacent to the covalently bound lysine which acts as an electron sink.
Step 6
GIF of Reaction Step M0222.stg06

Glu187 deprotonates water, which deprotonates a second water which deprotonates the phosphate of the bound intermediate.
0.25 Step 6
GIF of Reaction Step M0054.stg06

Lys170 donates its lone pair of electrons back into the ring, initiating a double bond rearrangement and elimination of water, which obtains its proton from His143, which deprotonates Glu86.
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.
0.23 Step 7
GIF of Reaction Step M0054.stg07

Glu86 deprotonates His143, which deprotonates water, which then attacks the carbon to which Lys170 is covalently attached.
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.
0.14 Step 8
GIF of Reaction Step M0054.stg08

Lys170 deprotonates the hydroxide, which causes Lys170 to be eliminated and the product to be formed.
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.
0.33 Step 9
GIF of Reaction Step M0054.stg09

Lys170 deprotonates His143, which deprotonates Glu86 in an inferred step that returns the enzyme to its starting state.
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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