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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 M0055 and M0054

These two reactions have a combined similarity of 0.51


M0055

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Comparison

M0054

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EC 4.2.1.10
3-dehydroquinate dehydratase (type II)
EC 4.2.1.10
3-dehydroquinate dehydratase (type I)

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
1

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

3.40.50.9100

Catalytic CATH Codes

3.20.20.70

Active Site



0.13652

Active Site



Catalytic Residues

Type Number Chain Location of Function
Pro 15 A Main Chain Carbonyl
Asn 16 A Side Chain
Arg 23 A Side Chain
Tyr 28 A Side Chain
Asn 79 A Side Chain
Ala 82 A Main Chain Amide
Glu 104 A Side Chain
His 106 A Side Chain
Arg 113 A Side Chain
0.1428

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 3 steps

0.5936

Reaction occurs across 9 steps

Step 1
GIF of Reaction Step M0055.stg01

Tyr28 deprotonates the substrate, forming a double bond and causing the ketone group to reduce and deprotonate water, which in turn deprotonates Asn16.
0.3 Step 1
GIF of Reaction Step M0054.stg01

Glu86 deprotonates His143, which deprotonates Lys170, activating it.
Step 2
GIF of Reaction Step M0055.stg02

Asn16 deprotonates water, which deprotonates the C1-hydroxy, causing a double bond rearrangement that eliminates water with deprotonation of His106, which in turn deprotonates Glu104.
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 M0055.stg03

Glu104 deprotonates His106, which deprotonates water, which in turn deprotonates Tyr28 in an inferred step.
0.27 Step 3
GIF of Reaction Step M0054.stg03

A proton is transferred from the covalently attached lysine to the newly formed hydroxide.
Step 4
No Step with this number present
N/A 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
No Step with this number present
N/A 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
No Step with this number present
N/A 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
No Step with this number present
N/A 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
No Step with this number present
N/A 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
No Step with this number present
N/A 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.

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