spacer

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 M0236 and M0054

These two reactions have a combined similarity of 0.25


M0236

View
Comparison

M0054

View
EC 4.1.1.85
3-dehydro-L-gulonate-6-phosphate decarboxylase
Sub-Class EC 4.2.1.10
3-dehydroquinate dehydratase (type I)

Image of 3-Dehydro-L-gulonate 6-phosphate

Image of Proton

right arrow

Image of Carbon dioxide

Image of L-Xylulose 5-phosphate

3-Dehydro-L-gulonate 6-phosphate
C14899
CHEBI:49039
Proton
C00080
CHEBI:15378
CHEBI:24636
Carbon dioxide
C00011
CHEBI:16526
L-Xylulose 5-phosphate
C03291
CHEBI:16593
0

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



0.675

Active Site



Catalytic Residues

Type Number Chain Location of Function
Asp 67 B Side Chain
Glu 112 A Side Chain
Lys 64 A Side Chain
His 136 A Side Chain
0.75

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

Type Het group Number Chain
magnesium MG 5300 _

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 3 steps

0.1274

Reaction occurs across 9 steps

Step 1
GIF of Reaction Step M0236.stg01

The substrate decarboxylates to form the 1,2-cis-enediolate intermediate and carbon dioxide.
0 Step 1
GIF of Reaction Step M0054.stg01

Glu86 deprotonates His143, which deprotonates Lys170, activating it.
Step 2
GIF of Reaction Step M0236.stg02

The carbonyl of the intermediate reforms and the C1 position is protonated. This can occur at the si-face (involving the si-water and His136, shown here) or at the re-face (involving the re-water and Arg139).
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 M0236.stg03

An acid, assumed to be water, protonates His136.
0 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.

spacer
spacer