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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 M0236 and M0148

These two reactions have a combined similarity of 0.26


M0236

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Comparison

M0148

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EC 4.1.1.85
3-dehydro-L-gulonate-6-phosphate decarboxylase
Class EC 2.2.1.2
transaldolase

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
0.22

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



0.5575

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
0.6

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

Type Het group Number Chain
magnesium MG 5300 _

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 3 steps

0.1544

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 M0148.stg01

Initial activation of Lys132 in which Glu96 deprotonates a bound water that in turn deprotonates Lys132.
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).
0.4 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 M0236.stg03

An acid, assumed to be water, protonates His136.
0.2 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
No Step with this number present
N/A 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
No Step with this number present
N/A 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
No Step with this number present
N/A 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
No Step with this number present
N/A 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
No Step with this number present
N/A 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
No Step with this number present
N/A 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.

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