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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 M0052 and M0236

These two reactions have a combined similarity of 0.40


M0052

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Comparison

M0236

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EC 4.1.2.13
fructose-bisphosphate aldolase (Class II)
Sub-SubClass EC 4.1.1.85
3-dehydro-L-gulonate-6-phosphate decarboxylase

Image of D-glyceraldehyde 3-phosphate

Image of glycerone phosphate

right arrow

Image of D-fructosefuranose 1,6-bisphosphate

D-glyceraldehyde 3-phosphate
C00118
CHEBI:59776
glycerone phosphate
C00111
CHEBI:57642
D-fructosefuranose 1,6-bisphosphate
C00354
CHEBI:49299
0.18

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

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.3752

Active Site



Catalytic Residues

Type Number Chain Location of Function
Asp 109 A Side Chain
Glu 182 A Side Chain
Asn 286 A Side Chain
0.4

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

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
zinc ZN 360 A
sodium NA 364 A

Metal Cofactors

Type Het group Number Chain
magnesium MG 5300 _

Reaction occurs across 4 steps

0.4444

Reaction occurs across 3 steps

Step 1
GIF of Reaction Step M0052.stg01

Glu182 deprotonates the C1 carbon of the substrate, which initiates double bond rearrangement to form the enol-intermediate.
0.33 Step 1
GIF of Reaction Step M0236.stg01

The substrate decarboxylates to form the 1,2-cis-enediolate intermediate and carbon dioxide.
Step 2
GIF of Reaction Step M0052.stg02

The oxyanion collapses, initiating nucleophilic addition of the intermediate to the glyceraldehyde-3-phosphate at the carbonyl carbon. The oxyanion formed deprotonates Asp109.
0.5 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).
Step 3
GIF of Reaction Step M0052.stg03

Asp109 deprotonates water which deprotonates Glu182 in an inferred step.
0.25 Step 3
GIF of Reaction Step M0236.stg03

An acid, assumed to be water, protonates His136.
Step 4
GIF of Reaction Step M0052.stg04

The sugar cyclises outside the enzyme active site.
N/A Step 4
No Step with this number present

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