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 M0222 and M0102

These two reactions have a combined similarity of 0.11


M0222

View
Comparison

M0102

View
EC 4.1.2.13
fructose-bisphosphate aldolase (Class I)
Class EC 1.1.2.3
L-lactate dehydrogenase (cytochrome)

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
0.09

Image of (S)-lactate

Image of ferricytochrome c

right arrow

Image of proton

Image of ferrocytochrome c

Image of pyruvate

(S)-lactate
C00186
CHEBI:16651
2 ferricytochrome c
C00125
CHEBI:16448
2 proton
C00080
CHEBI:24636
2 ferrocytochrome c
C00126
CHEBI:16707
pyruvate
C00022
CHEBI:15361

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.15754

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
0.1666

Catalytic Residues

Type Number Chain Location of Function
Tyr 254 A Side Chain
Asp 282 A Side Chain
His 373 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

Type Identity Chain
FMN FMN 570 A

Metal Cofactors

No Associated Metal Cofactors

Metal Cofactors

Type Het group Number Chain
iron HEM 560 A

Reaction occurs across 10 steps

0.1051

Reaction occurs across 6 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 M0102.stg01

His373 deprotonates the alcohol of the lactate which eliminates a hydride ion that is added to FAD.
Step 2
GIF of Reaction Step M0222.stg02

The oxyanion formed deprotonates the bound Lys229.
0 Step 2
GIF of Reaction Step M0102.stg02

A single electron is transferred from the FAD to the haem cofactor.
Step 3
GIF of Reaction Step M0222.stg03

Lys229 initiates an elimination of water, which gains an extra proton from Glu187.
0 Step 3
GIF of Reaction Step M0102.stg03

The haem cofactor transfers the electron to ferricytochrome c.
Step 4
GIF of Reaction Step M0222.stg04

The phosphate of the bound intermediate deprotonates water, which in turn deprotonates Tyr363.
0.22 Step 4
GIF of Reaction Step M0102.stg04

Water deprotonates the FAD, initiating the second single electron transfer from FAD to the haem cofactor.
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 Step 5
GIF of Reaction Step M0102.stg05

The haem cofactor transfers the electron to ferricytochrome c.
Step 6
GIF of Reaction Step M0222.stg06

Glu187 deprotonates water, which deprotonates a second water which deprotonates the phosphate of the bound intermediate.
0.17 Step 6
GIF of Reaction Step M0102.stg06

Water deprotonates His373 in an inferred return step.
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.
N/A Step 7
No Step with this number present
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.
N/A Step 8
No Step with this number present
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.
N/A Step 9
No Step with this number present
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

spacer
spacer