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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 M0102 and M0052

These two reactions have a combined similarity of 0.14


M0102

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Comparison

M0052

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

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
0.09

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

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.18

Active Site



Catalytic Residues

Type Number Chain Location of Function
Tyr 254 A Side Chain
Asp 282 A Side Chain
His 373 A Side Chain
0.2

Catalytic Residues

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

Organic Cofactors

Type Identity Chain
FMN FMN 570 A

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
iron HEM 560 A

Metal Cofactors

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

Reaction occurs across 6 steps

0.1451

Reaction occurs across 4 steps

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.
0.14 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.
Step 2
GIF of Reaction Step M0102.stg02

A single electron is transferred from the FAD to the haem cofactor.
0.14 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.
Step 3
GIF of Reaction Step M0102.stg03

The haem cofactor transfers the electron to ferricytochrome c.
0 Step 3
GIF of Reaction Step M0052.stg03

Asp109 deprotonates water which deprotonates Glu182 in an inferred step.
Step 4
GIF of Reaction Step M0102.stg04

Water deprotonates the FAD, initiating the second single electron transfer from FAD to the haem cofactor.
0 Step 4
GIF of Reaction Step M0052.stg04

The sugar cyclises outside the enzyme active site.
Step 5
GIF of Reaction Step M0102.stg05

The haem cofactor transfers the electron to ferricytochrome c.
N/A Step 5
No Step with this number present
Step 6
GIF of Reaction Step M0102.stg06

Water deprotonates His373 in an inferred return step.
N/A Step 6
No Step with this number present

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