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 M0102 and M0236

These two reactions have a combined similarity of 0.26


M0102

View
Comparison

M0236

View
EC 1.1.2.3
L-lactate dehydrogenase (cytochrome)
Class EC 4.1.1.85
3-dehydro-L-gulonate-6-phosphate decarboxylase

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
0.14

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



0.3738

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
0.4

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

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
magnesium MG 5300 _

Reaction occurs across 6 steps

0.2368

Reaction occurs across 3 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 M0236.stg01

The substrate decarboxylates to form the 1,2-cis-enediolate intermediate and carbon dioxide.
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 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 M0102.stg03

The haem cofactor transfers the electron to ferricytochrome c.
0 Step 3
GIF of Reaction Step M0236.stg03

An acid, assumed to be water, protonates His136.
Step 4
GIF of Reaction Step M0102.stg04

Water deprotonates the FAD, initiating the second single electron transfer from FAD to the haem cofactor.
N/A Step 4
No Step with this number present
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

spacer
spacer