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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 M0289 and M0116

These two reactions have a combined similarity of 0.18


M0289

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Comparison

M0116

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EC 2.2.1.6
acetolactate synthase
Class EC 1.6.1.2
NAD(P)+ transhydrogenase (AB-specific)

Image of pyruvate

Image of proton

right arrow

Image of carbon dioxide

Image of (S)-2-acetolactate

2 pyruvate
C00022
CHEBI:15361
proton
C00080
CHEBI:15378
CHEBI:24636
carbon dioxide
C00011
CHEBI:16526
(S)-2-acetolactate
C06010
CHEBI:18409
0

Image of NADP

Image of NADH

right arrow

Image of NADPH

Image of NAD

NADP
C00006
CHEBI:18009
NADH
C00004
CHEBI:16908
NADPH
C00005
CHEBI:16474
NAD
C00003
CHEBI:15846

Catalytic CATH Codes

3.40.50.970

Catalytic CATH Codes

3.40.50.720
3.40.50.1770
3.40.50.1220

Active Site



0

Active Site



Catalytic Residues

Type Number Chain Location of Function
Glu 139 A Side Chain
Lys 251 A Side Chain
Gln 202 A Side Chain
Met 582 B Side Chain
0

Catalytic Residues

Type Number Chain Location of Function
Arg 127 A Side Chain
Asp 135 A Side Chain
Tyr 235 A Side Chain
Asp 132 C Side Chain

Organic Cofactors

Type Identity Chain
Thiamine diphosphate TPP 1702 B

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
magnesium MG 699 A

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 6 steps

0.2888

Reaction occurs across 3 steps

Step 1
GIF of Reaction Step M0289.stg01

A glutamate residue deprotonates the thiamine diphosphate cofactor at the N1 position. This initiates double bond rearrangement which results in the deprotonation of the N=CH-S group. This activates the cofactor towards electrophilic attack.
0.12 Step 1
GIF of Reaction Step M0116.stg01

Asp132C obtains a proton, causing a rearrangement of the active site.
Step 2
GIF of Reaction Step M0289.stg02

The carbanion of thiamine diphosphate initiates a nucleophilic attack on the carbonyl carbon of pyruvate in an addition reaction. The conjugated double bond system of the cofactor undergoes rearrangement which results in the deprotonation of the glutamate residue.
0.37 Step 2
GIF of Reaction Step M0116.stg02

NAD eliminates a hydride ion, which adds to NADP.
Step 3
GIF of Reaction Step M0289.stg03

The covalently bound pyruvate undergoes decarboxylation.
0 Step 3
GIF of Reaction Step M0116.stg03

Asp132C releases its proton.
Step 4
GIF of Reaction Step M0289.stg04

A second pyruvate molecule approaches the cofactor intermediate in a Si orientation and undergoes electrophilic addition at the carbonanion to give the S enantiomeric acetolacty l-ThDP.
N/A Step 4
No Step with this number present
Step 5
GIF of Reaction Step M0289.stg05

The acetolacty l-ThDP intermediate undergoes an intramolecular proton transfer with concurrent elimination of S-acetolactate.
N/A Step 5
No Step with this number present
Step 6
GIF of Reaction Step M0289.stg06

The TPP cofactor is regenerated by reprotonation of the C2 position.
N/A Step 6
No Step with this number present

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