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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 M0141 and M0103

These two reactions have a combined similarity of 0.31


M0141

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Comparison

M0103

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EC 1.17.99.1
4-cresol dehydrogenase (hydroxylating)
Sub-Class EC 1.1.3.38
vanillyl-alcohol oxidase

Image of acceptor

Image of 4-cresol

Image of water

right arrow

Image of proton

Image of 4-hydroxybenzaldehyde

Image of reduced acceptor

2 acceptor
C00028
CHEBI:17654
4-cresol
C01468
CHEBI:17847
water
C00001
CHEBI:15377
4 proton
C00080
CHEBI:24636
4-hydroxybenzaldehyde
C00633
CHEBI:17597
2 reduced acceptor
C00030
0.36

Image of oxygen

Image of water

Image of 4-(methoxymethyl)phenol

right arrow

Image of 4-hydroxybenzaldehyde

Image of hydrogen peroxide

Image of methanol

oxygen
C00007
CHEBI:15379
water
C00001
CHEBI:15377
4-(methoxymethyl)phenol
X00032
4-hydroxybenzaldehyde
C00633
CHEBI:17597
hydrogen peroxide
C00027
CHEBI:16240
methanol
C00132
CHEBI:17790

Catalytic CATH Codes

3.40.462.10
3.30.465.10
1.10.45.10
1.10.760.10

Catalytic CATH Codes

3.30.43.10
3.30.465.10
3.40.462.10

Active Site



0.39573

Active Site



Catalytic Residues

Type Number Chain Location of Function
Asp 167 A Side Chain
Glu 177 A Side Chain
Glu 286 A Side Chain
Tyr 367 A Side Chain
Glu 380 A Side Chain
Tyr 384 A Side Chain
His 436 A Side Chain
Tyr 473 A Side Chain
Arg 474 A Side Chain
Arg 512 A Side Chain
Ala 649 C Main Chain Carbonyl
Met 650 C Side Chain
0.4347

Catalytic Residues

Type Number Chain Location of Function
Tyr 108 A Side Chain
Asp 170 A Side Chain
Tyr 503 A Side Chain
Arg 504 A Side Chain
His 422 A Side Chain

Organic Cofactors

Type Identity Chain
FAD FAD 599 A

Organic Cofactors

Type Identity Chain
FAD FAD 600 A

Metal Cofactors

Type Het group Number Chain
iron HEM 699 C

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 11 steps

0.2784

Reaction occurs across 8 steps

Step 1
GIF of Reaction Step M0141.stg01

Proton relay from bulk solvent through Glu177, His436 and Tyr473 to the substrate 4-cresol, resulting in a hydride transfer from the 4-cresol to the cofactor FAD599.
0.11 Step 1
GIF of Reaction Step M0103.stg01

Asp170 deprotonates the 4-OH of the substrate, forming a pheonlate.
Step 2
GIF of Reaction Step M0141.stg02

Glu380 deprotonates water, activating it for a nucleophilic addition to the creosol intermediate. This intermediate is re-protonated via the proton relay chain through Tyr473, His436 and Glu177 to bulk solvent.
0.25 Step 2
GIF of Reaction Step M0103.stg02

The oxyanion collapses with double bond rearrangement, eliminating a hydride from the 1-methoxy carbon, which is added to FAD.
Step 3
GIF of Reaction Step M0141.stg03

Glu380 is deprotonated through the proton relay chain of Tyr367, water, Glu286 and bulk solvent.
0 Step 3
GIF of Reaction Step M0103.stg03

The FAD undergoes double bond rearrangement which causes a single electron to be transferred to a dioxygen molecule.
Step 4
GIF of Reaction Step M0141.stg04

FAD599 loses a single electron through the Tyr384 covalently attached to the FAD, the main chain carbonyl of Ala649C, side chain of Met650C and the heme cofactor to the external electron acceptor.
0 Step 4
GIF of Reaction Step M0103.stg04

The dioxygen molecule undergoes a homolytic reaction in which it colligates to FAD, with concomitant deprotonation of Asp170.
Step 5
GIF of Reaction Step M0141.stg05

Glu380 deprotonates the activated FAD599, resulting in the second electron transfer through the Tyr384 covalently attached to the FAD, the main chain carbonyl of Ala649C, side chain of Met650C and the heme cofactor to the external electron acceptor.
0.75 Step 5
GIF of Reaction Step M0103.stg05

The peroxo group deprotonates FAD, which initiates the elimination of hydrogen peroxide.
Step 6
GIF of Reaction Step M0141.stg06

Glu380 is deprotonated through the proton relay chain of Tyr367, water, Glu286 and bulk solvent.
0.26 Step 6
GIF of Reaction Step M0103.stg06

Asp170 deprotonates water, which initiates a nucleophilic attack on the methoxy group, in a substitution reaction which eliminates methoxide.
Step 7
GIF of Reaction Step M0141.stg07

Glu380 deprotonates the intermediate, causing a reduction of the primary alcohol to an aldehyde with concomitant transfer of a hydride to FAD599.
0.33 Step 7
GIF of Reaction Step M0103.stg07

The methoxide deprotonates the alcohol group, initiating double bond rearrangement, which re-forms the phenolate moiety.
Step 8
GIF of Reaction Step M0141.stg08

Glu380 is deprotonated through the proton relay chain of Tyr367, water, Glu286 and bulk solvent.
0.28 Step 8
GIF of Reaction Step M0103.stg08

The pheonlate deprotonates Asp170.
Step 9
GIF of Reaction Step M0141.stg09

FAD599 loses a single electron through the Tyr384 covalently attached to the FAD, the main chain carbonyl of Ala649C, side chain of Met650C and the heme cofactor to the external electron acceptor.
N/A Step 9
No Step with this number present
Step 10
GIF of Reaction Step M0141.stg10

Glu380 deprotonates the activated FAD599, resulting in the second electron transfer through the Tyr384 covalently attached to the FAD, the main chain carbonyl of Ala649C, side chain of Met650C and the heme cofactor to the external electron acceptor.
N/A Step 10
No Step with this number present
Step 11
GIF of Reaction Step M0141.stg11

Glu380 is deprotonated through the proton relay chain of Tyr367, water, Glu286 and bulk solvent.
N/A Step 11
No Step with this number present

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