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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 M0144 and M0208

These two reactions have a combined similarity of 0.15


M0144

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Comparison

M0208

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EC 1.20.98.1
arsenite oxidase
Sub-Class EC 1.10.2.2
ubiquinol-cytochrome-c reductase

Image of oxidised azurin

Image of water

Image of arsenite

right arrow

Image of proton

Image of reduced azurin

Image of arsenate

oxidised azurin
C05357
water
C00001
CHEBI:15377
arsenite
C06697
CHEBI:29243
2 proton
C00080
CHEBI:24636
reduced azurin
C05358
arsenate
C11215
CHEBI:48597
0.10

Image of Ubiquinone

Image of Ubiquinol

Image of Ferricytochrome c

right arrow

Image of Ubiquinone

Image of Proton

Image of Ubiquinol

Image of Ferrocytochrome c

Ubiquinone
C00399
CHEBI:16389
2 Ubiquinol
C00390
CHEBI:17976
2 Ferricytochrome c
C00125
CHEBI:15991
2 Ubiquinone
C00399
CHEBI:16389
2 Proton
C00080
CHEBI:24636
Ubiquinol
C00390
CHEBI:17976
2 Ferrocytochrome c
C00126
CHEBI:16928

Catalytic CATH Codes

3.40.228.10
2.102.10.10
0.0.0.0

Catalytic CATH Codes

1.20.810.10
2.102.10.10

Active Site



0.41994

Active Site



Catalytic Residues

Type Number Chain Location of Function
Cys 24 A Side Chain
Ser 98 A Main Chain Carbonyl
Ser 99 A Main Chain Amide
Ser 238 A Main Chain Carbonyl
His 62 B Side Chain
His 81 B Side Chain
0.4666

Catalytic Residues

Type Number Chain Location of Function
His 161 E Side Chain
Glu 272 C Side Chain
His 202 C Side Chain
Lys 228 C Side Chain
Asp 229 C Side Chain
Ser 206 C Side Chain

Organic Cofactors

Type Identity Chain
Molybdopterin guanosine dinucleotide MGD 5002

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
molybdenum 4MO 5004 x
iron FS3 5005 x
iron FES 5006 x

Metal Cofactors

Type Het group Number Chain
iron HEM 401 C
iron HEM 402 C
iron HEM 3 D
iron FES 4 E

Reaction occurs across 5 steps

0.0687

Reaction occurs across 7 steps

Step 1
GIF of Reaction Step M0144.stg01

Arsenic of the arsenite substrate attacks one of the molybdenum coordinating oxo groups, resulting in a Mo(VI) to Mo(IV) reduction.
0 Step 1
GIF of Reaction Step M0208.stg01

Glu272 deprotonates the quinol substrate. His161 (bound to a Rieske iron-sulfur cluster) deprotonates the second alcohol group. This initiates a single electron transfer to the Rieske iron-sulfur cluster forming the semi-quinone intermediate.
Step 2
GIF of Reaction Step M0144.stg02

The attacking oxo group forms a second bond to the arsenic, forming the product arsenate and resulting in the loss of the oxo group from the molybdenum complex and the remaining oxo group binding in a much stronger interaction.
0 Step 2
GIF of Reaction Step M0208.stg02

The alkoxide of the semi-quinone intermediate initiates a second single electron transfer (forming the first quinone product) through two heme groups to the quinone substrate, which initiates double bond rearrangement generating a semi-quinone intermediate
Step 3
GIF of Reaction Step M0144.stg03

An unidentified base activates water to attack the Mo(IV), forming a hydroxide group in place of the lost oxo group in a nucleophilic addition to the Mo(IV).
0.25 Step 3
GIF of Reaction Step M0208.stg03

Water deprotonates His161, which initiates a single electron transfer from the Rieske iron-sulfur complex to the heme group of cytochrome-c1. Concurrently, water deprotonates Glu272.
Step 4
GIF of Reaction Step M0144.stg04

A second unidentified base deprotonates the Mo-bound hydroxide, reforming the oxo group. This results in a single electron transfer through the pterin portion of the cofactor, main chain carbonyl of Ser238, thiolate of Cys24, an iron-sulfur cluster, the peptide bond of Ser99-Ser98, His62B, a second iron-sulfur complex and His81B and finally yields the electron to a bound azurin and resulting in Mo(V).
0.4 Step 4
GIF of Reaction Step M0208.stg04

Glu272 deprotonates the second quinol substrate. His161 (bound to a Rieske iron-sulfur cluster) deprotonates the second alcohol group. This initiates a single electron transfer to the Rieske iron-sulfur cluster forming the semi-quinone intermediate.
Step 5
GIF of Reaction Step M0144.stg05

The second single electron is transferred from Mo(V) through the pterin portion of the cofactor, main chain carbonyl of Ser238, thiolate of Cys24, an iron-sulfur cluster, the peptide bond of Ser99-Ser98, His62B, a second iron-sulfur complex and His81B and finally yields the electron to a bound azurin. This regenerates the enzyme's Mo(VI) oxidation state.
0 Step 5
GIF of Reaction Step M0208.stg05

The alkoxide of the second semi-quinone intermediate initiates a second single electron transfer (forming the second quinone product) through two heme groups to the semi-quinone substrate, which initiates double bond rearrangement generating the quinol product, that deprotonates Lys228 through a water molecule.
Step 6
No Step with this number present
N/A Step 6
GIF of Reaction Step M0208.stg06

Water deprotonates His161, which initiates a single electron transfer from the Rieske iron-sulfur complex to the heme group of cytochrome-c1. Concurrently, water deprotonates Glu272.
Step 7
No Step with this number present
N/A Step 7
GIF of Reaction Step M0208.stg07

Lys228 deprotonates water.

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