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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 M0130

These two reactions have a combined similarity of 0.12


M0144

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Comparison

M0130

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EC 1.20.98.1
arsenite oxidase
Sub-Class EC 1.14.12.12
naphthalene 1,2-dioxygenase

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

Image of naphthalene

Image of oxygen

Image of proton

Image of NADH

right arrow

Image of NAD

Image of cis-1,2-dihydronaphthalene-1,2-diol

naphthalene
C00829
CHEBI:16482
oxygen
C00007
CHEBI:15379
proton
C00080
CHEBI:24636
NADH
C00004
CHEBI:16908
NAD
C00003
CHEBI:15846
cis-1,2-dihydronaphthalene-1,2-diol
C04314
CHEBI:15561

Catalytic CATH Codes

3.40.228.10
2.102.10.10
0.0.0.0

Catalytic CATH Codes

2.102.10.10
3.90.380.10

Active Site



0.23994

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
0.2666

Catalytic Residues

Type Number Chain Location of Function
His 104 A Side Chain
Asp 205 E Side Chain
His 208 E Side Chain

Organic Cofactors

Type Identity Chain
Molybdopterin guanosine dinucleotide MGD 5002

Organic Cofactors

Type Identity Chain
FAD FAD 0

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 FES 451 A
iron FE 452 A
iron FE(not in PDB) 1 x
iron FE(not in PDB) 2 x

Reaction occurs across 5 steps

0.0937

Reaction occurs across 9 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 M0130.stg01

NAD initiates a hydride transfer to the FAD cofactor.
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 M0130.stg02

FAD undergoes a double bond rearrangement that results in the transfer of a single electron from the FAD to one of the iron-sulfur clusters. This then initiates an electron relay through a second iron-sulfur cluster to a third.
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).
0.33 Step 3
GIF of Reaction Step M0130.stg03

The electron is transferred from the final iron-sulfur cluster to a dioxygen molecule, which also accepts a second electron from another Fe(II) centre, and deprotonates a water molecule.
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 Step 4
GIF of Reaction Step M0130.stg04

The peroxo group attacks the naphthalene substrate in a nucleophilic addition that causes the double bond to attack the peroxo group, cleaving the O-O bond and forming the epoxide 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 M0130.stg05

The epoxide intermediate collapses in a heterolysis resulting in a carbocation and anioinc oxygen bound to the Fe(III) centre.
Step 6
No Step with this number present
N/A Step 6
GIF of Reaction Step M0130.stg06

The iron-bound hydroxide group attacks the carbocation in a coordination reaction.
Step 7
No Step with this number present
N/A Step 7
GIF of Reaction Step M0130.stg07

An unidentified base deprotonates the FAD, initiating a single electron transfer to the one of the iron-sulfur clusters. This then initiates an electron relay through a second iron-sulfur cluster to a third.
Step 8
No Step with this number present
N/A Step 8
GIF of Reaction Step M0130.stg08

The electron is transferred from the final iron-sulfur cluster to the Fe(III) centre
Step 9
No Step with this number present
N/A Step 9
GIF of Reaction Step M0130.stg09

The cis-1,2-dihydronaphthalene-1,2-diol product deprotonates a water molecule and de-coordinates from the Fe(II) centre.

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