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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 M0149 and M0322

These two reactions have a combined similarity of 0.17


M0149

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Comparison

M0322

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EC 2.3.2.13
protein-glutamine gamma-glutamyltransferase
Class EC 1.1.3.9
galactose oxidiase

Image of protein glutamine

Image of protein lysine

right arrow

Image of protein N5-alkylglutamine

Image of ammonia

protein glutamine
C02583
CHEBI:32677
protein lysine
C02188
CHEBI:32568
protein N5-alkylglutamine
C03636
CHEBI:21844
ammonia
C00014
CHEBI:16134
0

Image of primary alcohol

Image of dioxygen

right arrow

Image of aldehyde

Image of hydrogen peroxide

primary alcohol
C00226
CHEBI:15734
dioxygen
C00007
CHEBI:15379
aldehyde
C00071
CHEBI:17478
hydrogen peroxide
C00027
CHEBI:16240

Catalytic CATH Codes

3.90.260.10
2.60.40.10

Catalytic CATH Codes

2.130.10.80
2.60.40.10

Active Site



0.51245

Active Site



Catalytic Residues

Type Number Chain Location of Function
Trp 279 A Side Chain
Cys 314 A Side Chain
Main Chain Amide
His 373 A Side Chain
Asp 396 A Side Chain
Tyr 560 A Side Chain
0.5555

Catalytic Residues

Type Number Chain Location of Function
Tyr 495 A Side Chain
His 581 A Side Chain
Tyr 272 A Side Chain
His 496 A Side Chain
Cys 228 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

No Associated Metal Cofactors

Metal Cofactors

Type Het group Number Chain
copper CU 700 A

Reaction occurs across 4 steps

0.0769

Reaction occurs across 7 steps

Step 1
GIF of Reaction Step M0149.stg01

The thiolate of Cys314 attacks the carbonyl carbon of the protein glutamine substrate. The formed oxyanion is stabilised through a H-bond with Trp279.
0 Step 1
GIF of Reaction Step M0322.stg01

The coordinated, anionic Tyr residue abstracts a proton from the coordinated primary alcohol substrate.
Step 2
GIF of Reaction Step M0149.stg02

The oxyanion initiates the elimination of ammonia, which achieves the correct protonation state through the deprotonation of His373.
0 Step 2
GIF of Reaction Step M0322.stg02

A radical is formed at the primary alcohol carbon.
Step 3
GIF of Reaction Step M0149.stg03

His373 deprotonates the substrate protein lysine, which attacks the carbonyl carbon of the cysteine-bound intermediate.
0 Step 3
GIF of Reaction Step M0322.stg03

One electron is transferred from the radical-anion alcohol to the Cu centre, reducing the metal from +2 to +1
Step 4
GIF of Reaction Step M0149.stg04

The oxyanion initiates the elimination of Cys314, producing the protein N5-alkylglutamine product and regenerating the enzyme's native state.
0 Step 4
GIF of Reaction Step M0322.stg04

Dioxygen forms a superoxide-radial anion on withdrawing an electron from the Cu centre, oxidising the metal to the +2 state.
Step 5
No Step with this number present
N/A Step 5
GIF of Reaction Step M0322.stg05

The oxide radical initiates homolytic hydrogen atom abstraction at Tyr272, regenerating the radical tyrosine ligand.
Step 6
No Step with this number present
N/A Step 6
GIF of Reaction Step M0322.stg06

The anionic peroxide abstracts a proton from Tyr495.
Step 7
No Step with this number present
N/A Step 7
GIF of Reaction Step M0322.stg07

Hydrogen peroxide is substituted from the Cu(II) coordination sphere by water.

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