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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 M0197 and M0279

These two reactions have a combined similarity of 0.05


M0197

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Comparison

M0279

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EC 6.1.1.1
tyrosine-tRNA ligase
Class EC 1.8.4.8
phosphoadenylyl-sulfate reductase (thioredoxin)

Image of L-tyrosine

Image of ATP

Image of tRNA(Tyr)

right arrow

Image of L-tyrosyl-tRNA(Tyr)

Image of AMP

Image of diphosphate

L-tyrosine
C00082
CHEBI:58315
ATP
C00002
CHEBI:30616
tRNA(Tyr)
C00787
CHEBI:29182
L-tyrosyl-tRNA(Tyr)
C02839
CHEBI:29161
AMP
C00020
CHEBI:456215
diphosphate
C00013
CHEBI:33019
0.2

Image of thioredoxin

Image of 3'-phosphoadenylyl sulfate

right arrow

Image of sulfite

Image of adenosine 3',5'-bisphosphate

Image of oxidised thioredoxin

thioredoxin
C00342
CHEBI:15967
3'-phosphoadenylyl sulfate
C00053
CHEBI:17980
sulfite
C00094
CHEBI:48854
adenosine 3',5'-bisphosphate
C00054
CHEBI:17985
oxidised thioredoxin
C00343
CHEBI:18191

Catalytic CATH Codes

3.40.50.620
1.10.240.10

Catalytic CATH Codes

3.40.50.620
0.0.0.0

Active Site



0

Active Site



Catalytic Residues

Type Number Chain Location of Function
Thr 40 A Side Chain
His 45 A Side Chain
His 48 A Side Chain
Lys 82 A Side Chain
Arg 86 A Side Chain
Gln 173 A Side Chain
Lys 230 A Side Chain
Lys 233 A Side Chain
Thr 234 A Side Chain
Asp 194 A Side Chain
0

Catalytic Residues

Type Number Chain Location of Function
Tyr 209 B Side Chain
Trp 204 B Side Chain
Cys 239 B Side Chain
Tyr 209 A Side Chain
Trp 204 A Side Chain
Cys 239 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
magnesium MG(not in PDB) 1 x

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 2 steps

0.0588

Reaction occurs across 5 steps

Step 1
GIF of Reaction Step M0197.stg01

The carboxylate group of the substrate L-tyrosine acts as a nucleophile and attacks the alpha-phosphate of the ATP in a substitution reaction that liberates pyrophosphate. Mg(II) and all catalytic residues stabilise the intermediates formed. Thr234 also affects the steric outcome of the reaction.
0 Step 1
GIF of Reaction Step M0279.stg01

Thioredoxin reduces the active site disulfide bridge.
Step 2
GIF of Reaction Step M0197.stg02

The phosphate of the tyrosine-AMP complex deprotonates the OH of the ribose ring, which acts as a nucleophile to attack the carbonyl group of the tyrosine in the tyrosine-AMP complex in a substitution reaction, liberating AMP. Mg(II), Thr40, His48, Lys82, Arg86 and Gln173 all stabilise the intermediates formed.
0 Step 2
GIF of Reaction Step M0279.stg02

Cys239' deprotonates the thioredoxin intermediate.
Step 3
No Step with this number present
N/A Step 3
GIF of Reaction Step M0279.stg03

The free thiol on Cys239 initiates nucleophilic attack at the substrate.
Step 4
No Step with this number present
N/A Step 4
GIF of Reaction Step M0279.stg04

The anionic phosphate leaving group accepts a proton from the covalently bound Cys239B.
Step 5
No Step with this number present
N/A Step 5
GIF of Reaction Step M0279.stg05

Cys239 attacks Cys239', eliminating sulfite with concomitant regeneration of the active site.

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