spacer

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 M0229 and M0197

These two reactions have a combined similarity of 0.33


M0229

View
Comparison

M0197

View
EC 6.3.2.1
pantoate-beta-alanine ligase
Sub-Class EC 6.1.1.1
tyrosine-tRNA ligase

Image of beta-Alanine

Image of ATP

Image of (R)-Pantoate

right arrow

Image of Pantothenate

Image of AMP

Image of diphosphate

beta-Alanine
C00099
CHEBI:57966
ATP
C00002
CHEBI:30616
(R)-Pantoate
C00522
CHEBI:15980
Pantothenate
C00864
CHEBI:29032
AMP
C00020
CHEBI:456215
diphosphate
C00013
CHEBI:33019
0.38

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

Catalytic CATH Codes

3.40.50.620
3.30.1300.10

Catalytic CATH Codes

3.40.50.620
1.10.240.10

Active Site



0.21037

Active Site



Catalytic Residues

Type Number Chain Location of Function
His 44 A Side Chain
His 47 A Side Chain
Ser 196 A Side Chain
Ser 197 A Side Chain
Arg 198 A Side Chain
0.2083

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

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
magnesium MG 1001 _

Metal Cofactors

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

Reaction occurs across 5 steps

0.375

Reaction occurs across 2 steps

Step 1
GIF of Reaction Step M0229.stg01

The carboxylate oxygen is involved in in-line nucleophilic attack on the alpha-phosphate of ATP to produce pyrophosphate and a pantoyl adenylate intermediate. The pyrophosphate is protonated by His147.
0.5 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.
Step 2
GIF of Reaction Step M0229.stg02

The phosphate group of the pantoyl adenylate forms a hydrogen-bond with the amine group of the beta-alanine substrate, deprotonating it to make the beta-alanine a better nucleophile
0.2 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.
Step 3
GIF of Reaction Step M0229.stg03

Beta-alanine initiates a nucleophilic attack on the carbonyl of the pantoyl adenylate intermediate to form a tetrahedral intermediate.
N/A Step 3
No Step with this number present
Step 4
GIF of Reaction Step M0229.stg04

The tetrahedral intermediate collapses to eliminate AMP and the product, pantothenate, which almost immediately dissociates from the active site.
N/A Step 4
No Step with this number present
Step 5
GIF of Reaction Step M0229.stg05

His47 deprotonates water in an inferred return step.
N/A Step 5
No Step with this number present

spacer
spacer