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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 M0223 and M0230

These two reactions have a combined similarity of 0.39


M0223

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Comparison

M0230

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EC 6.4.1.1
pyruvate carboxylase
Class EC 4.2.1.24
porphobilinogen synthase

Image of ATP

Image of bicarbonate

Image of pyruvate

right arrow

Image of proton

Image of oxaloacetate

Image of phosphate

Image of ADP

ATP
C00002
CHEBI:30616
bicarbonate
C00288
CHEBI:17544
pyruvate
C00022
CHEBI:15361
proton
C00080
CHEBI:24636
oxaloacetate
C00036
CHEBI:16452
phosphate
C00009
CHEBI:18367
ADP
C00008
CHEBI:456216
0.22

Image of 5-aminolevulinate

right arrow

Image of porphobilinogen

Image of water

2 5-aminolevulinate
C00430
CHEBI:12109
porphobilinogen
C00931
CHEBI:17381
2 water
C00001
CHEBI:15377

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.27123

Active Site



Catalytic Residues

Type Number Chain Location of Function
Asp 549 A Side Chain
Asp 655 A Side Chain
Lys 718 A Side Chain
0.2857

Catalytic Residues

Type Number Chain Location of Function
Lys 205 A Side Chain
Lys 260 A Side Chain

Organic Cofactors

Type Identity Chain
Biotin BTN 0

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
zinc ZN 1157 A
magnesium MG 1156 B
magnesium MG 1157 B

Metal Cofactors

Type Het group Number Chain
magnesium MG 1338 A
zinc No Available PDB Information

Reaction occurs across 7 steps

0.472

Reaction occurs across 16 steps

Step 1
GIF of Reaction Step M0223.stg01

Reaction occurs in the BC domain. The bicarbonate is deprotonated by an unidentified base. The activate bicarbonate then acts as a nucleophile and attacks the gamma-phosphate in a substitution reaction, liberating ADP. Mg(II) stabilises/activates the ATP
0 Step 1
GIF of Reaction Step M0230.stg01

The zinc activated water deprotonates Lys260, activating it for the first step in Schiff base formation.
Step 2
GIF of Reaction Step M0223.stg02

Reaction occurs in the BC domain. The phosphorylated bicarbonate undergoes a decarboxylation reaction (E1cb) to liberate carbon dioxide and phosphate.
0 Step 2
GIF of Reaction Step M0230.stg02

Lys260 initiates a nucleophilic attack at the substrate's C4 carbonyl carbon in the first step of Schiff base formation.
Step 3
GIF of Reaction Step M0223.stg03

Reaction occurs in the BC domain. The phosphate deprotonates one of the N-H groups of biotin with concomitant tautomerisation to produce an oxyanion.
0.5 Step 3
GIF of Reaction Step M0230.stg03

In a proton rearrangement, the newly formed oxyanion deprotonates the positively charged nitrogen of Lys260.
Step 4
GIF of Reaction Step M0223.stg04

Reaction occurs in the BC domain. The oxyanion re-forms the carbonyl group, causing the C=N bond of the activated biotin to add to the carbon dioxide in a nucleophilic manner.
0 Step 4
GIF of Reaction Step M0230.stg04

The long pair of Lys260 initiates the elimination of the hydroxyl group as water, with the extra proton being donated by the zinc activated water.
Step 5
GIF of Reaction Step M0223.stg05

Reaction occurs in the CT domain. The Asp549 deprotonates pyruvate, activating the pyruvate in a keto-enol tautomerisation.
0.2 Step 5
GIF of Reaction Step M0230.stg05

The zinc activated water deprotonates Lys205, activating it for the first step in Schiff base formation.
Step 6
GIF of Reaction Step M0223.stg06

Reaction occurs in the CT domain. The activated pyruvate attacks the carboxylated biotin in a nucleophilic substitution, producing the oxaloacetate product and activated biotin.
0.11 Step 6
GIF of Reaction Step M0230.stg06

Lys205 initiates a nucleophilic attack at the second substrate's C4 carbonyl carbon in the first step of Schiff base formation.
Step 7
GIF of Reaction Step M0223.stg07

Reaction occurs in the CT domain. Lys718 deprotonates the activated biotin, which in turn deprotonates Asp549, returning the enzyme to its ground state.
0 Step 7
GIF of Reaction Step M0230.stg07

In a proton rearrangement, the newly formed oxyanion deprotonates the positively charged nitrogen of Lys205.
Step 8
No Step with this number present
N/A Step 8
GIF of Reaction Step M0230.stg08

The long pair of Lys260 initiates the elimination of the hydroxyl group as water, with the extra proton being donated by the zinc activated water.
Step 9
No Step with this number present
N/A Step 9
GIF of Reaction Step M0230.stg09

Zinc activated water deprotonates the Lys205 bound intermediate at the C3 carbon, initiating a tautomerisation.
Step 10
No Step with this number present
N/A Step 10
GIF of Reaction Step M0230.stg10

The lone pair of Lys205 initiates a double bond rearrangement that results in a nucleophilic attack of the Lys205 bound intermediate upon the C4 carbonyl carbon of the Lys260 bound intermediate, forming the new C3-C4 double bond.
Step 11
No Step with this number present
N/A Step 11
GIF of Reaction Step M0230.stg11

The amine group of the Lys260 bound intermediate initiates an intramolecular nucleophilic attack upon the C4 of the Lys205 bound intermediate, which in turn deprotonates the zinc activated water.
Step 12
No Step with this number present
N/A Step 12
GIF of Reaction Step M0230.stg12

Zinc activated water deprotonates the intermediate, causing an elimination of Lys205.
Step 13
No Step with this number present
N/A Step 13
GIF of Reaction Step M0230.stg13

The covalently attached Lys260 deprotonates the zinc activated water.
Step 14
No Step with this number present
N/A Step 14
GIF of Reaction Step M0230.stg14

Zinc activated water deprotonates the intermediate, causing an elimination of Lys260.
Step 15
No Step with this number present
N/A Step 15
GIF of Reaction Step M0230.stg15

Lys260 deprotonates the intermediate causing a double bond rearrangement that results in the final, aromatic, product.
Step 16
No Step with this number present
N/A Step 16
GIF of Reaction Step M0230.stg16

Lys205 deprotonates the zinc activated water to regenerate the enzyme's starting state.

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