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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 M0267

These two reactions have a combined similarity of 0.46


M0223

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Comparison

M0267

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EC 6.4.1.1
pyruvate carboxylase
Class EC 4.2.1.52
dihydrodipicolinate 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 L-aspartate beta semi aldehyde (hydrate)

Image of Pyruvate

right arrow

Image of (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid

Image of water

L-aspartate beta semi aldehyde (hydrate)
X00125
Pyruvate
C00022
CHEBI:15361
(4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid
X00126
2 water
C00001
CHEBI:15377

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.14262

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
0.1428

Catalytic Residues

Type Number Chain Location of Function
Lys 161 A Side Chain
Tyr 133 A Side Chain
Ile 203 A Main Chain Carbonyl

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

No Associated Metal Cofactors

Reaction occurs across 7 steps

0.6235

Reaction occurs across 9 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
0.16 Step 1
GIF of Reaction Step M0267.stg01

Lys161 acts as a nucleophile towards the keto group of the pyruvate substrate, forming a covalently bound enzyme-substrate intermediate. The pyruvate is polarised by the presence of the main chain carbonyl of Ile203, increasing its electrophilicity.
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 M0267.stg02

Proton transfer activates Schiff base formation in the next reaction step.
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.
0.6 Step 3
GIF of Reaction Step M0267.stg03

Elimination of water results in Schiff base formation.
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.
0.14 Step 4
GIF of Reaction Step M0267.stg04

The covalently bound lysine abstracts a proton from the terminal carbon to form the ene tautomer.
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.
0.14 Step 5
GIF of Reaction Step M0267.stg05

L-aspartate semi aldehyde is thought to enter the active site in the hydrate form. It then undergoes reversible dehydration to form the protonated aldehyde form.
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.
0.5 Step 6
GIF of Reaction Step M0267.stg06

The enamine tautomer of the Schiff base adds to the dehydrated L-aspartate semi aldehyde in a conjugate nucleophilic attack.
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.
0.09 Step 7
GIF of Reaction Step M0267.stg07

A 6-exo-tet cyclisation (Baldwin's classification) occurs in the enzyme-substrate intermediate.
Step 8
No Step with this number present
N/A Step 8
GIF of Reaction Step M0267.stg08

Proton transfer is mediated through Tyr133.
Step 9
No Step with this number present
N/A Step 9
GIF of Reaction Step M0267.stg09

The product is formed and the active site is regenerated for further catalysis.

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