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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 M0243

These two reactions have a combined similarity of 0.30


M0223

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Comparison

M0243

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EC 6.4.1.1
pyruvate carboxylase
Class EC 2.6.99.2
pyridoxine 5'-phosphate 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
0.25

Image of 3-amino-2-oxopropyl phosphate

Image of 1-deoxy-D-xylulose 5-phosphate

right arrow

Image of pyridoxine 5'-phosphate

Image of phosphate

Image of water

3-amino-2-oxopropyl phosphate
C11638
1-deoxy-D-xylulose 5-phosphate
C11437
CHEBI:57792
pyridoxine 5'-phosphate
C00627
CHEBI:28803
phosphate
C00009
CHEBI:18367
2 water
C00001
CHEBI:15377

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.0084

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

Catalytic Residues

Type Number Chain Location of Function
His 12 A Side Chain
Arg 51 A Side Chain
Thr 103 A Side Chain
His 45 A Side Chain
Arg 47 A Side Chain
Glu 72 A Side Chain
Glu 153 A Side Chain
Asn 9 A Side Chain
His 193 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

No Associated Metal Cofactors

Reaction occurs across 7 steps

0.4339

Reaction occurs across 8 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
0.12 Step 1
GIF of Reaction Step M0243.stg01

The 3-amino-2-oxopropyl phosphate substrate initiates a nucleophilic attack upon the 1-deoxy-D-xylulose 5-phosphate in the first step of a Schiff base formation. The carbonyl oxygen is assumed to deprotonate the amine.
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.
0.09 Step 2
GIF of Reaction Step M0243.stg02

The newly formed secondary amine initiates a intramolecular elimination of water, which obtains its proton first from Glu72, and then from water.
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 Step 3
GIF of Reaction Step M0243.stg03

His45 deprotonates the C3 of the intermediate, which initiates double bond rearrangement, with the Schiff base acting as an electron sink.
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 M0243.stg04

The Schiff base reforms, initiating a double bond rearrangement and resulting in the elimination of water, which obtains it's proton from Glu72.
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.
0.25 Step 5
GIF of Reaction Step M0243.stg05

Glu72 deprotonates the remaining hydroxide, which initiates a double bond rearrangement and eliminates phosphate.
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.
0.37 Step 6
GIF of Reaction Step M0243.stg06

His12 activates water, which initiates a nucleophilic addition to the newly formed C=C. This causes ring closure, and the resulting oxyanion is protonated by His193. Glu72 is activated by a water molecule.
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 M0243.stg07

Glu72 deprotonates the C4 carbon, initiating the elimination of hydroxide, which obtains a proton from His12.
Step 8
No Step with this number present
N/A Step 8
GIF of Reaction Step M0243.stg08

His193 deprotonates C6, initiating a double bond rearrangement that results in the protonation of O3' by His45.

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