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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 M0270

These two reactions have a combined similarity of 0.30


M0223

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Comparison

M0270

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EC 6.4.1.1
pyruvate carboxylase
Class EC 5.1.3.1
ribulose-phosphate 3-epimerase

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

Image of D-Ribulose 5-phosphate

right arrow

Image of D-Xylulose 5-phosphate

D-Ribulose 5-phosphate
C00199
CHEBI:17363
D-Xylulose 5-phosphate
C00231
CHEBI:16332

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.59994

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
0.6666

Catalytic Residues

Type Number Chain Location of Function
Asp 178 A Side Chain
Asp 38 A Side Chain
Ser 11 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
zinc ZN 1224 A

Reaction occurs across 7 steps

0.2394

Reaction occurs across 3 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 M0270.stg01

Asp38 deprotonates the C3 of the substrate molecule, causing a rearrangement of the double bonds and the formation of the enolate form.
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.
0.2 Step 2
GIF of Reaction Step M0270.stg02

The enolate collapses back to the keto form with concomitant deprotonation of Asp178, forming the xylulose product.
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.
0.33 Step 3
GIF of Reaction Step M0270.stg03

Bulk solvent returns the two catalytic aspartate residues to their correct protonation states.
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.
N/A Step 4
No Step with this number present
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.
N/A Step 5
No Step with this number present
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.
N/A Step 6
No Step with this number present
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.
N/A Step 7
No Step with this number present

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