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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 M0102

These two reactions have a combined similarity of 0.26


M0223

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Comparison

M0102

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EC 6.4.1.1
pyruvate carboxylase
Class EC 1.1.2.3
L-lactate dehydrogenase (cytochrome)

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 (S)-lactate

Image of ferricytochrome c

right arrow

Image of proton

Image of ferrocytochrome c

Image of pyruvate

(S)-lactate
C00186
CHEBI:16651
2 ferricytochrome c
C00125
CHEBI:16448
2 proton
C00080
CHEBI:24636
2 ferrocytochrome c
C00126
CHEBI:16707
pyruvate
C00022
CHEBI:15361

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.29997

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
0.3333

Catalytic Residues

Type Number Chain Location of Function
Tyr 254 A Side Chain
Asp 282 A Side Chain
His 373 A Side Chain

Organic Cofactors

Type Identity Chain
Biotin BTN 0

Organic Cofactors

Type Identity Chain
FMN FMN 570 A

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
iron HEM 560 A

Reaction occurs across 7 steps

0.2588

Reaction occurs across 6 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
0.13 Step 1
GIF of Reaction Step M0102.stg01

His373 deprotonates the alcohol of the lactate which eliminates a hydride ion that is added to FAD.
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 M0102.stg02

A single electron is transferred from the FAD to the haem cofactor.
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 M0102.stg03

The haem cofactor transfers the electron to ferricytochrome c.
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 M0102.stg04

Water deprotonates the FAD, initiating the second single electron transfer from FAD to the haem cofactor.
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 Step 5
GIF of Reaction Step M0102.stg05

The haem cofactor transfers the electron to ferricytochrome c.
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.
0.25 Step 6
GIF of Reaction Step M0102.stg06

Water deprotonates His373 in an inferred return step.
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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