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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 M0066 and M0305

These two reactions have a combined similarity of 0.63


M0066

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Comparison

M0305

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EC 2.6.1.21
D-alanine transaminase
Class EC 4.1.3.38
aminodeoxychorismate lyase

Image of D-glutamate

Image of pyruvate

right arrow

Image of 2-oxoglutarate

Image of D-alanine

D-glutamate
C00217
CHEBI:29986
pyruvate
C00022
CHEBI:15361
2-oxoglutarate
C00026
CHEBI:16810
D-alanine
C00133
CHEBI:57416
0.25

Image of 4-amino-4-deoxychorismate

right arrow

Image of 4-aminobenzoate

Image of pyruvate

4-amino-4-deoxychorismate
C11355
CHEBI:35181
4-aminobenzoate
C00568
CHEBI:17836
pyruvate
C00022
CHEBI:15361

Catalytic CATH Codes

3.30.470.10
3.20.10.10

Catalytic CATH Codes

3.30.470.10
3.20.10.10

Active Site



0.3985

Active Site



Catalytic Residues

Type Number Chain Location of Function
Tyr 31 A Side Chain
Lys 145 A Side Chain
Glu 177 A Side Chain
Leu 201 A Side Chain
0.4

Catalytic Residues

Type Number Chain Location of Function
Thr 38 A Side Chain
Lys 159 A Side Chain
Glu 193 A Side Chain

Organic Cofactors

Type Identity Chain
Pyridoxal 5'-phosphate PLP 285 A

Organic Cofactors

Type Identity Chain
Pyridoxal 5'-phosphate PLP 413 A

Metal Cofactors

No Associated Metal Cofactors

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 12 steps

0.7878

Reaction occurs across 6 steps

Step 1
GIF of Reaction Step M0066.stg01

The amine of the substrate L-glutamate attacks the PLP cofactor in a nucleophilic addition and the bound Lys145 deprotonates the newly attached amine.
1 Step 1
GIF of Reaction Step M0305.stg01

The amine of the substrate attacks the PLP cofactor in a nucleophilic addition and the bound Lys159 deprotonates the newly attached amine.
Step 2
GIF of Reaction Step M0066.stg02

The secondary amine that results from the initial attack initiates an elimination of the covalently bound lysine, resulting in free PLP and lysine in a neutral state.
1 Step 2
GIF of Reaction Step M0305.stg02

The secondary amine initiates an elimination of the covalently bound lysine, forming free PLP and lysine in a neutral state.
Step 3
GIF of Reaction Step M0066.stg03

Lys145 deprotonates the CH adjacent to the bound amine, resulting in double bond rearrangement as the PLP acts as an electron sink.
1 Step 3
GIF of Reaction Step M0305.stg03

Lys159 deprotonates the CH adjacent to the bound amine, resulting in double bond rearrangement with the PLP cofactor acting as an electron sink.
Step 4
GIF of Reaction Step M0066.stg04

The PLP feeds the electrons back, resulting in the C=C attached to the aromatic ring deprotonates Lys145.
0.6 Step 4
GIF of Reaction Step M0305.stg04

The PLP feeds the electrons back, resulting in the cleavage of the C-O attached to the aromatic ring and the C=C of the released substrate deprotonating Lys159.
Step 5
GIF of Reaction Step M0066.stg05

Lys145 deprotonates water, which initiates a nucleophilic attack on the carbon of the C=N group in an addition reaction.
0.33 Step 5
GIF of Reaction Step M0305.stg05

The amine of Lys159 attacks the PLP in a nucleophilic addition reaction, the secondary amine of the attached substrate reprotonates from the bound Lys159.
Step 6
GIF of Reaction Step M0066.stg06

The secondary amine deprotonates the attached hydroxyl group, initiating an elimination which releases 2-oxoglutarate.
0.2 Step 6
GIF of Reaction Step M0305.stg06

The secondary amine that results from the initial attack initiates an elimination of the covalently bound product, resulting in 4-aminobenzoate and the regenerated PLP cofactor
Step 7
GIF of Reaction Step M0066.stg07

The amine of PMP initiates a nucleophilic attack on the carbonyl carbon of pyruvate. The oxyanion deprotonates the newly formed secondary amine in the first step of a Schiff base formation.
N/A Step 7
No Step with this number present
Step 8
GIF of Reaction Step M0066.stg08

The secondary amine initiates an elimination, forming the Schiff base and releasing water with concomitant deprotonation of Lys145.
N/A Step 8
No Step with this number present
Step 9
GIF of Reaction Step M0066.stg09

Lys145 deprotonates the CH2 adjacent to the nitrogen, resulting in double bond rearrangement as the PLP acts as an electron sink.
N/A Step 9
No Step with this number present
Step 10
GIF of Reaction Step M0066.stg10

The PLP feeds the electrons back, the N+=C bond deprotonates Lys145.
N/A Step 10
No Step with this number present
Step 11
GIF of Reaction Step M0066.stg11

The amine of Lys145 attacks the PLP in a nucleophilic addition reaction, the secondary amine of the attached substrate reprotonates from the bound Lys145.
N/A Step 11
No Step with this number present
Step 12
GIF of Reaction Step M0066.stg12

The secondary amine that results from the initial attack initiates an elimination of the covalently bound product, resulting in alanine and the regenerated PLP cofactor.
N/A Step 12
No Step with this number present

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