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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 M0188 and M0110

These two reactions have a combined similarity of 0.27


M0188

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Comparison

M0110

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EC 5.1.3.2
UDP-glucose 4-epimerase
Class EC 1.4.3.3
D-amino-acid oxidase

Image of UDP-galactose

right arrow

Image of UDP-glucose

UDP-galactose
C00052
CHEBI:58439
UDP-glucose
C00029
CHEBI:58367
0

Image of D-amino acid

Image of oxygen

Image of water

right arrow

Image of ammonium

Image of 2-oxo acid

Image of hydrogen peroxide

D-amino acid
C00405
CHEBI:59871
oxygen
C00007
CHEBI:15379
water
C00001
CHEBI:15377
ammonium
C01342
CHEBI:28938
2-oxo acid
C00161
CHEBI:35179
hydrogen peroxide
C00027
CHEBI:16240

Catalytic CATH Codes

3.40.50.720

Catalytic CATH Codes

3.40.50.720

Active Site



0.2144

Active Site



Catalytic Residues

Type Number Chain Location of Function
Ser 124 A Side Chain
Tyr 149 A Side Chain
Lys 153 A Side Chain
0.2

Catalytic Residues

Type Number Chain Location of Function
Ser 1335 A Main Chain Carbonyl
Side Chain
Asn 1054 A Main Chain Amide
Main Chain Carbonyl
Gln 1339 A Main Chain Carbonyl

Organic Cofactors

Type Identity Chain
NAD NAD 340

Organic Cofactors

Type Identity Chain
FAD FAD 1363

Metal Cofactors

No Associated Metal Cofactors

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 2 steps

0.3448

Reaction occurs across 5 steps

Step 1
GIF of Reaction Step M0188.stg01

Tyr149 deprotonates the 4-hydroxide of the substrate, resulting in an elimination of the hydride from the C4 position. The hydride then attacks the NAD cofactor in a nucleophilic addition reaction.
0.46 Step 1
GIF of Reaction Step M0110.stg01

Water deprotonates Ser1335, which deprotonates the amine of the D-amino acid, eliminating a hydride ion, which adds to FAD.
Step 2
GIF of Reaction Step M0188.stg02

The intermediate undergoes a conformational change before the NAD initiates an elimination of the hydride back to the intermediate, which in turn deprotonates Tyr149.
0.22 Step 2
GIF of Reaction Step M0110.stg02

The FAD undergoes double bond rearrangement which causes a single electron to be transferred to a dioxygen molecule.
Step 3
No Step with this number present
N/A Step 3
GIF of Reaction Step M0110.stg03

The dioxygen molecule undergoes a homolytic reaction in which it colligates to FAD, with concomitant deprotonation of water.
Step 4
No Step with this number present
N/A Step 4
GIF of Reaction Step M0110.stg04

The peroxo group deprotonates FAD, which initiates the elimination of hydrogen peroxide.
Step 5
No Step with this number present
N/A Step 5
GIF of Reaction Step M0110.stg05

The product of the enzyme undergoes spontaneous hydrolysis outside of the active site to produce ammonium and the 2-oxo acid.

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