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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 M0092

These two reactions have a combined similarity of 0.37


M0188

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Comparison

M0092

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EC 5.1.3.2
UDP-glucose 4-epimerase
Class EC 1.1.1.22
UDP-glucose 6-dehydrogenase

Image of UDP-galactose

right arrow

Image of UDP-glucose

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

Image of UDP-glucose

Image of water

Image of NAD

right arrow

Image of proton

Image of NADH

Image of UDP-glucuronate

UDP-glucose
C00029
CHEBI:58367
water
C00001
CHEBI:15377
2 NAD
C00003
CHEBI:18009
2 proton
C00080
CHEBI:24636
2 NADH
C00004
CHEBI:16908
UDP-glucuronate
C00167
CHEBI:17200

Catalytic CATH Codes

3.40.50.720

Catalytic CATH Codes

3.40.50.720
1.10.1040.10

Active Site



0.1125

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
0.125

Catalytic Residues

Type Number Chain Location of Function
Thr 118 A Side Chain
Glu 145 A Side Chain
Lys 204 A Side Chain
Asn 208 A Side Chain
Cys 260 A Side Chain
Asp 264 A Side Chain

Organic Cofactors

Type Identity Chain
NAD NAD 340

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

No Associated Metal Cofactors

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 2 steps

0.5272

Reaction occurs across 6 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.
0.71 Step 1
GIF of Reaction Step M0092.stg01

Asp264 deprotonates water, which deprotonated Lys204 which deprotonates the CH3OH group of UDP, which causes the elimination of a hydride which adds to NAD
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.
0.11 Step 2
GIF of Reaction Step M0092.stg02

Cys260 initiates a nucleophilic attack on the formed carbonyl carbon in an addition reaction.
Step 3
No Step with this number present
N/A Step 3
GIF of Reaction Step M0092.stg03

The oxyanion collapses, eliminating a second hydride, which adds to a second molecule of NAD.
Step 4
No Step with this number present
N/A Step 4
GIF of Reaction Step M0092.stg04

Glu145 deprotonates water, which initiates a nucleophilic attack on the carbonyl carbon of the covalently bound substrate.
Step 5
No Step with this number present
N/A Step 5
GIF of Reaction Step M0092.stg05

The oxyanion collapses, eliminating Cys260.
Step 6
No Step with this number present
N/A Step 6
GIF of Reaction Step M0092.stg06

In an inferred return step, two water molecules deprotonate Glu145 and Asp264.

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