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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 M0237 and M0226

These two reactions have a combined similarity of 0.50


M0237

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Comparison

M0226

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EC 1.5.1.33
pteridine reductase
Class EC 3.13.1.1
UDP-sulfoquinovose synthase

Image of NADPH

Image of Biopterin

Image of Proton

right arrow

Image of NADP+

Image of Tetrahydrobiopterin

2 NADPH
C00005
CHEBI:16474
Biopterin
C06313
CHEBI:15373
2 Proton
C00080
CHEBI:24636
2 NADP+
C00006
CHEBI:18009
Tetrahydrobiopterin
C00272
CHEBI:52447
0

Image of Hydrogen sulfite

Image of UDP-glucose

right arrow

Image of UDP-6-sulfoquinovose

Image of Water

Hydrogen sulfite
C11481
CHEBI:17137
UDP-glucose
C00029
CHEBI:58885
UDP-6-sulfoquinovose
C11521
CHEBI:60009
Water
C00001
CHEBI:15377

Catalytic CATH Codes

3.40.50.720

Catalytic CATH Codes

3.40.50.720

Active Site



0.15852

Active Site



Catalytic Residues

Type Number Chain Location of Function
Arg 14 A Side Chain
Asp 161 A Side Chain
Tyr 174 A Side Chain
0.1428

Catalytic Residues

Type Number Chain Location of Function
Tyr 182 A Side Chain
Lys 186 A Side Chain
Thr 145 A Side Chain
His 183 A Side Chain
Ser 180 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

Type Identity Chain
NAD NAD 401 A

Metal Cofactors

No Associated Metal Cofactors

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 3 steps

0.7083

Reaction occurs across 4 steps

Step 1
GIF of Reaction Step M0237.stg01

NADPH transfers a hydride to the C7 position of biopterin. The N8 position is protonated by Tyr174, which in turn is protonated by Asp161. Since Asp161 is exposed to the bulk solvent it is then protonated by water.
0.57 Step 1
GIF of Reaction Step M0226.stg01

Tyr182 deprotonates the 4'-hydroxyl of UDP-glucose causing the formation of a ketone with concomitant hydride transfer from C4' of the substrate to C4 of NAD+.
Step 2
GIF of Reaction Step M0237.stg02

The dihydrobiopterin intermediate tautomerises.
0.25 Step 2
GIF of Reaction Step M0226.stg02

His183 deprotonates C5' of the intermediate and causes the elimination of the O6' hydroxyl group to form a C5'=C6' double bond.
Step 3
GIF of Reaction Step M0237.stg03

NADPH transfers a hydride to the C6 position of the dihydrobiopterin intermediate. The N5 position is protonated by an activated water. This water then deprotonates the 4-hydroxyl group and causes tautomerisation back to the keto-form.
0.27 Step 3
GIF of Reaction Step M0226.stg03

Sulfite is added across the double bond by electrophilic addition with His183 protonating the C5' position.
Step 4
No Step with this number present
N/A Step 4
GIF of Reaction Step M0226.stg04

NADH transfers a hydride from C4 of NADH to C4' of the intermediate. The resulting alkoxide is protonated by Tyr182.

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