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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 M0048 and M0214

These two reactions have a combined similarity of 0.17


M0048

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Comparison

M0214

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EC 2.4.2.8
hypoxanthine phosphoribosyltransferase
Serial Number EC 2.4.2.14
amidophosphoribosyltransferase

Image of 5-phospho-alpha-D-ribose-1-diphosphate

Image of guanine

right arrow

Image of proton

Image of diphosphate

Image of GMP

5-phospho-alpha-D-ribose-1-diphosphate
C00119
CHEBI:58017
guanine
C00242
CHEBI:16235
proton
C00080
CHEBI:24636
diphosphate
C00013
CHEBI:18361
GMP
C00144
CHEBI:58115
0.25

Image of L-Glutamine

Image of Water

Image of 5-Phospho-alpha-D-ribose-1-diphosphate

right arrow

Image of 5-Phosphoribosylamine

Image of L-Glutamate

Image of diphosphate

L-Glutamine
C00064
CHEBI:29988
Water
C00001
CHEBI:15377
5-Phospho-alpha-D-ribose-1-diphosphate
C00119
CHEBI:17111
5-Phosphoribosylamine
C03090
CHEBI:17284
L-Glutamate
C00025
CHEBI:29985
diphosphate
C00013
CHEBI:33019

Catalytic CATH Codes

3.40.50.2020

Catalytic CATH Codes

3.60.20.10

Active Site



0

Active Site



Catalytic Residues

Type Number Chain Location of Function
Glu 133 A Side Chain
Asp 134 A Side Chain
Asp 137 A Side Chain
0

Catalytic Residues

Type Number Chain Location of Function
Cys 1 A Main Chain N Terminus
Side Chain
Asn 101 A Side Chain
Gly 102 A Main Chain Amide
Gly 27 A Main Chain Carbonyl
Tyr 258 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
magnesium MG 900 A
magnesium MG 901 A

Metal Cofactors

Type Het group Number Chain
magnesium MN 506 A
iron No Available PDB Information

Reaction occurs across 2 steps

0.2285

Reaction occurs across 5 steps

Step 1
GIF of Reaction Step M0048.stg01

Asp137 deprotonates the guanine which initiates a nucleophilic attack upon the C2 of the ribose ring in a substitution reaction, eliminating diphosphate.
0.11 Step 1
GIF of Reaction Step M0214.stg01

The N-terminus of Cys1 deprotonates the thiol group of Cys1, which attacks the amino carbon in a nucleophilic addition.)ReactiveCentres=(N,H,O,H,S,C,O
Step 2
GIF of Reaction Step M0048.stg02

Water deprotonates Asp137 in an inferred return step.
0.33 Step 2
GIF of Reaction Step M0214.stg02

The oxyanion initiates an elimination that cleaves ammonia from the bound L-Glutamine substrate. Ammonia deprotonates the N-terminus of Cys1.
Step 3
No Step with this number present
N/A Step 3
GIF of Reaction Step M0214.stg03

The N-terminus of Cys1 deprotonates water, which attacks the carbonyl carbon of the covalently bound intermediate.
Step 4
No Step with this number present
N/A Step 4
GIF of Reaction Step M0214.stg04

The oxyanion initiates an elimination that cleaves the C-S bond, the thiolate of Cys1 deprotonates the N-terminus of Cys1
Step 5
No Step with this number present
N/A Step 5
GIF of Reaction Step M0214.stg05

Ammonia attacks the C1 of the 5-Phospho-alpha-D-ribose-1-diphosphate substrate in a nucleophilic substitution. The product pyrophosphate deprotonates the newly attached ammonia.

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