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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 M0251 and M0297

These two reactions have a combined similarity of 0.12


M0251

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Comparison

M0297

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EC 2.1.1.63
methylated-DNA--[protein]-cysteine S-methyltransferase
Class EC 4.99.1.2
alkylmercury lyase

Image of DNA containing 6-O-methylguanine

Image of Protein L-cysteine

right arrow

Image of DNA containing guanine

Image of Protein S-methyl-L-cysteine

DNA containing 6-O-methylguanine
C04250
Protein L-cysteine
C02743
CHEBI:32460
DNA containing guanine
C11475
CHEBI:61292
Protein S-methyl-L-cysteine
C03800
CHEBI:32648
0

Image of alkylmercury

Image of proton

right arrow

Image of alkane

Image of mercury(II)

Image of thiol

alkylmercury
C01343
2 proton
C00080
CHEBI:24636
alkane
C01371
CHEBI:18310
mercury(II)
C00703
CHEBI:16793
thiol
C00145
CHEBI:29256

Catalytic CATH Codes

1.10.10.10

Catalytic CATH Codes

0.0.0.0

Active Site



0.225

Active Site



Catalytic Residues

Type Number Chain Location of Function
Glu 172 A Side Chain
His 146 A Side Chain
Cys 145 A Side Chain
Tyr 114 A Side Chain
Asn 137 A Side Chain
0.25

Catalytic Residues

Type Number Chain Location of Function
Cys 96 A Side Chain
Asp 99 A Side Chain
Cys 159 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

No Associated Metal Cofactors

Metal Cofactors

Type Het group Number Chain
unknown No Available PDB Information

Reaction occurs across 1 steps

0.1034

Reaction occurs across 3 steps

Step 1
GIF of Reaction Step M0251.stg01

His146 deprotonates water, which in turn deprotonates Cys145. Cys145 then initiates a nucleophilic attack upon the methylated DNA in a substitution reaction. The DNA base then undergoes double bond rearrangement, resulting in the deprotonation of Tyr114.
0.11 Step 1
GIF of Reaction Step M0297.stg01

Asp99 acts as a general base towards Cys96, activating the thiol for nucleophilic attack at the mercury centre of the organomercury substrate.
Step 2
No Step with this number present
N/A Step 2
GIF of Reaction Step M0297.stg02

Almost immediately after Cys96 attacks the organomercury compound, substitution of the metal coordinated thiol group by Cys159 occurs with concomitant deprotonation of the attacking thiol by the departing group.
Step 3
No Step with this number present
N/A Step 3
GIF of Reaction Step M0297.stg03

The polarised carbon-mercury bond is cleaved and then protonated by the close proximity Asp99, generating an alkane.

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