spacer

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 M0063 and M0062

These two reactions have a combined similarity of 0.68


M0063

View
Comparison

M0062

View
EC 5.4.99.1
methylaspartate mutase
Serial Number EC 5.4.99.2
methylmalonyl-CoA mutase

Image of L-glutamate

right arrow

Image of  L-threo-3-methylaspartate

L-glutamate
C00025
CHEBI:29988
L-threo-3-methylaspartate
C03618
CHEBI:16378
0.75

Image of succinyl-CoA

right arrow

Image of (R)-2-methyl-3-oxopropanoyl-CoA

succinyl-CoA
C00091
CHEBI:57292
(R)-2-methyl-3-oxopropanoyl-CoA
C01213
CHEBI:57327

Catalytic CATH Codes

3.40.50.280
3.20.20.240

Catalytic CATH Codes

3.20.20.240
3.40.50.280

Active Site



0.25713

Active Site



Catalytic Residues

Type Number Chain Location of Function
His 16 A Side Chain
Glu 171 B Side Chain
0.2857

Catalytic Residues

Type Number Chain Location of Function
Tyr 89 A Side Chain
His 244 A Side Chain
Lys 604 A Side Chain
Asp 608 A Side Chain
His 610 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
cobalt COB 800 A

Metal Cofactors

Type Het group Number Chain
cobalt B12 800 A

Reaction occurs across 6 steps

0.8333

Reaction occurs across 6 steps

Step 1
GIF of Reaction Step M0063.stg01

The Co(II)-C bond of the B12 cofactor undergoes homoloysis, forming the adenosyl radical and Co(I).
0 Step 1
GIF of Reaction Step M0062.stg01

The Co(II)-C bond of the B12 cofactor undergoes homoloysis, forming the adenosyl radical and Co(I).
Step 2
GIF of Reaction Step M0063.stg02

The adenosyl radical abstracts a hydrogen from the substrate.
1 Step 2
GIF of Reaction Step M0062.stg02

The adenosyl radical abstracts a hydrogen from the substrate.
Step 3
GIF of Reaction Step M0063.stg03

The substrate undergoes homolytic elimination producing prop-2-enoic acid and a glycyl radical with concomitant deprotonation of the positively charged amine of the glycyl radical by Glu171B.
0.33 Step 3
GIF of Reaction Step M0062.stg03

The substrate radical attacks its own carbonyl carbon, forcing the radical onto the oxygen, which deprotonates His244.
Step 4
GIF of Reaction Step M0063.stg04

The glycyl radical adds to the double bond of prop-2-enoic acid, forming the product radical with concomitant deprotonation of Glu171B by the glycyl amine.
0.33 Step 4
GIF of Reaction Step M0062.stg04

His244 deprotonates the oxygen, which causes radical rearrangement and the cleavage of the propane ring formed, the radical ends up on the newly formed CH2 branch.
Step 5
GIF of Reaction Step M0063.stg05

The substrate radical abstracts a hydrogen from the adenosine, re-forming the adenosyl radical.
1 Step 5
GIF of Reaction Step M0062.stg05

The substrate radical abstracts a hydrogen from the adenosine, re-forming the adenosyl radical.
Step 6
GIF of Reaction Step M0063.stg06

The adenosyl radical and Co(I) undergo colligation, reforming the B12 cofactor.
0 Step 6
GIF of Reaction Step M0062.stg06

The adenosyl radical and Co(I) undergo colligation, reforming the B12 cofactor.

spacer
spacer