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Entry M0222    4.1.2.13    fructose-bisphosphate aldolase (Class I)

Previous Step

Step 10

Phosphate deprotonates hydroxyl, and the carbonyl oxygen re-protonates from Lys229, which in turn re-protonates from the phosphate, thus catalysing the ring closure of D-fructose 1,6-bisphosphate.

GIF of Reaction Step M0222.stg10


Comment: There is evidence in archea that the ring opening/closing reaction is enzyme catalysed by the Lys229. Phosphate deprotonates hydroxyl, and the carbonyl oxygen re-protonates from Lys229, which in turn re-protonates from the phosphate. [4]



Mechanisms

Proton Transfer
Intramolecular Nucleophilic Addition

Mechanism Components

Bond Formation
Bond Cleavage
Bond Order Change
Intermediate Terminated
Proton Relay
Overall Product Formed
Enzyme Regenerated
Cyclisation

Amino acids involved in the reaction step.

Amino Acid Location of Function Activity Function
Lys229 Side Chain reactant Hydrogen Bond Donor
Proton Acceptor
Hydrogen Bond Acceptor
Proton Donor
Proton Relay
Glu187 Side Chain spectator Electrostatic Stabiliser
Hydrogen Bond Donor
Polar Interaction
Glu189 Side Chain spectator Polar Interaction
Hydrogen Bond Acceptor
Electrostatic Stabiliser
Activator
Lys146 Side Chain spectator Hydrogen Bond Donor
Electrostatic Stabiliser
Ser300 Side Chain spectator Hydrogen Bond Acceptor
Hydrogen Bond Donor
Asp33 Side Chain spectator Hydrogen Bond Acceptor
Electrostatic Stabiliser
Tyr363 Side Chain spectator Not Active

Reactive Centre

Bonds Formed Bonds Cleaved Bonds Changed in Order Atom Types Involved
C-O
N-H
O-H
O-H
N-H
O-H
O-H
The C-O bond changes from a double to single bond
C
H
N
O

View similar reactions in MACiE.


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