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Entry M0299    2.7.7.3    pantetheine-phosphate adenylyltransferase

Step 01

The phosphate group of pantetheine 4'-phosphate initiates a nucleophilic attack on the alpha phosphate group of ATP in a substitution reaction.

Rate Determining Step

GIF of Reaction Step M0299.stg01


Comment: The ATP adopts a strained conformation, as seen in the active sites of aminoacyl-tRNA synthetase enzymes. This raises the energy of the ground state towards that of the transition state, lowering the overall activation energy required for the reaction [1].



Mechanisms

Bimolecular Nucleophilic Substitution

Mechanism Components

Bond Cleavage
Bond Formation
Overall Reactant Used
Overall Product Formed
Enzyme Regenerated

Amino acids involved in the reaction step.

Amino Acid Location of Function Activity Function
Arg91 Side Chain spectator Attractive Charge Charge Interaction
Electrostatic Stabiliser
Lys42 Side Chain spectator Attractive Charge Charge Interaction
Electrostatic Stabiliser
His18 Side Chain spectator Hydrogen Bond Donor
Electrostatic Stabiliser
Ser129 Main Chain Amide spectator Hydrogen Bond Donor
Electrostatic Stabiliser

Metal Cofactors involved in Step 01

Metal Type Metal Identity Chain Activity Function
magnesium No Information available from the PDB spectator Substrate Binding
Electrostatic Stabiliser
Increase Electrophilicity
Activator

Reactive Centre

Bonds Formed Bonds Cleaved Bonds Changed in Order Atom Types Involved
P-O
P-O
None
O
P

View similar reactions in MACiE.


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