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Entry M0194    5.4.2.8    phosphomannomutase/phosphoglucomutase

Next Step

Step 01

D-mannose 6-phosphate attacks the phosphorylated Ser108 in a nucleophilic substitution, resulting in phosphorylation of the 1 position.

GIF of Reaction Step M0194.stg01


Comment: Experimental determination of the mass of the enzyme by MALDI-TOF mass spectrometry is consistent with its assignment as a phosphoenzyme. Structural studies by X-ray crystallography have also revealed that Ser108 is phosphorylated [1], here depicted as Sep108.



Mechanisms

Bimolecular Nucleophilic Substitution

Mechanism Components

Overall Reactant Used
Bond Formation
Bond Cleavage
Enzyme-Substrate Bond Cleavage
Intermediate Formation

Amino acids involved in the reaction step.

Amino Acid Location of Function Activity Function
His329 Side Chain spectator Electrostatic Stabiliser
Polar Interaction
Arg247 Side Chain spectator Hydrogen Bond Donor
Electrostatic Stabiliser
His109 Side Chain spectator Hydrogen Bond Donor
Electrostatic Stabiliser
Sep108 Post-Translationally Modified Residue reactant Hydrogen Bond Acceptor
Nucleofuge
Lys118 Side Chain spectator Hydrogen Bond Donor
Electrostatic Stabiliser
Arg20 Side Chain spectator Hydrogen Bond Donor
Electrostatic Stabiliser

Metal Cofactors involved in Step 01

Metal Type Metal Identity Chain Activity Function
magnesium ZN 500 x spectator Increase Electrophilicity
Activator
Electrostatic Stabiliser

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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