MG_438_MONOMER_MODIFICATION_007 – protein threonine phosphorylation

Name
WID MG_438_MONOMER_MODIFICATION_007 View in model
Name protein threonine phosphorylation View in model
Cross references EC: 2.7.11.1 , BioCyc: PROTEIN-KINASE-RXN
 
Classification
Type adduction View in model
 
Reaction
Stoichiometry [c]: ATP + THR ⇒ ADP + H + pTHR View in model
Modification (364) MG_438_MONOMER [c] View in model
 
Catalysis
Enzyme MG_109_DIMER [m] View in model
 
Energetics
Is spontaneous (pH 7.5, 25C, I = 0) False View in model
 
Kinetics
Forward kinetics Vmax = 2.56 1/min View in model
 
Associations
Process Process_ProteinModification View in model
 
Comments
Comments Phosphorylation identified in genome-scale screen by Su et al [PUB_0094]. Of the multiple residues consistent with the mass-spec data, we assigned the phosphorylation to the most conserved residue as determined by ClustalW multiple sequence alignment.Kinetic rate of protein phosphorylation was measured by Fan, Fromm, and Bobik [PUB_0289].
References

  1. Fan C, Fromm HJ, Bobik TA. Kinetic and functional analysis of L-threonine kinase, the PduX enzyme of Salmonella enterica. J Biol Chem 284, 20240-8 (2009). WholeCell: PUB_0289, PubMed: 19509296

  2. Su HC, Hutchison CA 3rd, Giddings MC. Mapping phosphoproteins in Mycoplasma genitalium and Mycoplasma pneumoniae. BMC Microbiol 7, 63 (2007). WholeCell: PUB_0094, PubMed: 17605819
 
Metadata
Created 2012-10-01 15:08:44
Last updated 2012-10-01 15:17:01