Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Protein Class: a phosphatase-2A

Summary:
Protein phosphatase 2A (PP2A) removes the serine- or threonine-bound phosphate group from a wide range of phosphoproteins. The enzyme is very versatile owing to a large number of regulatory subunits and its ability to interact with numerous other proteins. The PP2A holoenzyme is a dimeric or trimeric protein built up from a catalytic subunit (PP2AC) (catalytic subunit of PP2A), a second constant regulatory subunit, and a third variable subunit. Three major classes of third subunits are currently described. Each of the three subunits of PP2A exists in at least two isoforms, thereby leading to a great variety of possible holoenzyme conformations, all with potential different substrate affinities and catalytic activities.

The common heterodimeric core of the human enzyme consists of PPP2CA, a 36 kDa catalytic subunit, and PPP2R1A, a 65 kDa constant regulatory subunit. The regulatory subunit exists as two closely related isoforms designated Aα and Aβ [Zhou03a]. The dimer can associate with a variety of additional regulatory subunits.

Credits:
Created 10-Apr-2011 by Caspi R , SRI International


References

Zhou03a: Zhou J, Pham HT, Ruediger R, Walter G (2003). "Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: differences in expression, subunit interaction, and evolution." Biochem J 369(Pt 2);387-98. PMID: 12370081


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, BIOCYC13B.