Structural highlights
Function
[KPYM_FELCA] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of cat-muscle pyoruvate kinase has been refined at a resolution of 2.6 A. The details of the structure permit interpretation of the original heavy-atom studies and give insight into the importance of conserved residues in pyruvate kinases and the allosteric behaviour of the enzyme. There are a small number of essential residues which determine the relative orientations of domains and the precise nature of intersubunit contacts. Arginine residues are particularly important.
Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A.,Allen SC, Muirhead H Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):499-504. PMID:15299671[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Allen SC, Muirhead H. Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A. Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):499-504. PMID:15299671 doi:10.1107/S0907444995016040
