Homologous Superfamily

Pyruvate kinase-like domain superfamily (IPR040442)

Short name: Pyrv_Kinase-like_dom_sf

Overlapping entries


Pyruvate kinase controls the exit from the glysolysis pathway, catalysing the transfer of phosphate from phosphooenolpyruvate (PEP) to ADP. Mammalian pyruvate kinase is a homotetramer, where each polypeptide subunit consists of four domains: N-terminal, A domain, B domain and C-terminal. Activation of the enzyme is believed to occur via the clamping down of the B domain onto the A domain to dehydrate the active site cleft. The N- and C-terminal domains are situated at inter-subunit contact sites, and could be involved in assembly and communication within the complex. The N-terminal domain has a TIM beta/alpha-barrel structure [PMID: 11563914].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.