Properties of chicken skeletal muscle pyruvate kinase and a proposal for its evolutionary relation to the other avian and mammalian isoenzymes

Abstract

Pyruvate kinase (EC 2.7.1.40) was isolated and purified from chicken and turkey breast muscle with a purification procedure very similar to that used for the bovine skeletal muscle isozyme (Cardenas, J., Dyson, R., and strandholm, J. (1973), J. Biol. Chem. 248,6931). A study of the chemical and physical properties of the chicken enzyme revealed that it is a tetramer of four apparently identical subunits, closely resembling in this and most other respects the mamalian type 7 isozyme. The properties of these two enzymes are similar enough to permit subunits of chicken type M pyruvate kinase to combine with subunits of mammalian type L (one of the three mammalian isozymes) to form interspecies tetrameric hybrid isozymes in relative quantities that do not differ makedly from those formed when both the M and L isozymes are of mammalian origin. The similarity between the mammalian and avian type M pyruvates kinases suggests a close evolutionary relationship. Further comparisons among the three mammalian and two avian isozymes of pyruvate kinase are consistent with a common evolutionary origin, perhaps from an ancestral form of the type K isozyme, which is the only pyruvate kinase identified in mammalian and avian embryos.

Primary structure of chicken muscle pyruvate kinase mRNA.

“…Genetic studies suggest two structural genes: one coding for the M and K types and one coding for the L and R types (32,33). Only two isozymes have been observed in chickens: a fetal form and an adult skeletal muscle form (discussed in this paper), corresponding to the mammalian K and M types, respectively (18,27).…”

“…The molecular weight of chicken muscle PK estimated from the cDNA sequence is 57,865. Sedimentation equilibrium of the purified protein has given an estimated monomer molecular weight of 53,000 (27).…”

Pyruvate kinase: Function, regulation and role in cancer

“…The distribution of heterotetramer species obtained from these experiments is consistent with random assortment of individual PKM1 and PKL monomers into all possible heterotetramer species, which indicates a lack of binding preference between the isozymes. The high degree of conservation among vertebrate pyruvate kinase isoforms is further highlighted by the ability of chicken PKM1 to form functional heterotetramers with bovine PKL [47]. This ability to heterotetramerize may explain why most individual cells restrict expression to a single isoform to retain the allosteric regulatory properties of that isoform.…”

Immunohistological demonstration of pyruvate kinase isoenzyme type L in rat with monoclonal antibodies.

“…The pyruvate kinase isoenzymes were isolated according to Riou et al (1978) (LPK from rat liver), Cardenas et al (1975) (MI-PK from rat skeletal muscle), and (M2-PK from rat lung).…”