Pyruvate-kinase isoenzymes from zygotic and microspore-derived embryos of Brassica napus

Planta ◽  
1992 ◽  
Vol 187 (2) ◽  
Author(s):  
RajenderS. Sangwan ◽  
DavidA. Gauthier ◽  
DavidH. Turpin ◽  
M.Keith Pomeroy ◽  
WilliamC. Plaxton
Keyword(s):  
Brassica Napus ◽  
Pyruvate Kinase ◽  
Pyruvate Kinase Isoenzymes

Effects of phenylalanine and alanine on the kinetics of bovine pyruvate kinase isoenzymes

Biochemistry ◽  
1975 ◽  
Vol 14 (18) ◽  
pp. 4041-4045 ◽  
Author(s):  
Janet M. Cardenas ◽  
J. Jeffrey Strandholm ◽  
Joan M. Miller
Keyword(s):  
Pyruvate Kinase ◽  
Pyruvate Kinase Isoenzymes ◽  
Kinetics Of

Pyruvate kinase isoenzymes in human serum.

1984 ◽  
Vol 30 (1) ◽  
pp. 111-113
Author(s):  
J L Ngo ◽  
K N Garratt ◽  
P Eversole ◽  
R A Orlando ◽  
K H Ibsen
Keyword(s):  
Human Serum ◽  
Pyruvate Kinase ◽  
Electrophoretic Mobility ◽  
Kinase Activity ◽  
Published Data ◽  
Healthy Individuals ◽  
Progressive Decrease ◽  
Pyruvate Kinase Activity ◽  
Pyruvate Kinase Isoenzymes

Abstract Pyruvate kinase activity in serum from presumably healthy individuals is labile, but can be maintained for a week when samples are stored frozen. Contrary to published data our electrophoretic and isoelectrofocusing studies with fresh sera show the presence of both K and M isoenzymes; the latter predominates. In freezer-stored serum the putative M isoenzyme showed a progressive decrease in pl value as well as a decreased electrophoretic mobility.

Phosphorylation is switch of L-type pyruvate kinase allostery

2010 ◽  
Vol 5 (2) ◽  
pp. 135-142 ◽  
Author(s):  
Ilona Faustova ◽  
Aleksei Kuznetsov ◽  
Erkki Juronen ◽  
Mart Loog ◽  
Jaak Järv
Keyword(s):  
Pyruvate Kinase ◽  
Hill Coefficient ◽  
Stoichiometric Ratio ◽  
Allosteric Enzyme ◽  
E Coli ◽  
Glycolysis Regulation ◽  
Regulatory Phosphorylation ◽  
Pyruvate Kinase Isoenzymes ◽  
Dependent Protein ◽  
The Hill

AbstractAmong four pyruvate kinase isoenzymes, M1, M2, R and L, only M1 is considered as a nonallosteric enzyme. However, here we show that the non-phosphorylated L-type pyruvate kinase (L-PK) is also a non-allosteric enzyme with respect to its substrate phosphoenolpyruvate (PEP). The allosteric catalytic properties of L-PK are switched on through phosphorylation by cAMP-dependent protein kinase. The non-phosphorylated enzyme was produced by expressing the rat L-PK in E. coli, as the bacterium does not have mammalian-type protein kinases. The resulting tetrameric protein was phosphorylated with a stoichiometric ratio of one mole of phosphate per one L-PK monomer. Activity of the phosphorylated enzyme was allosterically regulated by PEP with the Hill coefficient n=2.5. It was observed that allostery was engaged by phosphorylation of the first subunit in the tetrameric enzyme, while further phosphorylation only modulated this effect. The discovered switching between non-allosteric and allosteric forms of L-PK and the possibility of modulating the allostery by phosphorylation are important for understanding of the interrelationship between allostery and the regulatory phosphorylation in general, and may have implication for further analysis of glycolysis regulation in the liver.

Immunohistochemical localization of pyruvate kinase isoenzymes in chicken tissues

1979 ◽  
Vol 64 (2) ◽  
pp. 145-161 ◽  
Author(s):  
M. Reinacher ◽  
E. Eigenbrodt ◽  
Beate Schering ◽  
W. Schoner
Keyword(s):  
Pyruvate Kinase ◽  
Immunohistochemical Localization ◽  
Chicken Tissues ◽  
Pyruvate Kinase Isoenzymes
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