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http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2285| Título : | Dichotomic Phylogenetic Tree of the Pyruvate Kinase Family: k+ -Dependent and -Independent Enzymes. |
| Creador: | Oria Hernández J |
| Nivel de acceso: | Open access |
| Palabras clave : | Secuencia de Aminoácidos - genética - Conejos Sitios de Unión - genética - Conejos Biología Computacional - Métodos - Conejos Ácido Glutámico - Química - Conejos Lisina - Química - Conejos Datos de Secuencia Molecular - Conejos Familia de Multigenes - genética - Conejos Mutagénesis - Genética - Conejos Filogenia - Conejos Potasio - Química - Conejos Unión Proteica - genética - Conejos Piruvato Quinasa - química - Conejos Piruvato Quinasa - genética - Conejos Piruvato Quinasa - metabolismo - Conejos Amino Acid Sequence - Genetics - Rabbits Binding Sites - Genetics - Rabbits Computational Biology -methods - Rabbits Glutamic Acid - Chemistry - Rabbits Lysine - chemistry - Rabbits Molecular Sequence Data - Rabbits Multigene Family - Genetics - Rabbits Mutagenesis - Genetics - Rabbits Phylogeny - Rabbits Potassium - chemistry - Rabbits Protein Binding - Genetics - Rabbits Pyruvate Kinase - Chemistry - Rabbits Pyruvate Kinase - Genetics - Rabbits Pyruvate Kinase - Metabolism - Rabbits Piruvato Quinasa Isoenzimas conejos Filogenia genética Enlace Proteico Pyruvate Kinase Isoenzymes rabbits Phylogeny genetics Enlace Proteico |
| Descripción : | K+ dependence was assumed to be a feature of all pyruvate kinases until it was discovered that some enzymes express K+ -independent activity. Almost all the K+-independent pyruvate kinases have Lys at position 117, instead of the Glu present in the K+-dependent muscle enzyme. Mutagenesis studies show that the internal positive charge substitutes for the K+ requirement (Laughlin, L. T. & Reed, G. H. (1997) Arch. Biochem. Biophys. 348, 262–267). In this work a phylogenetic analysis of pyruvate kinase was performed to ascertain the abundance of K+ -independent activities and to explore whether the K+ activating effect is related to the evolutionary history of the enzyme. Of the 230 studied sequences, 46% have Lys at position 117, and the rest have Glu. Pyruvate kinases with Lys117 and Glu117 are separated in two clusters. All of the enzymes of the Glu117 cluster that have been characterized are K+-dependent, whereas those of the Lys117 cluster are K+-independent. Thus, there is a strict correlation between the dichotomy of the tree and the dependence of activity on K+. 77% of the pyruvate kinases that possess Lys117 have Lys113/Gln114; they also have Ile, Val, or Leu at position 120. These residues are replaced by Glu117 and Thr113/Lys114/Thr120 in 80% of K+-dependent pyruvate kinases. Structural analysis indicates that these residues are in a hinge region involved in the acquisition of the catalytic conformation of the enzyme. The route of conversion from K+-independent to K+-dependent pyruvate kinases is described. A plausible explanation of how enzymes developed K+ dependence is put forth. |
| Colaborador(es) u otros Autores: | Riveros-Rosas H Ramírez-Sílva L. |
| Fecha de publicación : | 2006 |
| Tipo de publicación: | Artículo |
| Formato: | |
| Identificador del Recurso : | 10.1074/jbc.M605310200 |
| Fuente: | J Biol Chem 281(41):30717-30724 |
| URI : | http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2285 |
| Idioma: | eng |
| Aparece en las colecciones: | Artículos |
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