Por favor, use este identificador para citar o enlazar este ítem: 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: PDF
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

Ficheros en este ítem:
No hay ficheros asociados a este ítem.


Los ítems de DSpace están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.