Genetic reconstruction and characterization of the recombinant transacylase (E2b) component of bovine branched-chain alpha-keto acid dehydrogenase complex. Implication of histidine 391 as an active site residue

Genetically altered transacylase (E2b) proteins of the bovine branched-chain alpha-keto acid dehydrogenase complex were overexpressed in Escherichia coli and characterized. Deletion by PstI or Bal31 digestion of the amino-terminal region of the inner-core domain (residues 175-421) beyond residue 209...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	The Journal of biological chemistry 1990-08, Vol.265 (22), p.13174-13180
Hauptverfasser:	GRIFFIN, T. A, CHUANG, D. T
Format:	Artikel
Sprache:	eng
Schlagworte:	2-oxoisovalerate dehydrogenase (lipoamide) 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) Acyltransferases - genetics Acyltransferases - isolation & purification Acyltransferases - metabolism Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Binding Sites Biological and medical sciences Blotting, Western Cattle Chromosome Deletion Cloning, Molecular Enzymes and enzyme inhibitors Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Genetic Vectors Histidine Hydrogen-Ion Concentration Ketone Oxidoreductases - genetics Ketone Oxidoreductases - metabolism Kinetics Molecular Sequence Data Molecular Weight Multienzyme Complexes - genetics Multienzyme Complexes - metabolism Mutation Oligonucleotide Probes Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Restriction Mapping Sequence Homology, Nucleic Acid transacylase Transferases
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!