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| Titel eines Journals oder einer Zeitschrift: | Archives of Microbiology | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Verlag: | Springer Verlag | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Band: | 181 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Nummer des Zeitschriftenheftes oder des Kapitels: | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Seitenbereich: | S. 195-203 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Datum: | 2004 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Institutionen: | Biologie und Vorklinische Medizin > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Rainer Merkl | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Stichwörter / Keywords: | Amino Acid Sequence Chorismate Mutase/antagonists & inhibitors/chemistry/genetics/*metabolism Cloning, Molecular DNA, Bacterial/chemistry/isolation & purification Enzyme Inhibitors/pharmacology Enzyme Stability Genes, Bacterial Kinetics Models, Molecular Molecular Sequence Data Molecular Weight Phylogeny Protein Conformation Protein Subunits/physiology Recombinant Proteins/metabolism Research Support, Non-U.S. Gov't Sequence Alignment Sequence Analysis, DNA Sequence Homology, Amino Acid Thermus thermophilus/*enzymology/*genetics Tyrosine/*pharmacology | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Dewey-Dezimal-Klassifikation: | 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Status: | Veröffentlicht | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Begutachtet: | Ja, diese Version wurde begutachtet | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| An der Universität Regensburg entstanden: | Nein | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Dokumenten-ID: | 10913 |
Zusammenfassung
aroG, encoding the monofunctional chorismate mutase (TtCM) of the thermophilic gram-negative bacterium Thermus thermophilus, was cloned and its gene product characterized. TtCM was purified to homogeneity on an SDS polyacrylamide gel as a His-fusion protein with a deduced molecular mass of 15.8 kDa. The enzyme belongs to the rare group of AroH-type chorismate mutases which are mainly found in ...
Zusammenfassung
aroG, encoding the monofunctional chorismate mutase (TtCM) of the thermophilic gram-negative bacterium Thermus thermophilus, was cloned and its gene product characterized. TtCM was purified to homogeneity on an SDS polyacrylamide gel as a His-fusion protein with a deduced molecular mass of 15.8 kDa. The enzyme belongs to the rare group of AroH-type chorismate mutases which are mainly found in gram-positive bacteria of the Bacillus/ Clostridia group and have recently also been described for gram-negative organisms. The native molecular mass is consistent with a pseudo-alpha/beta barrel enzyme that is organized as a trimer. Comparison of the enzyme's structure with that of its mesophilic counterpart from Bacillus revealed an increase in hydrophilicity on the protein's surface, greater hydrophobicity in cavities within the protein, and greater restriction of conformational freedom, features that contribute to the thermal stability of this chorismate mutase. The kinetic data show Michaelis-Menten substrate saturation with a Km of 290 microM, and a kcat/ Km value of 180 s(-1) mM(-1). TtCM was inhibited by tyrosine with a Ki =34 microM, possibly in a competitive manner.
Metadaten zuletzt geändert: 29 Sep 2021 07:31
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