Interactions between Large and Small Subunits of Different Acetohydroxyacid Synthase Isozymes of Escherichia coli
Autor: | Inna Belenky, Ze'ev Barak, Maria Vyazmensky, Yuri Zherdev, Alex Slutzker, David M. Chipman, Olga Kryukov |
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Rok vydání: | 2009 |
Předmět: |
Ketol-Acid Reductoisomerase
Biology medicine.disease_cause Biochemistry Isozyme Bacterial Proteins Holoenzymes Valine Catalytic Domain Escherichia coli medicine health care economics and organizations Sequence Deletion chemistry.chemical_classification Molecular mass Acetohydroxyacid synthase Escherichia coli Proteins Molecular biology Isoenzymes Molecular Weight Acetolactate Synthase Protein Subunits Enzyme chemistry |
Zdroj: | Biochemistry. 48:8731-8737 |
ISSN: | 1520-4995 0006-2960 |
Popis: | The large, catalytic subunits (LSUs; ilvB, ilvG and ilvI, respectively) of enterobacterial acetohydroxyacid synthases isozymes (AHAS I, II and III) have molecular weights approximately 60 kDa and are paralogous with a family of other thiamin diphosphate dependent enzymes. The small, regulatory subunits (SSUs) of AHAS I and AHAS III (ilvN and ilvH) are required for valine inhibition, but ilvN and ilvH can only confer valine sensitivity on their own LSUs. AHAS II is valine resistant. The LSUs have only approximately 15, < |
Databáze: | OpenAIRE |
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