Abstract
Escherichia coli expresses two L-asparaginase (EC 3.5.1.1) isozymes: L-asparaginse I, which is a low affinity, cytoplasmic enzyme that is expressed constitutively, and L-asparaginase II, a high affinity periplasmic enzyme that is under complex co-transcriptional regulation by both Fnr and Crp. The distinct localisation and regulation of these enzymes suggest different roles. To define these roles, a set of isogenic mutants was constructed that lacked either or both enzymes. Evidence is provided that L-asparaginase II, in contrast to L-asparaginase I, can be used in the provision of an anaerobic electron acceptor when using a non-fermentable carbon source in the presence of excess nitrogen.
Keywords:
Anaerobic growth; Asparaginase; Escherichia coli; Isozymes.
Copyright © 2013. Published by Elsevier Inc.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anaerobiosis
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Asparaginase / genetics
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Asparaginase / physiology*
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Asparagine / metabolism
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Culture Media / metabolism
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Cyclic AMP / metabolism
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Cyclic AMP Receptor Protein / genetics
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Cyclic AMP Receptor Protein / metabolism
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Cytoplasm / enzymology
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Electron Transport
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli / physiology
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism
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Escherichia coli Proteins / physiology*
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Fumarates / metabolism
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Gene Expression Regulation, Bacterial
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Iron-Sulfur Proteins / genetics
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Iron-Sulfur Proteins / metabolism
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Isoenzymes / genetics
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Isoenzymes / physiology
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Nitrogen / metabolism
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Transcription, Genetic
Substances
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Culture Media
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Cyclic AMP Receptor Protein
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Escherichia coli Proteins
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FNR protein, E coli
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Fumarates
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Iron-Sulfur Proteins
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Isoenzymes
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crp protein, E coli
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Asparagine
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Cyclic AMP
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Asparaginase
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Nitrogen