Abstract
In the allosteric aspartate transcarbamylase (ATCase) from the hyperthermophilic eubacterium Thermotoga maritima, the catalytic and regulatory functions, which in class B ATCases are carried out by specialized polypeptides, are combined on a single type of polypeptide assembled in trimers. The ATCases from T. maritima and Treponema denticola present intriguing similarities, suggesting horizontal gene transfer.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Allosteric Site
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Amino Acid Sequence
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Aspartate Carbamoyltransferase / chemistry*
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Aspartate Carbamoyltransferase / genetics
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Aspartate Carbamoyltransferase / metabolism
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Cloning, Molecular
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Gene Transfer, Horizontal
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Genes, Bacterial
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Molecular Sequence Data
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Protein Conformation
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Thermotoga maritima / enzymology*
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Thermotoga maritima / genetics
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Treponema / enzymology
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Treponema / genetics
Substances
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Recombinant Proteins
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Aspartate Carbamoyltransferase