Aspartate Transcarbamoylase of Aeromonas Hydrophila

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This study focused on the enzyme, aspartate transcarbamoylase (ATCase) from A. hydrophila, a Gram-negative bacterium found in fresh water. The molecular mass of the ATCase holoenzyme from A. hydrophila is 310 kDa. The enzyme is likely composed of 6 catalytic polypeptides of 34 kDa each and 6 regulatory polypeptides of 17 kDa each. The velocity-substrate curve for A. hydrophila ATCase is sigmoidal for both aspartate and carbamoylphosphate. The Km for aspartate was the highest to date for an enteric bacterium at 97.18 mM. The Km for carbamoylphosphate was 1.18 mM. When heated to 60 ºC, the specific activity of the ... continued below

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Higginbotham, Leah December 2000.

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  • Higginbotham, Leah

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This study focused on the enzyme, aspartate transcarbamoylase (ATCase) from A. hydrophila, a Gram-negative bacterium found in fresh water. The molecular mass of the ATCase holoenzyme from A. hydrophila is 310 kDa. The enzyme is likely composed of 6 catalytic polypeptides of 34 kDa each and 6 regulatory polypeptides of 17 kDa each. The velocity-substrate curve for A. hydrophila ATCase is sigmoidal for both aspartate and carbamoylphosphate. The Km for aspartate was the highest to date for an enteric bacterium at 97.18 mM. The Km for carbamoylphosphate was 1.18 mM. When heated to 60 ºC, the specific activity of the enzyme dropped by more than 50 %. When heated to 100 ºC, the enzyme showed no activity. The enzyme's activity was inhibited by ATP, CTP or UTP.

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  • December 2000

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  • June 24, 2008, 6:15 p.m.

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  • April 26, 2016, 4:13 p.m.

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Citations, Rights, Re-Use

Higginbotham, Leah. Aspartate Transcarbamoylase of Aeromonas Hydrophila, thesis, December 2000; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc5840/: accessed December 11, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .