2.6.1.55: taurine-2-oxoglutarate transaminase
This is an abbreviated version!
For detailed information about taurine-2-oxoglutarate transaminase, go to the full flat file.
Word Map on EC 2.6.1.55
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2.6.1.55
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transamination
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sulfoacetaldehyde
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hypotaurine
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sulfonate
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isethionate
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pyridoxal
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2-aminoethanesulfonate
- 2.6.1.55
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transamination
- sulfoacetaldehyde
- hypotaurine
- sulfonate
- isethionate
- pyridoxal
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2-aminoethanesulfonate
Reaction
Synonyms
aminotransferase, taurine, BkToa, taurine transaminase, taurine-alpha-ketoglutarate aminotransferase, taurine-glutamate transaminase, taurine:2-oxoglutarate aminotransferase, taurine:alpha-ketoglutarate aminotransferase
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General Information
General Information on EC 2.6.1.55 - taurine-2-oxoglutarate transaminase
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evolution
metabolism
physiological function
additional information
sequence comparisons and phylogenetic analysis of taurine:oxoglutarate aminotransferases and taurine:pyruvate aminotransferases, overview
evolution
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sequence comparisons and phylogenetic analysis of taurine:oxoglutarate aminotransferases and taurine:pyruvate aminotransferases, overview
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BkToa is part of a gene cluster putatively involved in taurine nitrogen assimilation. In this pathway, isothionate is formed by a sulfoacetaldehyde reductase TauF, a member of the metal-dependent alcohol dehydrogenase family
metabolism
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BkToa is part of a gene cluster putatively involved in taurine nitrogen assimilation. In this pathway, isothionate is formed by a sulfoacetaldehyde reductase TauF, a member of the metal-dependent alcohol dehydrogenase family
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taurine is thought to serve as a source of carbon, nitrogen and sulfur for certain gut bacteria, particularly for strict anaerobes residing in the nutrient-poor environment of the distal gut. Taurine aminotransferases catalyze the first step in taurine catabolism in many taurine-degrading bacteria and play an important role in bacterial taurine metabolism in the mammalian gut
physiological function
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taurine is thought to serve as a source of carbon, nitrogen and sulfur for certain gut bacteria, particularly for strict anaerobes residing in the nutrient-poor environment of the distal gut. Taurine aminotransferases catalyze the first step in taurine catabolism in many taurine-degrading bacteria and play an important role in bacterial taurine metabolism in the mammalian gut
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molecular docking reveals a role for active site residues Trp21 and Arg156, conserved in Toa enzymes, in interacting with the sulfonate group of taurine
additional information
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molecular docking reveals a role for active site residues Trp21 and Arg156, conserved in Toa enzymes, in interacting with the sulfonate group of taurine
additional information
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molecular docking reveals a role for active site residues Trp21 and Arg156, conserved in Toa enzymes, in interacting with the sulfonate group of taurine
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