2.5.1.2: thiamine pyridinylase
This is an abbreviated version!
For detailed information about thiamine pyridinylase, go to the full flat file.
Word Map on EC 2.5.1.2
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2.5.1.2
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thiaminolyticus
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medicine
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thiazole
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aniline
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pseudoharengus
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viscera
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bivalve
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alosa
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analysis
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nutrition
- 2.5.1.2
- thiaminolyticus
- medicine
- thiazole
- aniline
- pseudoharengus
- viscera
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bivalve
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alosa
- analysis
- nutrition
Reaction
Synonyms
pyrimidine transferase, thiamin hydrolase, thiamin pyridinolase, thiamin pyridinylase, thiaminase, thiaminase I, thiamine pyridinolase, thiamine pyridinylase
ECTree
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General Information
General Information on EC 2.5.1.2 - thiamine pyridinylase
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evolution
malfunction
metabolism
physiological function
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thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
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thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
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thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
thiaminase I is specifically implicated in thiamine deficiency syndromes in animals
malfunction
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thiaminase I is specifically implicated in thiamine deficiency syndromes in animals
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the enzyme cleaves phosphorylated thiamine and toxic analogs, which releases precursors that can then be used for thiamine synthesis
metabolism
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the enzyme cleaves phosphorylated thiamine and toxic analogs, which releases precursors that can then be used for thiamine synthesis
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crucian carp known to harbor thiaminase I activity are injected intramuscularly with live Aeromonas salmonicida. Significantly higher thiaminase activities are measured in all tissues of fish injected with live bacteria than in the control group. Different allocation pattern are shown: The amount of thiaminase I enzyme is elevated in the whole blood of injected fish in the absence of natural cosubstrate(s). The thiaminase activity of the injected, inflamed muscle suggests that both the amount of thiaminase enzyme and an unidentified natural cosubstrate(s) is elevated. This suggests that in addition to the enzyme, some cosubstrate(s) of fish or pathogen origin play a regulatory role in the physiological significance of thiaminase I activity in vivo
physiological function
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although thiaminase I exposure does not stimulate the energy-sensing signaling kinases AKT, AMPK and GSK-3beta in MCF-7, ZR75, HS-578T and T-47D cell lines, thiaminase I exposure does stimulate expression of the ER stress response protein GRP78. Thiaminase I is cytotoxic in breast cancer cell lines and triggers the unfolded protein response
physiological function
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Burkholderia pseudomallei possesses thiaminase I which catalyzes degradation of thiamine to 4-methyl-5-thiazoleethanol. ThiM, which encodes hydroxyethylthiazole kinase responsible for degradation of 4-methyl-5-thiazoleethanol, is absent or not expressed in all Burkholderia pseudomallei strains. The high 4-methyl-5-thiazoleethanol level in Burkholderia pseudomallei is likely due to the absence of hydroxyethylthiazole kinase and hence reduced downstream degradation
physiological function
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Burkholderia thailandensis possesses thiaminase I which catalyzes degradation of thiamine to 4-methyl-5-thiazoleethanol. ThiM, which encodes hydroxyethylthiazole kinase responsible for degradation of 4-methyl-5-thiazoleethanol, is present and expressed in Burkholderia thailandensis
physiological function
thiaminase I provides a growth advantage by salvaging precursors from environmental thiamine and its analogs in Burkholderia thailandensis
physiological function
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thiaminase I provides a growth advantage by salvaging precursors from environmental thiamine and its analogs in Burkholderia thailandensis
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