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
-
bivalve
-
alosa
- analysis
- nutrition
Reaction
Synonyms
pyrimidine transferase, thiamin hydrolase, thiamin pyridinolase, thiamin pyridinylase, thiaminase, thiaminase I, thiamine pyridinolase, thiamine pyridinylase
ECTree
2.5.1.2 thiamine pyridinylaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 2.5.1.2 - thiamine pyridinylase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
4-Amino-5-(anilinomethyl)-6-chloro-2-methylpyrimidine
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complete irreversible inhibition 2 times faster than 4-amino-6-chloro-2-methylpyrimidine
Cd2+
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the degree of cadmium inhibition, when aniline is the cosubstrate, shows obvious differences between pI isozymes
4-Amino-6-chloro-2-methylpyrimidine
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complete irreversible inhibition, activity protected by thiamine and quinolone
4-Amino-6-chloro-2-methylpyrimidine
this suicide substrate is linked to Cys113 of the enzyme
Heteropyrithiamine
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inactivation at 0.006 mM that is restored by pyridine at 25 mM and inhibition of restoration of activity by pyridine at 1 mM
p-chloromercuribenzoate
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50% of inhibition at 0.2 mM and inhibits reactivation by pyridine
thiamine
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inactivation is proportional to thiamine concentration and the thiamine/enzyme ratio is 1 mol/1 mol
additional information
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chloramphenicol does not affect activity suggesting that the enzyme has an inactive form
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additional information
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primary substrates inactivate the enzyme at 0.006 mM, the lost activity can be restored by incubation at 37°C for 60 min after dialysis or by incubation with secondary substrates or acceptor bases, each substrate at high concentrations abolishes the inactivation of the other substrate
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additional information
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acidic conditions prevent inactivation but low pH does not restore activity after inactivation, quaternary nitrogen linked to a substituted pyrimidine ring through a methylene bridge is shared by compounds that inactivates the enzyme, inactivation alters either the net charge or the structure of the protein or both
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additional information
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4-amino-2-methyl pyrimidine does not inactivate nor competitively inhibits the enzyme
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