3.5.1.6: beta-ureidopropionase
This is an abbreviated version!
For detailed information about beta-ureidopropionase, go to the full flat file.
Word Map on EC 3.5.1.6
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3.5.1.6
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pyrimidine
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uracil
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dihydropyrimidinase
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thymine
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dihydrouracil
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kluyveri
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nitrilase
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amidohydrolases
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beta-aminoisobutyric
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beta-ureidoisobutyrate
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medicine
- 3.5.1.6
- pyrimidine
- uracil
- dihydropyrimidinase
- thymine
- dihydrouracil
- kluyveri
- nitrilase
-
amidohydrolases
-
beta-aminoisobutyric
- beta-ureidoisobutyrate
- medicine
Reaction
Synonyms
3-ureidopropionase, beta-Ala synthase, beta-alanine synthase, beta-UP, beta-ureidopropionase, beta-ureidopropionate decarbamylase, betaAS, betaUP, betaUPase, BUP-1, BUP1, human liver beta-ureidopropionase, N-carbamoyl-beta-Ala amidohydrolase, N-carbamoyl-beta-alanine amidohydrolase, N-carbamyl-beta-alanine decarbamylase, NCbetaA, PYD3, SkbetaAS, UPB1
ECTree
3.5.1.6 beta-ureidopropionaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.5.1.6 - beta-ureidopropionase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(RS)-2-(2,6-dinitrophenoxy)-propionate
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most potent inhibitor of aryl propionates, IC50: 500 nM, completely reversible by passing the enzyme-inhibitor complex over a gel filtration column
1,10-phenanthroline
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1 mM, 96% inhibition, activity can be partially restored by Zn2+
2-methyl-beta-alanine
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product inhibition, the presence of product leads to dissociation of hexamers to inactive trimers
2-methyl-N-carbamoyl-beta-alanine
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competitive inhibitor of the reaction with N-carbamoyl-beta-alanine
beta-Alanine
causes dissociation to inactive dimers, competitive inhibition
beta-Alanine
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product inhibition, the presence of product leads to dissociation of hexamers to inactive trimers
chloramphenicol
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1.6fold reduced activity in chloramphenicol-treated cells
iodoacetamide
30 min preincubation with 50 mM iodoacetamide renders the enzyme completely inactive, probably due to covalent modification of the active-site cysteine (C233)
iodoacetamide
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1 mM, complete inhibition, completely prevented by addition of substrate, the sensitive thiol group is located at the active site
Zn2+
5.5% residual activity is measured after preincubation with 50 mM ZnCl2
additional information
preincubation of the enzyme with 1 mM EDTA has no influence on activity
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additional information
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removal of the enzyme-bound zinc by chelators leads to loss of activity
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additional information
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not inhibited by hydroxyurea, acetohydroxamic acid, benzenesulfonamide, 4-carboxybenzenesulfonamide, 4-nitrobenzenesulfonamide, all up to 1 mM, substrate analogs, such as alpha-ureidopropionate, alpha-ureidoisobutyrate, alpha-ureido-n-butyrate, N-carbamoyl-Asp, or product beta-alanine, all up to 2 mM
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