3.5.2.5: allantoinase
This is an abbreviated version!
For detailed information about allantoinase, go to the full flat file.
Word Map on EC 3.5.2.5
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3.5.2.5
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allantoic
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ureide
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uricase
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allantoicase
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urate
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hydantoinase
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dihydropyrimidinase
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ureidoglycolate
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hydantoin
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imidase
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dihydroorotase
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amidohydrolases
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1.7.3.3
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diagnostics
- 3.5.2.5
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allantoic
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ureide
- uricase
- allantoicase
- urate
- hydantoinase
- dihydropyrimidinase
- ureidoglycolate
- hydantoin
- imidase
- dihydroorotase
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amidohydrolases
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1.7.3.3
- diagnostics
Reaction
Synonyms
AaALN, allantoin amidohydrolase, allantoinase, ALLase, AllBali, ALN, aln-1, aln-2, Fe-allantoinase, IsoI, IsoII, metal-dependent allantoinase, metal-independent allantoinase, Os04g0680400, OsALN, puuE, Salk_142607, Salk_146783, zinc-amended allantoinase
ECTree
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Substrates Products
Substrates Products on EC 3.5.2.5 - allantoinase
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REACTION DIAGRAM
(S)-allantoin + H2O
allantoate
allantoinase catalyzes the reversible hydrolysis of allantoin into allantoate by hydrolytic cleavage of the N1-C2 amide bond of the five-membered hydantoin ring. The enzyme shows an inverted enantioselectivity towards allantoin, R-enantioselective
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r
(S)-allantoin + H2O
allantoate
best substrate, enantioselectivity of Co2+-enzyme toward allantoin enantiomers
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(S)-allantoin + H2O
allantoate
allantoinase catalyzes the reversible hydrolysis of allantoin into allantoate by hydrolytic cleavage of the N1-C2 amide bond of the five-membered hydantoin ring. The enzyme shows an inverted enantioselectivity towards allantoin, R-enantioselective
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r
(S)-allantoin + H2O
allantoate
best substrate, enantioselectivity of Co2+-enzyme toward allantoin enantiomers
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?
(S)-allantoin + H2O
allantoate
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zinc enzyme uses only the S-isomer, cobalt-enzyme prefers S-isomer but also hydrolyses R-isomer
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?
(S)-allantoin + H2O
allantoate
0.2 mM, assay at pH 7.6, 25°C, 10 min
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r
allantoin + H2O
allantoate
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key enzyme in the biogenesis and catabolism of ureide compounds in plants, pathway overview
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ir
allantoin + H2O
allantoate
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step in the purine degradation pathway producing nitrogen waste for excretion
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allantoin + H2O
allantoate
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development of a enzyme cycling method for measuring allantoin concentrations in human serum involving allantoinase, glutamine synthetase II, EC 6.3.1.2, allantoate amidohydrolase, EC 3.5.3.9, and NAD synthetase, EC 6.3.1.5, followed by action of glucose dehydrogenase, EC 1.1.1.47, and diaphorase, EC 1.6.99.2, in the presence of glucose and 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-(2,4-disulfophenyl)-2H-tetrazolium, overview, optimal reaction for allantoinase at 0.07 mM allantoin concentration
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allantoin + H2O
allantoate
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a key reaction step in the biosynthesis and degradation of ureides, overview
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allantoin + H2O
allantoate
key enzyme in the biogenesis and catabolism of ureide compounds in plants, pathway overview
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ir
allantoin + H2O
allantoate
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step in the purine degradation pathway, changes during the annual reproductive cycle of the fish
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the enzyme might be regulated by exogenous nitrogen conditions
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additional information
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no substrate: hydantoin, dihydrouracil, phthalimide, dihydroorotate, and 3-imonoisoindolinone
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additional information
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no activity with hydantoin and 5-bromouracil
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additional information
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spectrometric fluorescence quantification of allantoin in biological samples by cap-immobilized allantoinase/resorcinol assay, formation of the lactone of 2,2',4,4'-tetrahydroxy-diphenylacetic acid at 100°C, specific for allantoin, method development and evaluation, overview. Other compounds such as sodium pyruvate, 2-oxoglutaric acid, 2-oxobutyric acid, oxalacetic acid, oxalic acid, formic acid, citric acid,glycolic acid, succinic acid, acetic acid, tartaric acid and salicylic acid do not form the fluorescent species. Also no reactivity with the intermediates of uricolytic pathway, 5-hydroxyisourate and 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline. The assay can be applied to the evaluation of the catalytic activity of PEGylated enzymes conceived for the treatment of hyperuricemia-related conditions
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additional information
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the enzyme is inducible by allantoin and is upregulated in spring in trunk bark, the enzyme might be regulated by exogenous nitrogen conditions
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additional information
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the enzyme is inducible by allantoin and is upregulated in spring in trunk bark, the enzyme might be regulated by exogenous nitrogen conditions
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additional information
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dihydroorotate, hydantoin, and phthalimide are not hydrolyzed by allantoinase
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