3.5.2.2: dihydropyrimidinase
This is an abbreviated version!
For detailed information about dihydropyrimidinase, go to the full flat file.
Word Map on EC 3.5.2.2
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3.5.2.2
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5-fluorouracil
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thymidylate
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dihydropyridine
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colorectal
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fluoropyrimidine
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phosphorylase
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thymidine
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capecitabine
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l-type
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uracil
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nifedipine
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orotate
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resect
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blocker
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pharmacogenetic
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1,4-dihydropyridine
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tegafur
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prodrugs
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voltage-dependent
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dihydrouracil
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5-fu-based
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fluoropyrimidine-based
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nitrendipine
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leucovorin
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phosphoribosyltransferase
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diltiazem
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oxaliplatin
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irinotecan
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hemoperfusion
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phosphoribosyl
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5-fluorouracil-based
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mucositis
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neutropenia
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pyrrolizidine
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11-ketotestosterone
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excitation-contraction
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isradipine
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nisoldipine
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coniferyl
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5-fu-induced
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dihydropyridine-sensitive
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felodipine
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5\'-dfur
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dihydroorotase
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photochromic
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nicardipine
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synthesis
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industry
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5'-deoxy-5-fluorouridine
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pretherapeutic
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omega-conotoxin
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nutrition
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medicine
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hand-foot
- 3.5.2.2
- 5-fluorouracil
- thymidylate
-
dihydropyridine
- colorectal
-
fluoropyrimidine
- phosphorylase
- thymidine
- capecitabine
-
l-type
- uracil
- nifedipine
- orotate
-
resect
-
blocker
-
pharmacogenetic
-
1,4-dihydropyridine
-
tegafur
-
prodrugs
-
voltage-dependent
- dihydrouracil
-
5-fu-based
-
fluoropyrimidine-based
-
nitrendipine
- leucovorin
-
phosphoribosyltransferase
- diltiazem
- oxaliplatin
- irinotecan
-
hemoperfusion
-
phosphoribosyl
-
5-fluorouracil-based
- mucositis
- neutropenia
-
pyrrolizidine
- 11-ketotestosterone
-
excitation-contraction
- isradipine
- nisoldipine
-
coniferyl
-
5-fu-induced
-
dihydropyridine-sensitive
- felodipine
-
5\'-dfur
- dihydroorotase
-
photochromic
- nicardipine
- synthesis
- industry
- 5'-deoxy-5-fluorouridine
-
pretherapeutic
-
omega-conotoxin
- nutrition
- medicine
-
hand-foot
Reaction
Synonyms
4,5-dihydropyrimidine amidohydrolase, aaHYD, bar9HYD, bpHYD, bsHYD, CRMP, D-CpHPG, D-HYD, D-hydantionase, D-hydantoin-hydrolyzing enzyme, D-hydantoinase, D-PfHYD, DHP, DHP-1, DHP-2, DHPase, dht, DHTase, dihydropyrimidase/hydantoinase, Dihydropyrimidinase, dihydropyrimidine amidohydrolase, dihydropyrimidine dehydrogenase, HDT, HYD, hydantoin peptidase, hydantoinase, hydropyrimidine hydrase, hyuH, L-Hyd, L-hydantoinase, microbial hydantoinase, P479, PA0441, PaDHPase, PYD2, PydB, pyrimidine hydrase, SmelDhp, thHYD
ECTree
3.5.2.2 dihydropyrimidinaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.5.2.2 - dihydropyrimidinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F159A
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turnover number for hydantoin is 10% of that of the wild-type enzyme, Km-value for hydantoin is 4.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 6.1fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme
F159I
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turnover number for hydantoin is 61% of that of the wild-type enzyme, Km-value for hydantoin is 1.9fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 2.6fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.5fold lower than that of the wild-type enzyme
F159L
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turnover number for hydantoin 64% of the turnover number of the wild-type enzyme, Km-value for hydantoin is 90% of the value of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 61% of that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 2.5fold lower than that of the wild-type enzyme
F159S
F159V
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turnover number for hydantoin is 22% of that of the wild-type enzyme, Km-value for hydantoin is 1.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 2.8fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.5fold lower than that of the wild-type enzyme
L65F/F159A F159A
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turnover number for hydantoin is 10.9% of that of the wild-type enzyme, Km-value for hydantoin is 4.8fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 11fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 2.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme
M63F/L65V F159A
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turnover number for hydantoin is 9.5% of that of the wild-type enzyme, Km-value for hydantoin is 2.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 10fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 4.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme
F159A
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turnover number for hydantoin is 10% of that of the wild-type enzyme, Km-value for hydantoin is 4.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 6.1fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme
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F159I
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turnover number for hydantoin is 61% of that of the wild-type enzyme, Km-value for hydantoin is 1.9fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 2.6fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.5fold lower than that of the wild-type enzyme
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F159L
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turnover number for hydantoin 64% of the turnover number of the wild-type enzyme, Km-value for hydantoin is 90% of the value of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 61% of that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 2.5fold lower than that of the wild-type enzyme
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F159S
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turnover number for hydantoin is 4.7% of that of the wild-type enzyme, Km-value for hydantoin is 4fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 15.5fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 5fold higher than that of the wild-type enzyme
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F159V
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turnover number for hydantoin is 22% of that of the wild-type enzyme, Km-value for hydantoin is 1.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 2.8fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.5fold lower than that of the wild-type enzyme
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R412M
W360R
N337A
site-directed mutagenesis, the mutant enzyme is active, but its activity is about 20fold less than that of the wild-type dihydropyrimidinase
DELTA474-479
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C-terminally truncated mutant, expressed in the form of random aggregates without any activity
DELTA475-479
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C-terminally truncated mutant, dissociated into the monomeric state, the activity is largely retained
DELTA476-479
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C-terminally truncated mutant, dissociated into the monomeric state, the activity is largely retained
DELTA477-479
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C-terminally truncated mutant, dissociated into the monomeric state, the activity is largely retained
DELTA478-479
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C-terminally truncated mutant, dissociated into the monomeric state, the activity is largely retained
R474
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mutant is expressed in the form of random aggregates without any activity
R479A
R479D
R479A
additional information
F159S
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turnover number for hydantoin is 4.7% of that of the wild-type enzyme, Km-value for hydantoin is 4fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 15.5fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 5fold higher than that of the wild-type enzyme
R479A
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mutant is expressed in the form of random aggregates without any activity
R479A
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the mutant is expressed in the form of random aggregates without any activity, the relative activity of mutant is about twice as that of the wild type enzyme at pH 6.0 and pH 10.0
R479D
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dissociates into the monomeric state but 78.2% retains activity of the wild type enzyme
R479D
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dissociated into the monomeric state, activity is largely retained
R479D
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the C-terminal-substituted enzyme is dissociated into the monomeric state, but the activity is largely retained, the relative activity of mutant is about twice as that of the wild type enzyme at pH 6.0 and pH 10.0
R479A
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mutant is expressed in the form of random aggregates without any activity
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additional information
immobilization of the purified recombinant enzyme on N-carbamoyl-D-4-hydroxyphenylglycine in batch reactions, method optimization: 0.155 mM enzyme/disc, in 0.1 M Tris-HCl, pH 8, and 0.8 M sodium chloride, 14 h, overview. 99% enzyme activity remains after 15 reaction cycles. The immobilized DHTase membrane can achieve a larger pH and thermal tolerant range than that of free enzyme
additional information
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immobilization of the purified recombinant enzyme on N-carbamoyl-D-4-hydroxyphenylglycine in batch reactions, method optimization: 0.155 mM enzyme/disc, in 0.1 M Tris-HCl, pH 8, and 0.8 M sodium chloride, 14 h, overview. 99% enzyme activity remains after 15 reaction cycles. The immobilized DHTase membrane can achieve a larger pH and thermal tolerant range than that of free enzyme
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additional information
HYDc1 with the C-terminal Arg deletion retains 43% activity, while HYDn1 with the N-terminal Ser deletion has no activity using DL-hydantoin as substrate
additional information
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the truncated mutants P478, P477, P476, and P475 are dissociated into the monomeric state, but their activities are largely retained (86.7-57.0% of wild type activity)
additional information
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the flexibility of the non-conservative region at the C-terminus is quite limited implying that the intact enzyme structure is essential for enzyme activity
additional information
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several truncated mutants (P478, P477, P476, and P475) are dissociated into the monomeric state as well, but their activities are largely retained, the relative activities of mutants is about twice as that of the wild type enzyme at pH 6.0 and pH 10.0
additional information
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the truncated mutants P478, P477, P476, and P475 are dissociated into the monomeric state, but their activities are largely retained (86.7-57.0% of wild type activity)
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additional information
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the flexibility of the non-conservative region at the C-terminus is quite limited implying that the intact enzyme structure is essential for enzyme activity
-
additional information
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several truncated mutants (P478, P477, P476, and P475) are dissociated into the monomeric state as well, but their activities are largely retained, the relative activities of mutants is about twice as that of the wild type enzyme at pH 6.0 and pH 10.0
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additional information
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HYDc1 with the C-terminal Arg deletion retains 43% activity, while HYDn1 with the N-terminal Ser deletion has no activity using DL-hydantoin as substrate
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additional information
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whole-cell immobilization on calcium alginate of D-hydantoinase-engineered Escherichia coli strain BL21(DE3) for D-carbamoyl-4-hydroxyphenylglycine (D-CpHPG) biosynthesis. Whole-cell immobilization method involves addition of 3.0% w/v alginate, 1.5% w/v diatomite, 0.05% w/v CaCl2, and 1.0 mM MnCl2. The optimized diameter of immobilized beads for the whole-cell biosynthesis is 2.60 mm. The maximized production rates of D-CpHPG are up to 76%, and the immobilized beads can be reused for 12 batches. Method optimization and evaluation, overview
