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
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Subunits
Subunits on EC 3.5.2.2 - dihydropyrimidinase
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dimer
dimer or tetramer
homodimer
homotetramer
monomer
oligomer
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2 * 60000 + 2 * 62000 + 1 * 110000, room temperature, 2-mercaptoethanol, SDS-PAGE
tetramer
additional information
dimer
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
homotetramer
structure solved by molecular replacement, corresponding to the native state of the enzyme in solution
homotetramer
4 * 55000, recombinant N-terminally His-tagged enzyme, SDS-PAGE, 4 * 54400, about, sequence calculation
homotetramer
Pseudomonas fluorescens CGMCC 1.1802
-
4 * 55000, recombinant N-terminally His-tagged enzyme, SDS-PAGE, 4 * 54400, about, sequence calculation
-
monomer
-
mutant enzymes R479D, P478, P477, P476, P475, and P474, determined by size-exclusion chromatography
monomer
-
mutant enzymes R479D, P478, P477, P476, P475, and P474, determined by size-exclusion chromatography
-
tetramer
-
purified enzyme from the native Bacillus sp. AR9 by gel filtration
tetramer
-
purified enzyme from the native Bacillus sp. AR9 by gel filtration
-
tetramer
each subunit of the tetrameric enzyme consists of an elliptically distorted (alpha/beta)8-barrel domain
tetramer
-
in the absence of Zn2+, the protein acquires a tetrameric functional structure at pH 6.0, which is stable up to pH 9
additional information
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
additional information
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-