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Literature summary for 3.5.2.2 extracted from

  • Slomka, C.; Zhong, S.; Fellinger, A.; Engel, U.; Syldatk, C.; Braese, S.; Rudat, J.
    Chemical synthesis and enzymatic, stereoselective hydrolysis of a functionalized dihydropyrimidine for the synthesis of beta-amino acids (2015), AMB Express, 5, 85 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.2.2

Cloned(Commentary)

Cloned (Comment) Organism
functional recombinant expression in Escherichia coli strain JM109 Arthrobacter crystallopoietes

Organism

Organism UniProt Comment Textmining
Arthrobacter crystallopoietes Q84FR6
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Arthrobacter crystallopoietes DSM 20117 Q84FR6
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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 hydantoinase in recombinant Escherichia coli cells has a specific activity of 0.326 mU/mgcdw with 6-(4-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione Arthrobacter crystallopoietes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-(4-nitrophenyl)-3-ureidopropanoic acid + H2O NCarbpNO2betaPhe, chemically synthesized artificial substrate. Enantioselective reactivity, preference of the hydantoinase for the (S)-enantiomer Arthrobacter crystallopoietes ?
-
 ?
3-(4-nitrophenyl)-3-ureidopropanoic acid + H2O NCarbpNO2betaPhe, chemically synthesized artificial substrate. Enantioselective reactivity, preference of the hydantoinase for the (S)-enantiomer Arthrobacter crystallopoietes DSM 20117 ?
-
 ?
6-(4-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione + H2O pNO2PheDU, chemically synthesized artificial substrate. Recombinant Escherichia coli cells expressing the hydantoinase show degradation of the substrate. Enantioselective reactivity, preference of the hydantoinase for the (S)-enantiomer Arthrobacter crystallopoietes ?
-
 ?
6-(4-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione + H2O pNO2PheDU, chemically synthesized artificial substrate. Recombinant Escherichia coli cells expressing the hydantoinase show degradation of the substrate. Enantioselective reactivity, preference of the hydantoinase for the (S)-enantiomer Arthrobacter crystallopoietes DSM 20117 ?
-
 ?
additional information the enzyme shows activity with 6-monosubstituted dihydrouracils. The enzyme shows enantioselectivity Arthrobacter crystallopoietes ?
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additional information the enzyme shows activity with 6-monosubstituted dihydrouracils. The enzyme shows enantioselectivity Arthrobacter crystallopoietes DSM 20117 ?
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Synonyms

Synonyms Comment Organism
D-hydantoinase
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 Arthrobacter crystallopoietes
hydantoinase
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 Arthrobacter crystallopoietes
hyuH
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 Arthrobacter crystallopoietes

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 assay at Arthrobacter crystallopoietes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Arthrobacter crystallopoietes