Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
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Drug
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Target Concepts:
Gene/Protein
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Query: EC:3.5.1.5 (
urease
)
7,257
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Artificial cells containing glucose dehydrogenase (
EC 1.1.1.47
), leucine dehydrogenase (EC 1.4.1.9),
urease
(
EC 3.5.1.5
), and dextran-NAD+ were prepared. Ammonia or urea could be converted into L-leucine, L-valine, and L-isoleucine with artificial cells. Low-specific-activity glucose dehydrogenase could effectively regenerate dextran-NADH, which was recycled at a rate of 0.4 to 0.5 cycle per minute under reaction conditions. The effects of ammonium salts and urea on the conversion rate for the leucine dehydrogenase multienzyme system were also studied. The relative activities in ammonium salts solutions were 40 to 70% of those in urea solutions.
...
PMID:Conversion of ammonia or urea into L-leucine, L-valine, and L-isoleucine using artificial cells containing an immobilized multienzyme system and dextran-NAD+. Glucose dehydrogenase for co-factor recycling. 245 27
Artificial cells containing leucine dehydrogenase (EC 1.4.1.9), alcohol dehydrogenase (EC 1.1.1.1; or glucose dehydrogenase,
EC 1.1.1.47
; or lactic dehydrogenase, EC 1.1.1.27; or malic dehydrogenase, EC 1.1.1.37),
urease
(
EC 3.5.1.5
) and dextran-NAD+ were prepared. Ammonia or urea could be converted into L-leucine, L-valine and L-isoleucine using artificial cells with four different multienzyme systems.
...
PMID:Conversion of urea or ammonia into essential amino acids (L-leucine, L-valine, and L-isoleucine) using multienzyme systems and NADH-dextran immobilised in artificial cells. 344 45
We prepared artificial cells each containing leucine dehydrogenase (EC 1.4.1.9),
urease
(
EC 3.5.1.5
), soluble dextran-NAD(+), and one of the following coenzyme regenerating dehydrogenases: glucose dehydrogenase (
EC 1.1.1.47
); yeast alcohol dehydrogenase (EC 1.1.1.1); malate dehydrogenase (EC 1.1.1.37); or lactate dehydrogenase (EC 1.1.1.27). Artificial cells were packed in small columns. L-Leucine, L-valine, and L-isoleucine were continuously produced with simultaneous dextran-NADH regeneration. The maximum production ratios depended on the coenzyme regenerating systems used: 83-93% for D-glucose and glucose dehydrogenase system; 90% for ethanol and yeast alcohol dehydrogenase system; 45-55% for L-malate and malate dehydrogenase system; and 64-78% for L-lactate and lactate dehydrogenase system. Kinetic experiments were also carried out. The apparent K(m) values are as follows: 0.33 mM for alpha-ketoisocaproate (KIC); 0.51 mM for alpha-ketoisovalerate (KIV); 0.58 mM for DL-alpha-keto-beta-methyl-n-valerate (KMV); 3.52 mM for urea; 27.82 mM for D-glucose; 3.89 mM for ethanol; 3.02 mM for L-malate; and 16.67 mM for L-lactate. Kinetic analysis showed that KIC, KIV, and KMV were all competitive inhibitors in the reactions catalyzed by leucine dehydrogenase. Their inhibitor constants were the corresponding K(m) values.
...
PMID:Production of essential L-branched-chain amino acids in bioreactors containing artificial cells immobilized multienzyme systems and dextran-NAD+. 1859 77
