6.3.4.6: urea carboxylase
This is an abbreviated version!
For detailed information about urea carboxylase, go to the full flat file.
Word Map on EC 6.3.4.6
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6.3.4.6
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allophanate
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allantoin
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carboxylases
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biotin-dependent
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utilis
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diagnostics
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analysis
- 6.3.4.6
- allophanate
- allantoin
- carboxylases
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biotin-dependent
- utilis
- diagnostics
- analysis
Reaction
Synonyms
ATP-urea amidolyase, ATP:urea amidolyase, DUR1,2, EC 3.5.1.45, KLLA0_E08119g, UALase, UCA, Urea amido-lyase, urea amidolyase, urea carboxylase, Urea carboxylase (hydrolysing), Urease (ATP-hydrolysing)
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General Information
General Information on EC 6.3.4.6 - urea carboxylase
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physiological function
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urea amidolyase is comprised of two enzymatic components: urea carboxylase and allophanate hydrolase. There is no substrate channeling or interdomain/intersubunit communication between urea carboxylase and allophanate hydrolase. Neither stable nor transient interactions can be detected between urea carboxylase and allophanate hydrolase and the catalytic efficiencies are independent of one another. An artificial fusion of urea carboxylase and allophanate hydrolase does not significantly alter the allophanate hydrolase enzyme activity or catalytic efficiency
physiological function
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urea amidolyase is comprised of two enzymatic components: urea carboxylase and allophanate hydrolase. There is no substrate channeling or interdomain/intersubunit communication between urea carboxylase and allophanate hydrolase. Neither stable nor transient interactions can be detected between urea carboxylase and allophanate hydrolase and the catalytic efficiencies are independent of one another. An artificial fusion of urea carboxylase and allophanate hydrolase does not significantly alter the allophanate hydrolase enzyme activity or catalytic efficiency
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physiological function
Pseudomonas syringae pv. tomato ATCC BAA-871D-5
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urea amidolyase is comprised of two enzymatic components: urea carboxylase and allophanate hydrolase. There is no substrate channeling or interdomain/intersubunit communication between urea carboxylase and allophanate hydrolase. Neither stable nor transient interactions can be detected between urea carboxylase and allophanate hydrolase and the catalytic efficiencies are independent of one another. An artificial fusion of urea carboxylase and allophanate hydrolase does not significantly alter the allophanate hydrolase enzyme activity or catalytic efficiency
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physiological function
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urea amidolyase is comprised of two enzymatic components: urea carboxylase and allophanate hydrolase. There is no substrate channeling or interdomain/intersubunit communication between urea carboxylase and allophanate hydrolase. Neither stable nor transient interactions can be detected between urea carboxylase and allophanate hydrolase and the catalytic efficiencies are independent of one another. An artificial fusion of urea carboxylase and allophanate hydrolase does not significantly alter the allophanate hydrolase enzyme activity or catalytic efficiency
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