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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

Reaction

ATP
+
Urea
 +
HCO3-
 +
H+
=
ADP
 +
phosphate
 +
urea-1-carboxylate

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)

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.6 urea carboxylase

Engineering

Engineering on EC 6.3.4.6 - urea carboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D1321A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
D1584N
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
E1792A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
G559E/G572E
mutation renders the protein monomeric
K1605A
S177A
mutation in the active site of the allophanate hydrolase. A mixture of mutants K1605A and S177A is as efficient as wild-type
Y1324F
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
Y1628F
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
D1321A
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
D1584N
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
K1605A
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
Y1324F
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
Y1628F
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
G559E/G572E
-
mutation renders the protein monomeric
-
K1605A
-
mutation in active site of the carboxylyase. A mixture of mutants K1605A and S177A is as efficient as wild-type
-
S177A
-
mutation in the active site of the allophanate hydrolase. A mixture of mutants K1605A and S177A is as efficient as wild-type
-