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Literature summary extracted from

  • Zhao, J.; Zhu, L.; Fan, C.; Wu, Y.; Xiang, S.
    Structure and function of urea amidolyase (2018), Biosci. Rep., 38, pii: BSR20171617.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.4.6
-
 Kluyveromyces lactis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.4.6 deletion mutant lacking the biotin-carboxyl carrier protein domain, to 6.5 A resolution. Space group P212121, with four monomers per asymmetric unit Kluyveromyces lactis

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.6 G559E/G572E mutation renders the protein monomeric Kluyveromyces lactis
6.3.4.6 K1605A mutation in active site of the carboxylyase. A mixture of mutants K1605A and S177A is as efficient as wild-type Kluyveromyces lactis
6.3.4.6 S177A mutation in the active site of the allophanate hydrolase. A mixture of mutants K1605A and S177A is as efficient as wild-type Kluyveromyces lactis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.6 0.203
-
 Urea mutant S177A, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 0.216
-
 Urea mixture of mutants S177A and mutant K1605A, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 0.246
-
 Urea isolated urea carboxyxlase domain plus allophanate hydrolase domain, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 0.255
-
 Urea wild-type, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 0.299
-
 Urea mutant K1605A, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 0.361
-
 Urea mutant G559E/G572E, pH 8.0, temperature not specified in the publication Kluyveromyces lactis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.4.6 500000
-
 gel filtration Kluyveromyces lactis

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.6 Kluyveromyces lactis Q6CP22 enzyme is composed of urea carboxylase domain plus allophanate hydrolase domain, EC 3.5.1.54
-
6.3.4.6 Kluyveromyces lactis DSM 70799 Q6CP22 enzyme is composed of urea carboxylase domain plus allophanate hydrolase domain, EC 3.5.1.54
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.6 ATP + urea + HCO3-
-
 Kluyveromyces lactis ADP + phosphate + urea-1-carboxylate
-
 ?
6.3.4.6 ATP + urea + HCO3-
-
 Kluyveromyces lactis DSM 70799 ADP + phosphate + urea-1-carboxylate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.4.6 dimer 2 * 202000, SDS-PAGE Kluyveromyces lactis
6.3.4.6 More holo-enzyme formation is essential for optimal activity Kluyveromyces lactis

Synonyms

EC Number Synonyms Comment Organism
6.3.4.6 KLLA0_E08119g
-
 Kluyveromyces lactis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.4.6 0.78
-
 Urea mutant S177A, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 1.33
-
 Urea mutant K1605A, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 3
-
 Urea mutant G559E/G572E, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 10.07
-
 Urea isolated urea carboxyxlase domain plus allophanate hydrolase domain, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 12.68
-
 Urea mixture of mutants S177A and mutant K1605A, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 13.9
-
 Urea wild-type, pH 8.0, temperature not specified in the publication Kluyveromyces lactis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.3.4.6 3.87
-
 Urea mutant S177A, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 4.45
-
 Urea mutant K1605A, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 8.31
-
 Urea mutant G559E/G572E, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 40.9
-
 Urea isolated urea carboxyxlase domain plus allophanate hydrolase domain, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 54.6
-
 Urea wild-type, pH 8.0, temperature not specified in the publication Kluyveromyces lactis
6.3.4.6 58.7
-
 Urea mixture of mutants S177A and mutant K1605A, pH 8.0, temperature not specified in the publication Kluyveromyces lactis