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ATP + 2-chloroacetamide + HCO3-
?
-
-
-
-
?
ATP + acetamide + HCO3-
?
ATP + cyanamide + HCO3-
?
-
-
-
-
?
ATP + formamide + HCO3-
?
ATP + formylurea + HCO3-
?
-
-
-
-
?
ATP + hydantoic acid + HCO3-
?
-
-
-
-
?
ATP + hydroxyurea + HCO3-
?
ATP + imidodicarbonic acid diamide + HCO3-
?
-
iminodicarbonic acid diamide, i.e. biuret
-
-
?
ATP + N-methylurea + HCO3-
?
ATP + propionamide + HCO3-
?
-
-
-
-
?
ATP + urea + CO2
ADP + phosphate + urea-1-carboxylate
ATP + urea + HCO3-
?
-
enzyme is involved in urea cleavage
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
ATP + urea + HCO3-
ADP + phosphate + urea-1-carboxylate
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
ATP + urethane + HCO3-
?
-
-
-
-
?
dATP + urea + HCO3-
?
-
one-third as effective as ATP
-
-
?
urea + H2O + ATP
CO2 + NH3 + ADP + phosphate
in the presence of enzyme, ATP, bicarbonate, magnesium, and potassium ions, ammonium ion is produced from human serum urea
-
-
?
ATP + acetamide + HCO3-
?
-
-
-
-
?
ATP + acetamide + HCO3-
?
-
-
-
?
ATP + acetamide + HCO3-
?
-
-
-
-
?
ATP + formamide + HCO3-
?
-
-
-
-
?
ATP + formamide + HCO3-
?
-
-
-
?
ATP + formamide + HCO3-
?
-
-
-
-
?
ATP + hydroxyurea + HCO3-
?
-
-
-
-
?
ATP + hydroxyurea + HCO3-
?
-
-
-
-
?
ATP + N-methylurea + HCO3-
?
-
-
-
-
?
ATP + N-methylurea + HCO3-
?
-
-
-
-
?
ATP + urea + CO2
ADP + phosphate + urea-1-carboxylate
activity is inducible by urea, acetamide or formamide
-
-
?
ATP + urea + CO2
ADP + phosphate + urea-1-carboxylate
multifunctional enzyme, catalyzes carboxylation of urea with urea carboxylase, EC 6.3.4.6, and hydrolysis of allophanate with allophanate hydrolase, EC 3.5.1.54
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
Ankistrodesmus braunii
-
-
i.e. urea-1-carboxylate
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
i.e. urea-1-carboxylate
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
i.e. urea-1-carboxylate
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
i.e. urea-1-carboxylate
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
i.e. urea-1-carboxylate
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
i.e. urea-1-carboxylate
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
i.e. urea-1-carboxylate
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
-
ir
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
i.e. urea-1-carboxylate
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
-
-
i.e. urea-1-carboxylate
?
ATP + urea + HCO3-
ADP + phosphate + urea-1-carboxylate
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + urea-1-carboxylate
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
-
?
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126
acetamide
30°C, pH 7.5
56.5
Formamide
30°C, pH 7.5
additional information
additional information
-
0.5
HCO3-
-
-
0.1
Urea
-
-
0.203
Urea
mutant S177A, pH 8.0, temperature not specified in the publication
0.216
Urea
mixture of mutants S177A and mutant K1605A, pH 8.0, temperature not specified in the publication
0.246
Urea
isolated urea carboxyxlase domain plus allophanate hydrolase domain, pH 8.0, temperature not specified in the publication
0.255
Urea
wild-type, pH 8.0, temperature not specified in the publication
0.299
Urea
mutant K1605A, pH 8.0, temperature not specified in the publication
0.32
Urea
wild type enzyme, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
0.361
Urea
mutant G559E/G572E, pH 8.0, temperature not specified in the publication
0.39
Urea
mutant enzyme E1792A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
1 - 1.3
Urea
mutant enzyme D1564N, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
7.7
Urea
mutant enzyme Y1324F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
15
Urea
mutant enzyme Y1628F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
78
Urea
mutant enzyme D1321A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
493
Urea
mutant enzyme K1605A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
additional information
additional information
-
-
additional information
additional information
-
-
-
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40.4
acetamide
30°C, pH 7.5
16.8
Formamide
30°C, pH 7.5
0.78
Urea
mutant S177A, pH 8.0, temperature not specified in the publication
1.33
Urea
mutant K1605A, pH 8.0, temperature not specified in the publication
1.44
Urea
mutant enzyme K1605A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
3
Urea
mutant G559E/G572E, pH 8.0, temperature not specified in the publication
3.16
Urea
mutant enzyme D1321A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
10.07
Urea
isolated urea carboxyxlase domain plus allophanate hydrolase domain, pH 8.0, temperature not specified in the publication
12.68
Urea
mixture of mutants S177A and mutant K1605A, pH 8.0, temperature not specified in the publication
13.9
Urea
wild-type, pH 8.0, temperature not specified in the publication
45.8
Urea
mutant enzyme Y1324F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
61.8
Urea
mutant enzyme D1564N, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
64.9
Urea
mutant enzyme Y1628F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
68.7
Urea
mutant enzyme E1792A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
210.8
Urea
wild type enzyme, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
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0.0029
Urea
mutant enzyme K1605A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
0.041
Urea
mutant enzyme D1321A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
3.87
Urea
mutant S177A, pH 8.0, temperature not specified in the publication
4.3
Urea
mutant enzyme Y1628F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
4.45
Urea
mutant K1605A, pH 8.0, temperature not specified in the publication
5.5
Urea
mutant enzyme D1564N, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
5.9
Urea
mutant enzyme Y1324F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
8.31
Urea
mutant G559E/G572E, pH 8.0, temperature not specified in the publication
40.9
Urea
isolated urea carboxyxlase domain plus allophanate hydrolase domain, pH 8.0, temperature not specified in the publication
54.6
Urea
wild-type, pH 8.0, temperature not specified in the publication
58.7
Urea
mixture of mutants S177A and mutant K1605A, pH 8.0, temperature not specified in the publication
176
Urea
mutant enzyme E1792A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
659
Urea
wild type enzyme, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
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Roon, R.J.; Levenberg, B.
An adenosine triphosphate-dependent avidin-sensitive enzymatic cleavage of urea in yeast and green algae
J. Biol. Chem.
243
5213-5215
1968
Cyberlindnera jadinii, Pseudochlorella pringsheimii, Auxenochlorella pyrenoidosa
brenda
Whitney, P.A.; Cooper, T.G.
Urea carboxylase and allophanate hydrolase. Two components of adenosine triphosphate:urea amido-lyase in Saccharomyces cerevisiae
J. Biol. Chem.
247
1349-1353
1972
Saccharomyces cerevisiae
brenda
Roon, R.J.; Levenberg, B.
Urea amidolyase. I. Properties of the enzyme from Candida utilis
J. Biol. Chem.
247
4107-4113
1972
Saccharomyces cerevisiae, Debaryomyces subglobosus, Cyberlindnera jadinii, Chlamydomonas reinhardtii, Pseudochlorella pringsheimii, Auxenochlorella pyrenoidosa
brenda
Whitney, P.A.; Cooper, T.G.
Urea carboxylase and allophanate hydrolase: two components of a multienzyme complex in Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
49
45-51
1972
Saccharomyces cerevisiae
brenda
Roon, R.J.; Hampshire, J.; Levenberg, B.
Urea amidolyase. The involvement of biotin in urea cleavage
J. Biol. Chem.
247
7539-7545
1972
Saccharomyces cerevisiae, Cyberlindnera jadinii
brenda
Whitney, P.A.; Cooper, T.
Urea carboxylase from Saccharomyces cerevisiae. Evidence for a minimal two-step reaction sequence
J. Biol. Chem.
248
325-330
1973
Saccharomyces cerevisiae
brenda
Leftley, J.W.; Syrett, P.J.
Urease and ATP: urea amidolyase activity in unicellular algae
J. Gen. Microbiol.
77
109-115
1973
Ankistrodesmus braunii, Asterococcus superbus, Chlamydomonas reinhardtii, Chlorophyceae, Dunaliella primolecta, Nannochloris bacillaris, Marvania coccoides, Scenedesmus basiliensis, Tetradesmus obliquus
-
brenda
Castric, P.A.; Levenberg, B.
Urea amidolyase of Candida utilis. Characterization of the urea cleavage reactions
Biochim. Biophys. Acta
438
574-583
1976
Cyberlindnera jadinii
brenda
Waheed, A.; Castric, P.A.
Purification and properties of the urea amidolyase from Candida utilis
J. Biol. Chem.
252
1628-1632
1977
Cyberlindnera jadinii
brenda
Metz, W.; Reuter, G.
Anabole und katabole Enzyme des Harnstoffmetabolismus in einem kohlenwasserstoffverwertenden Stamm von Candida guilliermondii
Z. Allg. Mikrobiol.
17
599-610
1977
Meyerozyma guilliermondii
brenda
Sumrada, R.A.; Cooper, T.G.
Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast
J. Biol. Chem.
257
9119-9127
1982
Saccharomyces cerevisiae
brenda
Rees, T.A.V.; Bekheet, I.A.
The role of nickel in urea assimilation by algae
Planta
156
386-387
1982
[Chlorella] fusca
-
brenda
Kimura, S.; Iyama, S.; Yamaguchi, Y.; Hayashi, S.; Fushimi, R.; Amino, N.
New enzymatic assay with urea amidolyase for determining potassium in serum
Ann. Clin. Biochem.
34
384-388
1997
Saccharomyces cerevisiae
brenda
Genbauffe, F.S.; Cooper, T.G.
The urea amidolyase (DUR1,2) gene of Saccharomyces cerevisiae
DNA Seq.
2
19-32
1991
Saccharomyces cerevisiae
brenda
Jones, R.A.; Montague, M.J.; Taylor, J.
Urease and urea amidolyase determination of activity in liverworts
Phytochemistry
12
1675-1676
1973
no activity in Marchantia polymorpha
-
brenda
Kimura, S.; Iyama, S.; Yamaguchi, Y.; Kanakura, Y.
New enzymatic assay for serum urea nitrogen using urea amidolyase
J. Clin. Lab. Anal.
17
52-56
2003
Saccharomyces cerevisiae (P32528), Saccharomyces cerevisiae
brenda
Kanamori, T.; Kanou, N.; Atomi, H.; Imanaka, T.
Enzymatic characterization of a prokaryotic urea carboxylase
J. Bacteriol.
186
2532-2539
2004
Oleomonas sagaranensis (Q75RY4), Oleomonas sagaranensis
brenda
Navarathna, D.H.; Harris, S.D.; Roberts, D.D.; Nickerson, K.W.
Evolutionary aspects of urea utilization by fungi
FEMS Yeast Res.
10
209-213
2010
Aspergillus fumigatus, Aspergillus nidulans, Candida albicans, Clavispora lusitaniae, Eremothecium gossypii, Fusarium graminearum, Kluyveromyces lactis, Parastagonospora nodorum, Pyricularia grisea, Saccharomyces cerevisiae (P32528), [Candida] glabrata
brenda
Navarathna, D.; Das, A.; Morschhauser, J.; Nickerson, K.; Roberts, D.
Dur3 is the major urea transporter in Candida albicans and is co-regulated with the urea amidolyase Dur1,2
Microbiology
157
270-279
2011
Candida albicans
brenda
Strope, P.K.; Nickerson, K.W.; Harris, S.D.; Moriyama, E.N.
Molecular evolution of urea amidolyase and urea carboxylase in fungi
BMC Evol. Biol.
11
80
2011
Aspergillus fumigatus, Aspergillus nidulans, Aspergillus terreus, Bipolaris maydis, Cryptococcus neoformans, Fusarium oxysporum, Fusarium verticillioides, Fusarium solani, Nitrosomonas europaea, Parastagonospora nodorum, Sorangium cellulosum
brenda
Fan, C.; Chou, C.Y.; Tong, L.; Xiang, S.
Crystal structure of urea carboxylase provides insights into the carboxyltransfer reaction
J. Biol. Chem.
287
9389-9398
2012
Kluyveromyces lactis (Q6CP22), Kluyveromyces lactis, Kluyveromyces lactis ATCC 8585 (Q6CP22)
brenda
Zhao, J.; Zhu, L.; Fan, C.; Wu, Y.; Xiang, S.
Structure and function of urea amidolyase
Biosci. Rep.
38
pii: BSR20171617
2018
Kluyveromyces lactis (Q6CP22), Kluyveromyces lactis DSM 70799 (Q6CP22)
brenda
Lin, Y.; Boese, C.; St. Maurice, M.
The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent
Protein Sci.
25
1812-1824
2016
Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato ATCC BAA-871
brenda