BRENDA - Enzyme Database
show all sequences of 3.5.1.54

Production of urea amidolase by recombinant yeast and application to the enzymic determination of urea

Nishiya,Y.; Toda, A.; Kawamura, Y.; Seibutsu Shiro Bunseki 18, 288-293 (1995)
No PubMed abstract available

Data extracted from this reference:

Organism
Organism
UniProt
Commentary
Textmining
Cyberlindnera jadinii
-
-
-
Cyberlindnera jadinii CA (u)-37
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
as a component of urea amidolase, allophanate hydrolase domain inactivated, urea carboxylase activity detected
Cyberlindnera jadinii
Purification (Commentary) (protein specific)
Commentary
Organism
as a component of urea amidolase, allophanate hydrolase domain inactivated, urea carboxylase activity detected
Cyberlindnera jadinii
Other publictions for EC 3.5.1.54
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
753037
Zhao
Structure and function of ure ...
Kluyveromyces lactis, Kluyveromyces lactis ATCC 8585, Kluyveromyces lactis CBS 2359, Kluyveromyces lactis DSM 70799, Kluyveromyces lactis NBRC 1267, Kluyveromyces lactis NRRL Y-1140, Kluyveromyces lactis WM37
Biosci. Rep.
38
BSR20171617
2018
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-
1
1
3
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1
7
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11
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1
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14
2
3
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1
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1
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1
3
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1
7
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1
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14
2
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1
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2
2
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746393
Lin
The urea carboxylase and allo ...
Candida albicans, Candida albicans ATCC MYA-2876, Granulibacter bethesdensis, Granulibacter bethesdensis ATCC BAA-1260, Granulibacter bethesdensis CGDN1H1, Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato ATCC BAA-871D-5, Pseudomonas syringae pv. tomato DC3000, Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
Protein Sci.
25
1812-1824
2016
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1
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1
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1
10
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11
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15
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1
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11
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6
4
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1
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1
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10
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11
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1
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11
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6
4
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13
13
-
6
6
733179
Balotra
X-ray structure of the amidase ...
Pseudomonas sp.
Appl. Environ. Microbiol.
81
470-480
2015
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-
1
1
2
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1
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3
1
1
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1
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2
2
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752542
Balotra
X-Ray structure of the amidas ...
Pseudomonas sp. ADP
Appl. Environ. Microbiol.
81
470-480
2015
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1
1
1
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1
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1
1
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2
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753254
Zhang
-
Theoretical investigation on ...
Granulibacter bethesdensis, Granulibacter bethesdensis ATCC BAA-1260, Granulibacter bethesdensis CGDNIH1
Chem. Res. Chin. Univ.
31
1023-1028
2015
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1
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5
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3
3
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733034
Balotra
Crystallization and preliminar ...
Pseudomonas sp.
Acta crystallogr. Sect. F
70
310-315
2014
-
-
1
1
1
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2
1
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3
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1
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1
1
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1
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2
1
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2
2
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733342
Lin
The structure of allophanate h ...
Granulibacter bethesdensis, Granulibacter bethesdensis ATCC BAA-1260
Biochemistry
52
690-700
2013
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1
1
8
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2
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1
2
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5
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1
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4
1
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1
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8
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2
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1
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4
1
1
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1
1
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3
3
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8
8
734220
Fan
Structure and function of allo ...
Kluyveromyces lactis
J. Biol. Chem.
288
21422-21432
2013
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1
1
3
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2
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718475
Jacques
The structure of TTHA0988 from ...
no activity in Thermus thermophilus
Acta Crystallogr. Sect. D
67
105-111
2011
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667267
Shapir
Purification and characterizat ...
Enterobacter cloacae, Enterobacter cloacae 99
Appl. Environ. Microbiol.
72
2491-2495
2006
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1
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1
1
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1
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2
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6
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10
1
1
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1
1
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667259
Cheng
Allophanate hydrolase, not ure ...
Agrobacterium tumefaciens, Agrobacterium tumefaciens J14a, Enterobacter cloacae, Enterobacter cloacae 99, Herbaspirillum huttiense, Herbaspirillum huttiense NRRL B-12228, Pseudomonas sp., Ralstonia pickettii, Ralstonia pickettii D
Appl. Environ. Microbiol.
71
4437-4445
2005
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4
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9
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18
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19
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4
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9
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19
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1
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1
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668661
Kanamori
Allophanate hydrolase of Oleom ...
Oleomonas sagaranensis, Oleomonas sagaranensis HD-1
FEMS Microbiol. Lett.
245
61-65
2005
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1
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669098
Shapir
Purification and characterizat ...
Pseudomonas sp.
J. Bacteriol.
187
3731-3738
2005
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1
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3
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2
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2
1
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1
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1
1
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209193
Nishiya
-
Production of urea amidolase b ...
Cyberlindnera jadinii, Cyberlindnera jadinii CA (u)-37
Seibutsu Shiro Bunseki
18
288-293
1995
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1609
Sumrada
Urea carboxylase and allophana ...
Saccharomyces cerevisiae
J. Biol. Chem.
257
9119-9127
1982
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209196
Maitz
-
Purification and properties of ...
Chlamydomonas reinhardtii
Biochim. Biophys. Acta
714
486-491
1982
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1
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1602
Whitney
Urea carboxylase and allophana ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
49
45-51
1972
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