Information on EC 3.5.1.75 - urethanase

Substrates: substrate specificity
Products: -

additional information

Substrates: no activity with urea, methylurea, ethylurea, n-butylurea, tert-butylurea, phenylurea
Products: -

additional information

Substrates: no activity with glycinamide, N-alkyl ureas, N-allylurea, ethyl esters of organic acids, ethyl acetate, ethyl benzoate, diethyl carbonate, phenylphosphorodiamide, phenylthiophosphorodiamide, N-benzoylphosphoric triamide
Products: -

additional information

Substrates: enzyme additionally cleavs the amide bonds in 1-acetamidonaphthalene and para-nitroacetanilide
Products: -

additional information

Substrates: the bacterium that degrades aliphatic and aromatic urethane compounds, it also hydrolyzes anilides, amides, and esters
Products: -

additional information

Substrates: substrate specificity, overview, no activity with L-leucine-4-nitroanilide, methyl benzoate, and ethyl benzoate
Products: -

additional information

Substrates: the bacterium that degrades aliphatic and aromatic urethane compounds, it also hydrolyzes anilides, amides, and esters
Products: -

additional information

Substrates: the enzyme exhibits not only urease activity, but also urethanase activity
Products: -

additional information

Substrates: the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
Products: -

additional information

Substrates: the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
Products: -

additional information

Substrates: high-sensitive electrochemical determination of ethyl carbamate using urethanase and glutamate dehydrogenase modified electrode, with high selectivity during biorecognition between enzymes and the targets, overview
Products: -

additional information

Providencia rettgeri CGMCC 8326

Substrates: the enzyme exhibits not only urease activity, but also urethanase activity
Products: -

additional information

Providencia rettgeri CGMCC 8326

Substrates: the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
Products: -

additional information

Providencia rettgeri CGMCC 8326

Substrates: the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
Products: -

additional information

Providencia rettgeri CGMCC 8326

additional information

Providencia rettgeri JN-B815

Substrates: the enzyme exhibits not only urease activity, but also urethanase activity
Products: -

additional information

Providencia rettgeri JN-B815

Substrates: the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
Products: -

additional information

Providencia rettgeri JN-B815

Substrates: the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
Products: -

additional information

Providencia rettgeri JN-B815

additional information

Substrates: no or poor activity with gamma-aminobutyric acid, glutamic acid, and glycine
Products: -

additional information

Substrates: a highly sensitive spectrophotometric method for ethyl carbamate (EC) determination is established through glutamate dehydrogenase/urethanase cascade reactions and the corresponding change in NADH concentration. The absorbance at 340 nm is linearly related to the EC concentration within the range of 300-5000 nM, with a low detection limit of 9.28 nM. Method optimization. The absorbance declines slowly at either pH 4.5 or pH 8.0, which is around the optimal pH of one of the enzymes. But the absorbance decreases with the fastest rate at pH 6.0
Products: -

additional information

Substrates: no or poor activity with gamma-aminobutyric acid, glutamic acid, and glycine
Products: -

additional information

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

ethylcarbamate + H2O

CO2 + NH3 + ethanol

hexamethylene dicarbamic acid dibutyl ester + H2O

methylene bisphenyl dicarbamic acid dibutyl ester + H2O

toluene-2,4-dicarbamic acid dibutyl ester + H2O

toluene diamine + ?

urethane + H2O

ethanol + CO2 + NH3

7 entries

additional information

ethylcarbamate + H2O

CO2 + NH3 + ethanol

Substrates: urethane, potentially carcinogenic, mutagenic and teratogenic to human
Products: equimolar amounts of ammonia and ethanol

ethylcarbamate + H2O

CO2 + NH3 + ethanol

Substrates: urethane, potentially carcinogenic, mutagenic and teratogenic to human
Products: noncarcinogenic compounds

ethylcarbamate + H2O

CO2 + NH3 + ethanol

Substrates: enzyme may play an important role in detoxification of urethane
Products: noncarcinogenic compounds

ethylcarbamate + H2O

CO2 + NH3 + ethanol

Substrates: enzyme may play an important role in detoxification of urethane
Products: equimolar amounts of ammonia and ethanol

hexamethylene dicarbamic acid dibutyl ester + H2O

Substrates: -
Products: -

hexamethylene dicarbamic acid dibutyl ester + H2O

Substrates: -
Products: -

methylene bisphenyl dicarbamic acid dibutyl ester + H2O

Substrates: -
Products: -

methylene bisphenyl dicarbamic acid dibutyl ester + H2O

Substrates: -
Products: -

toluene-2,4-dicarbamic acid dibutyl ester + H2O

toluene diamine + ?

Substrates: -
Products: -

toluene-2,4-dicarbamic acid dibutyl ester + H2O

toluene diamine + ?

Substrates: -
Products: -

urethane + H2O

ethanol + CO2 + NH3

754024, 754697, 753406

Substrates: -
Products: -

urethane + H2O

ethanol + CO2 + NH3

Providencia rettgeri CGMCC 8326

754024, 754697, 753406

Substrates: -
Products: -

urethane + H2O

ethanol + CO2 + NH3

Providencia rettgeri JN-B815

754024, 754697, 753406

Substrates: -
Products: -

urethane + H2O

ethanol + CO2 + NH3

Substrates: -
Products: -

urethane + H2O

ethanol + CO2 + NH3

Substrates: -
Products: -

urethane + H2O

ethanol + CO2 + NH3

733136, 733131, 752484

Substrates: -
Products: -

urethane + H2O

ethanol + CO2 + NH3

733136, 733131, 752484

Substrates: -
Products: -

additional information

Substrates: the bacterium that degrades aliphatic and aromatic urethane compounds, it also hydrolyzes anilides, amides, and esters
Products: -

additional information

Substrates: the bacterium that degrades aliphatic and aromatic urethane compounds, it also hydrolyzes anilides, amides, and esters
Products: -

additional information

Substrates: the enzyme exhibits not only urease activity, but also urethanase activity
Products: -

additional information

Substrates: the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
Products: -

additional information

Providencia rettgeri CGMCC 8326

Substrates: the enzyme exhibits not only urease activity, but also urethanase activity
Products: -

additional information

Providencia rettgeri CGMCC 8326

Substrates: the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
Products: -

additional information

Providencia rettgeri JN-B815

Substrates: the enzyme exhibits not only urease activity, but also urethanase activity
Products: -

additional information

Providencia rettgeri JN-B815

Substrates: the enzyme exhibits not only urease activity (cf. acid urease, EC 3.5.1.5), but also urethanase activity
Products: -

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

additional information

does not require any cofactor

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Fe3+

strain IFO 12107, iron-containing urethanase, contains a typical high-spin Fe3+

Mg2+

20% activation at 1 mM

NEM

12% activation at 1 mM

Zn2+

probably belongs to category of Zn enzyme

additional information

6 entries

additional information

no effect, activation by 1 mM Co2+, Ni2+, Mn2+, Cu2+, Mg2+, Zn2+, Fe2+, Ca2+

additional information

metal ions not required

additional information

metal ions not required

additional information

metal ions not required

additional information

no effect of Ca2+, Mg2+, Na+, major cations of sea water

additional information

no effect, activation by Co2+, Ni2+, Mn2+, Fe2+, Cu2+, Ca2+

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1,10-phenanthroline

strong inhibition

4-chloromercuribenzoate

37% inhibition at 1 mM

Ag+

1 mM: complete inhibition

bathophenanthroline

complete inhibition, activity fully restored by addition of Fe3+ at a ratio of 4 iron atoms to 1 mol inactive protein, the apoenzyme

Cd2+

18% inhibition at 1 mM

Co2+

Cu2+

EDTA

ethanol

50% inhibition at 30% v/v

F-

1 mM: complete inhibition

Fe2+

1 mM: 67% inhibition, 10 mM: complete inhibition

Hg2+

iodoacetamide

iodoacetic acid

0.1 mM: 40% inhibition

Mn2+

slight inhibition

N-Benzoylphosphoric triamide

Ni2+

O,O-Dimethyl-O-(2,2-dichlorovinyl) phosphate

O,O-Dimethyl-O-(3-methyl-4-nitrophenyl) phosphate

p-chloromercuribenzoate

0.1 mM: 52% inhibition

phenylmethylsulfonyl fluoride

phenylphosphorodiamide

phenylthiophosphorodiamide

phosphoramidon

PMSF

84% inhibition at 1 mM

Sodium laurylsulfate

35 mM: complete inhibition

Zn2+

additional information

5 entries

Co2+

1 mM: 41% inhibition, 20 mM: complete inhibition

Co2+

11% inhibition at 1 mM

Cu2+

1 mM: 37% inhibition, 20 mM: 69% inhibition

Cu2+

61% inhibition at 1 mM

EDTA

no inhibition

EDTA

no inhibition

EDTA

no inhibition

EDTA

strong inhibition, 0.00074 mM: 50% inhibition. Complete inhibition fully recovered by addition of Zn2+, but no activity recovered by addition of Mg2+

Hg2+

1 mM: complete inhibition

Hg2+

98% inhibition at 1 mM

iodoacetamide

no inhibition at 0.1 mM

iodoacetamide

0.1 mM: 48% inhibition

Ni2+

1 mM: 14% inhibition, 20 mM: 58% inhibition

Ni2+

32% inhibition at 1 mM

phenylmethylsulfonyl fluoride

PMSF

phenylmethylsulfonyl fluoride

0.1 mM: 61% inhibition; PMSF

Zn2+

1 mM: 29% inhibition, 25 mM: complete inhibition

Zn2+

21% inhibition at 1 mM

additional information

no inhibition by 1 mM EDTA or 1 mM EGTA

additional information

no inhibition by 1 mM EDTA and 2-mercaptoethanol

additional information

no inhibition by 1 mM EDTA and 2-mercaptoethanol; no inhibition by diethyldicarbonate, N-ethylmaleimide or iodoacetamide at 0.1 mM

additional information

no inhibition by EDTA

additional information

no or poor inhibition by Mn2+, EDTA, 8-hydroxyquinoline, DTT, and iodoacetamide

show all columns Go to Activating Compound Search

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

Triton X-100

slight activation, activation depending on increasing concentrations of Triton X-100

additional information

the enzyme is strongly induced by acetanilide, effect of carbon sources and inducers on cell growth, overview

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.15

4-nitroacetanilide

pH 7.0, 30°C

0.07

4-nitrophenyl acetate

pH 7.0, 30°C

0.1

4-nitrophenylbutyrate

pH 7.0, 30°C

acetamide

pH 7.0, 30°C

0.13

acetanilide

pH 7.0, 30°C

11.8

Benzamide

pH 7.0, 30°C

2.5

butyramide

pH 7.0, 30°C

4.86 - 6.59

ethyl carbamate

5 entries

0.07

ethyl N-phenylcarbamate

pH 7.0, 30°C

2.49

L-alanine 4-nitroanilide

pH 7.0, 30°C

9.4

phenyl acetamide

pH 7.0, 30°C

0.0272 - 56

urethane

additional information

4.86

ethyl carbamate

mutant N194V, 40°C, pH not specified in the publication

6.03

ethyl carbamate

wild-type, 40°C, pH not specified in the publication

6.36

ethyl carbamate

mutant Y133A, 40°C, pH not specified in the publication

6.37

ethyl carbamate

mutant T111L, 40°C, pH not specified in the publication

6.59

ethyl carbamate

pH 7.0, 30°C

0.0272

urethane

pH 6.0, 50°C

0.078

urethane

0.17

urethane

strain IFO 12107

0.88

urethane

1.6

urethane

urethane

strain 1013, at pH 4.5

urethane

urethane

strain 1013, at pH 7.5

additional information

kinetic properties

additional information

kinetic data

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1.29 - 2.91

ethyl carbamate

1.29

ethyl carbamate

mutant Y133A, 40°C, pH not specified in the publication

1.68

ethyl carbamate

mutant T111L, 40°C, pH not specified in the publication

2.84

ethyl carbamate

mutant N194V, 40°C, pH not specified in the publication

2.91

ethyl carbamate

wild-type, 40°C, pH not specified in the publication

show all columns Go to kcat/KM Value Search

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.20266 - 0.58452

ethyl carbamate

0.20266

ethyl carbamate

mutant Y133A, 40°C, pH not specified in the publication

0.26368

ethyl carbamate

mutant T111L, 40°C, pH not specified in the publication

0.48291

ethyl carbamate

wild-type, 40°C, pH not specified in the publication

0.58452

ethyl carbamate

mutant N194V, 40°C, pH not specified in the publication

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.003

0.004

mutant E210D, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.005

mutant S198K, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.008

mutant G205H, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.009

0.012

0.014

wild-type, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.016

0.018

mutant H199T, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.038

mutant S198G, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.041

strain IFO 12107

0.135

mutant S198K, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.177

mutant A365R, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.254

0.371

mutant F306V, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.377

isoform SP-2, pH 8, 30°C

0.437

mutant T211W, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.447

mutant N207Y, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.491

mutant S131A, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.551

mutant H199K, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.651

isoform SP-3, pH 8, 30°C

0.736

mutant A365P, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.749

isoform SP-1, pH 8, 30°C

0.76

0.778

mutant G205D, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.797

mutant S198G, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.912

mutant N207D, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.995

mutant G205H, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

1.127

mutant G299R, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

1.215

mutant G127M, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

2.37

mutant Y133A, 40°C, pH not specified in the publication

2.55

mutant T111L, 40°C, pH not specified in the publication

3.15

wild-type, 40°C, pH not specified in the publication

3.3

mutant N194V, 40°C, pH not specified in the publication

3.8

purified recombinant apoenzyme, urethanase activity, pH 4.5, temperature not specified in the publication

4.6

purified enzyme, urethanase activity, pH 4.5, 37°C

purified native enzyme

additional information

0.003

mutant T211W, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.003

mutant A365P, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.009

mutant E210D, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.009

mutant S131A, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.012

mutant S171C, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.012

mutant G299R, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.016

mutant G127M, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.016

mutant N207D, substrate ethyl N-nitrophenylcarbamate, pH 7.5, 23°C

0.76

wild-type, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

0.76

mutant H199T, substrate 7-carbethoxyamino-4-methylcoumarin, pH 7.5, 23°C

additional information

additional information

additional information

additional information

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4.5

5.5

6 - 8

7 - 8

7.5

strain 1013, pH-optimum at, a second, higher pH-optimum at pH 4.5

additional information

isoforms SP-1, SP-2, SP-3

4.5

4.5

strain 1013, highest pH-optimum at, second pH-optimum at pH 7.5

4.5

assay at

4.5

recombinant enzyme

4.5

assay at

733136, 733131

6 - 8

6 - 8

7 - 8

7 - 8

additional information

pI: 5.5

additional information

significantly higher urethanase activity at acidic condition than at neutral condition

additional information

significantly higher urethanase activity at acidic condition than at neutral condition

additional information

significantly higher urethanase activity at acidic condition than at neutral condition

additional information

significantly higher urethanase activity at acidic condition than at neutral condition

show all columns Go to pH Range Search

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

3 - 10

activity range, profile overview

3 - 8.5

activity range, recombinant enzyme, profile overview

4 - 8.5

half of maximum activity at pH 4.0 and pH 8.5

5.5

about 50% of maximum activity at pH 5.5

5.5 - 10

6 - 7

pH 6.0: 98% of maximum activity, pH 7.0: 78% of maximum activity

additional information

urethanase activity sharply declines in alkaline region

no activity at pH 5 or below

half of maximum activity at pH 5.0

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

isoform SP-3

wild-type, mutant I97L

isoforms SP-1, SP-2

assay at

assay at

mutants G195A, I97L/G195A

733136, 733131

show all columns Go to Temperature Range Search

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TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

20 - 50

strain 1013, about 50% of maximum activity at 20°C and 50°C

30 - 50

activity between

40 - 60

40% of maximum activity

22% of maximum activity

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

UniProt

brenda

UniProt

brenda

isolated from mouse feces

brenda

marine bacterium, associated with the marine sponge, Spirastrella species

brenda

brenda

IAM 1034

Paenibacillus thiaminolyticus IAM 1034

brenda

IAM 1034

brenda

isolated from mineral medium

brenda

isolated from mineral medium

brenda

753406, 754024, 754697

brenda

Providencia rettgeri CGMCC 8326

753406, 754024, 754697

brenda

Providencia rettgeri JN-B815

753406, 754024, 754697

brenda

brenda

brenda

brenda

brenda

eight strains, highest activity in strain IFO 12107

brenda

gastrointestinal bacterium

209235, 209236

brenda

sp. 1013, isolated from mouse gastrointestine

brenda

brenda

isolated DNA from soil from a site that had been exposed to polyurethanes

brenda

733136, 752484

brenda

isolated from mouse gastrointestine

brenda

733136, 752484

brenda

isolated from mouse gastrointestine

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

highest activity

brenda

brenda

brenda

additional information

cell culture

urethanase activity detected in the cells not in the culture medium

brenda

cell culture

urethanase activity detected in the cells not in the culture medium

brenda

cell culture

80% of urethanase activity is cell associated

brenda

mycelium

brenda

mycelium

brenda

additional information

urethanase activity detected in the cells not in the culture medium

brenda

additional information

urethanase activity detected in the cells not in the culture medium

brenda

additional information

80% of urethanase activity is cell associated

brenda

additional information

effect of carbon sources and inducers on cell growth, overview

brenda

additional information

effect of carbon sources and inducers on cell growth, overview

brenda

additional information

tissue distribution

brenda

additional information

identification of strain CGMCC 5081 and culture condition optimization for enzyme production in immobilized cells, best at pH 3.0-7.0, 30°C

brenda

additional information

identification of strain CGMCC 5081 and culture condition optimization for enzyme production in immobilized cells, best at pH 3.0-7.0, 30°C

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

cytosol

3 entries

extracellular

brenda

lysosome

highest activity, located mainly in the lysosomal fraction

brenda

brenda

moderate activity

brenda

additional information

intracellular distribution

brenda

cytosol

strain 1013, 70% of activity in a cytosolic fraction

brenda

80% of activity in a cytosolic fraction

brenda

moderate activity

brenda

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

additional information

physiological function

urethanase can directly catalyze the decomposition of urethane, which has potential carcinogenic and teratogenic effects and exists widely in various fermented foods and alcoholic beverages

physiological function

urethanase can directly catalyze the decomposition of urethane, which has potential carcinogenic and teratogenic effects and exists widely in various fermented foods and alcoholic beverages

additional information

residue S176 in SP-1 acts as nucleophile, attacking substrate carbonyls. S176 is deprotonated catalytic base S152.S152 is deprotonated by the K77

additional information

enzyme conatins the catalytic triad Ser-cisSer-Lys of the amidase family

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

Q9AHE8 pBLAST

AMDA_RHIRD

Rhizobium radiobacter

517

55888

Swiss-Prot

Show Sequence

other Location (Reliability: 3)

A0A679EIJ6 pBLAST

A0A679EIJ6_CANPA

Sphingomonas yantingensis

551

61741

TrEMBL

Show Sequence

A0A7W9ANY4 pBLAST

A0A7W9ANY4_9SPHN

433

45098

TrEMBL

Show Sequence

other Location (Reliability: 1)

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PDB

SCOP

CATH

UNIPROT

ORGANISM

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

13700

x * 13700, SDS-PAGE

160000

strain IFO 12107, gel filtration

240000

blue native PAGE

42000

strain IFO 12107, homotetramer, 4 * 42000, SDS-PAGE

55000

approximately, gel filtration

96000

gel filtration

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

monomer

oligomer

tetramer

additional information

x * 61570, SDS-PAGE

Providencia rettgeri CGMCC 8326

x * 61570, SDS-PAGE

Providencia rettgeri JN-B815

x * 61570, SDS-PAGE

monomer

1 * 55000, SDS-PAGE

monomer

1 * 55000, SDS-PAGE

oligomer

x * 13700, SDS-PAGE

oligomer

x * 13700, SDS-PAGE

tetramer

strain IFO 12107, homotetramer, 4 * 42000, SDS-PAGE

tetramer

4 * 60000, SDS-PAGE

additional information

peptide map fingerprinting analysis by MALDI/TOF-TOF mass spectrometry, the N-terminal sequence of urethanase is GTNTADNDAA

additional information

peptide map fingerprinting analysis by MALDI/TOF-TOF mass spectrometry, the N-terminal sequence of urethanase is GTNTADNDAA

Go to Crystallization (commentary) Search

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structure to 2.66 A resolution

structure in ligand-free form, to 2.67 A resolution

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

A172G

about 50% of wild-type activity

G195A

about 190% of wild-type

I97L

about 110% of wild-type activity

I97L/G195A

about 310% of wild-type activity. Catalyitc activity is 2442 U/l, and ethanol tolerance is 1.5fold increased

L200C

about 60% of wild-type activity

N175G

about 25% of wild-type activity

P163A

about 50% of wild-type activity

R94P

activity similatr to wild-type

N194V

mutant's urethanase activity is increased by 6.12%, the catalytic efficiency by 21.04%, and the enzyme stability is also enhanced

T111L

about 50% of wild-type catalytic efficiency

Y133A

about 40% of wild-type catalytic efficiency

A365P

mutation does not affect the hydrolysis of 7-carbethoxyamino-4-methylcoumarin but reduces the activity for the other substrates

A365R

mutation almost abolishes activity

E210D

exhibits a strongly reduced activity against 7-carbethoxyamino-4-methylcoumarin and N-nitrophenylcarbamate

F306L

mutant displays a decrease in activity with carbamates, hydrolysis of the acetamides is improved

F306V

mutant displays a decrease in activity with carbamates, hydrolysis of the acetamides is improved

G127M

exhibits a 1.6- and 1.2fold improved activity against 7-carbethoxyamino-4-methylcoumarin and N-nitrophenylcarbamate, respectively

G205D

activity with 7-carbethoxyamino-4-methylcoumarin similar to wild-type

G205H

mutant displays increased activity

G299R

exhibits a slightly improved activity against 7-carbethoxyamino-4-methylcoumarin

H199K

mutant displays a decrease in overall activity

H199T

mutant displays a decrease in overall activity

N207D

mutant displays a strong decrease in overall activity

N207Y

mutant displays a strong decrease in overall activity

S131A

exhibits a slightly improved activity against 7-carbethoxyamino-4-methylcoumarin and N-nitrophenylcarbamate

S171C

exhibits a strongly reduced activity against 7-carbethoxyamino-4-methylcoumarin and N-nitrophenylcarbamate

S198G

activtiy similar to wild-type

S198K

mutant displays a decrease in overall activity

T211W

mutant displays a decrease in activity with carbamates, hydrolysis of the acetamides is improved

additional information

6 entries

additional information

crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) are prepared using genipin as crosslinking agent, method, overview. Optimal at 0.3 g/l of bovine serum albumin. The aggregates remove urea, but the treatment with PRU-CLEAs reveals no significant change of volatile flavor substances in Chinese rice wine. By using urea as the substrate, the values of Km and Vmax of free urease from Providencia rettgeri JN-B815 are estimated to be 5.99 mmol/l and 840 nmol/min, while those of immobilized urease are 13.54 mmol/l and 940 nmol/min, respectively. By using urethane as the substrate, the Km and Vmax value of free urethanase are determined to be 183.82 mmol/l and 970 nmol/min, while those of immobilized enzyme are 705.78 mmol/l and 650 nmol/min, respectively

additional information

development of an amperometric biosensor for ethyl carbamate (urethane) with urethanase and glutamate dehydrogenase (GLDH). Urethanase decomposes ethyl carbamate to produce ammonia, which is converted to L-glutamate under the catalysis of GLDH in the presence of 2-oxoglutarate and NADH. The two enzymes are entrapped into chitosan/gelatine/gamma-glycidoxy propyl trimethoxy silane sol-gel and immobilized on the surface of pyrolytic graphite electrode (PGE). The modified electrode is characterized by cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). Under the optimized conditions, the amperometric EC biosensor exhibits a linear detection range from 0.0005 to 0.040 mM with a low detection limit of 5.30 nM. The biosensor is successfully used to detect urethane in mimic Chinese rice wine samples, and satisfactory recovery and relative standard deviation are achieved

additional information

Providencia rettgeri CGMCC 8326

additional information

Providencia rettgeri CGMCC 8326

additional information

Providencia rettgeri JN-B815

additional information

Providencia rettgeri JN-B815

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

1 - 2

1 h, 4°C, 50% of maximal activity remaining

4 - 8

strain IFO 12107, stable between

4.5 - 7.5

strain 1013, 37°C, 30 min, stable between

1 h, 4°C, 50% of maximal activity remaining,

5 - 8

stable between

7 - 10

stable at, 1 h, 4°C, over 80% activity remaining

7 - 9

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purified native enzyme, stable at

8 - 10

stable

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

12 h, no residual activity for isoform SP-3

12 h, 44% for isoform SP-1

40 - 50

purified native enzyme, stable at

40 - 60

rapid inactivation at pH 4.0, more slowly inactivation at 60°C

stable up to, 1 h, stability sharply declined above

strain IFO 12107, stable below

half-life of enzyme at 60°C: 30 min

15 min, complete loss of activity

1 h, complete loss of activity

strain 1013, pH 4.5-7.5, 30 min, stable at

12 h, 48% for isoform SP-1

unstable above

halflife 31.5 min for wild-type, 210.0 min for mutant N194V

strain 1013, 1 h, complete loss of activity

half-life of enzyme at 50°C: 120 min

stable at for 1 h

stable up to

show all columns Go to Organic Solvent Search

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ORGANIC SOLVENT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

DMSO

isoforms SP-1, SP-2 are most active in presence of 10% DMSO

Ethanol

Ethanol

strain IFO 12107, considerably resistant to high concentrations of ethanol, 64% of the activity retained in 20% ethanol, great advantage for industrial removal of urethane from alcoholic beverages

Ethanol

strain 1013, 20% ethanol, 54% residual activity after 2 h at 37°C and pH 4.5

Ethanol

20%, 73% of initial activity, enzyme is stable in 0%-40% ethanol solutions

Ethanol

inactive at high concentrations of alcohol, 20% ethanol, 8.9% residual activity after 2 h at 37°C

Ethanol

100% resistant to 10%, v/v, ethanol, above 10% ethanol the activity decreased depending upon ethanol concentration, resistant to 20%, v/v, ethanol: 82% activity remained

Ethanol

20% ethanol, 20% residual activity after 2 h at 37?C

Paenibacillus thiaminolyticus IAM 1034

Ethanol

20% ethanol, 20% residual activity after 2 h at 37?C

Ethanol

no resistance to ethanol

Go to Oxidation Stability Search

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OXIDATION STABILITY

ORGANISM

UNIPROT

LITERATURE

the enzyme exhibits ethanol tolerance, 50% activity remaining at 27% ethanol, 65% activity remaining at 15% ethanol

733131

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

native enzyme by ultrasonication, concentration by PEG 20000, gel filtration, and ultrafilatration

native enzyme to homogeneity by ammonium sulfate fractionation, gel filtration, and ion exchange chromatography

native enzyme, purified using ion-exchange chromatography

native urethanase 3.1fold by ethanol precipitation, and anion exchange chromatography

partial

recombinant His-tagged enzyme, refolded from Escherichia coli strain BL21(DE3) inclusion bodies, 1.22fold by nickel affinity chromatography

strain IFO 12107

Go to Cloned (commentary) Search

partial

partial

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

DNA and amino acid sequence determination and analysis

expression in Escherichia coli

expression in Saccharomyces cerevisiae

gene ureC, functional recombinant expression of His-tagged enzyme from operon ureABC in Escherichia coli strain BL21(DE3) in inclusion bodies

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

expression is increased by growth on polyurethane

Go to Renatured Search

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

recombinant His-tagged enzyme is solubilized and refolded from Escherichia coli strain BL21(DE3) inclusion bodies. Secondary structure analysis of renatured recombinant urease

show all columns Go to Application Search

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

analysis

degradation

food industry

nutrition

analysis

the enzyme is used in spectrophotometric determination of ethyl carbamate through bi-enzymatic cascade reactions, method, overview. Detection of ethyl carbamate (urethane) in Chinese rice wine. Urethane is known as a genotoxic carcinogen1 that widely exists in fermented foods and alcoholic beverages, such as bread, yogurt, cheese, brandy, Chinese rice wine, sake, and wine, due to the natural biochemical processes in the fermentation process

analysis

degradation

use of a urethanase in a chemoenzymatic process for polyurethane foam recycling. The urethanase hydrolyses low molecular weight dicarbamates resulting from chemical glycolysis of polyether-polyurethane foam

degradation

Moraxella catarrhalis BMPPS3 is able to colonize on polyurethane surface and form a biofilm. Maximum urethanase activity is attained as 1.639 mM/min/mg enzyme at 25th day of growth on polyurethane

food industry

with good ethanol tolerance, the crude urethanase is able to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine without the change of flavor substance in wine

food industry

urethanase is useful to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine, strain CGMCC 5081 culture condition optimization for enzyme production in immobilized cells

food industry

with good ethanol tolerance, the crude urethanase is able to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine without the change of flavor substance in wine

food industry

crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) have great potential in the elimination of urethane (ethyl carbamate) from Chinese rice wine. Process flow diagram of PRU-CLEAs applied in membrane reactor, overview

food industry

with good ethanol tolerance, the crude urethanase is able to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine without the change of flavor substance in wine

food industry

urethanase is useful to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine, strain CGMCC 5081 culture condition optimization for enzyme production in immobilized cells

food industry

Providencia rettgeri JN-B815

food industry

Providencia rettgeri CGMCC 8326

nutrition

practically ineffective for the elimination of urethane from alcoholic beverages, because the enzyme is inactive in high concentrations of alcohol, ethanol, and at acidic pH

nutrition

enzyme may be practically applicable in removal of urethane from alcoholic beverages, because very high ethanol resistance, high activity at acidic condition, pH 5.0 and very low Km value for urethane

nutrition

great advantage for industrial removal of urethane, potentially carcinogenic, mutagenic and teratogenic to human, from alcoholic beverages

209235, 209236

nutrition

great advantage for industrial removal of urethane, potentially carcinogenic, mutagenic and teratogenic to human, from alcoholic beverages

nutrition

great advantage for industrial removal of urethane, potentially carcinogenic, mutagenic and teratogenic to human, from alcoholic beverages

nutrition

strain IFO 12107, enzyme may be a practical means of removing urethane from alcoholic beverages, because its higher activity under acidic conditions, pH 4.5, its high ethanol resistance and its low Km value for urethane

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Zhao, C.J.; Kobashi, K.

Purification and characterization of iron-containing urethanase from Bacillus licheniformis

Biol. Pharm. Bull.

773-778

1994

Bacillus licheniformis

7951136

brenda

Zhao, C.J.; Imamura, L.; Kobashi, K.

Urethanase of Bacillus licheniformis sp. isolated from mouse gastrointestine

Chem. Pharm. Bull.

3303-3306

1991

Bacillus licheniformis, Paenibacillus thiaminolyticus, Purpureocillium lilacinum, Paenibacillus thiaminolyticus IAM 1034

1814624

brenda

Kobashi, K.; Takebe, S.; Sakai, T.

Urethane-hydrolyzing enzyme from Citrobacter sp

Chem. Pharm. Bull.

1326-1328

1990

Citrobacter sp.

2393957

brenda

Zhao, C.J.; Kobashi, K.

Urethanase in rat tissues

J. Toxicol. Environ. Health

37-45

1992

Rattus norvegicus

1522612

brenda

Mohapatra, B.R.; Bapuji, M

Characterization of urethanase from Micrococcus species associated with the marine sponge (Spirastrella species)

Lett. Appl. Microbiol.

393-396

1997

Micrococcus sp.

brenda

Akutsu-Shigeno, Y.; Adachi, Y.; Yamada, C.; Toyoshima, K.; Nomura, N.; Uchiyama, H.; Nakajima-Kambe, T.

Isolation of a bacterium that degrades urethane compounds and characterization of its urethane hydrolase

Appl. Microbiol. Biotechnol.

422-429

2006

Prescottella equi, Prescottella equi TB-60

16041575

brenda

Zhou, N.D.; Gu, X.L.; Tian, Y.P.

Isolation and characterization of urethanase from Penicillium variabile and its application to reduce ethyl carbamate contamination in Chinese rice wine

Appl. Biochem. Biotechnol.

170

718-728

2013

Talaromyces variabilis, Talaromyces variabilis JN-A525

23609903

brenda

Wu, Q.; Zhao, Y.; Wang, D.; Xu, Y.

Immobilized Rhodotorula mucilaginosa: a novel urethanase-producing strain for degrading ethyl carbamate

Appl. Biochem. Biotechnol.

171

2220-2232

2013

Rhodotorula mucilaginosa, Rhodotorula mucilaginosa CGMCC 5081

24037516

brenda

Zhou, N.D.; Gu, X.L.; Zha, X.H.; Tian, Y.P.

Purification and characterization of a urethanase from Penicillium variabile

Appl. Biochem. Biotechnol.

172

351-360

2014

Talaromyces variabilis, Talaromyces variabilis JN-A525

24078254

brenda

Lu, X.; Zhou, N.; Tian, Y.

Spectrophotometric determination of ethyl carbamate through bi-enzymatic cascade reactions

Anal. Methods

1261-1264

2015

Talaromyces variabilis, Talaromyces variabilis JN-A525

brenda

Zhang, Z.; Lu, X.; Tian, Y.; Zhou, N.

High-sensitive electrochemical determination of ethyl carbamate using urethanase and glutamate dehydrogenase modified electrode

Electroanalysis

481-488

2017

Providencia rettgeri, Providencia rettgeri JN-B815, Providencia rettgeri CGMCC 8326

brenda

Zhang, Q.; Zha, X.; Zhou, N.; Tian, Y.

Preparation of crosslinked enzyme aggregates (CLEAs) of acid urease with urethanase activity and their application

J. Basic Microbiol.

422-431

2016

Providencia rettgeri, Providencia rettgeri JN-B815, Providencia rettgeri CGMCC 8326

26627914

brenda

Liu, X.; Zhang, Q.; Zhou, N.; Tian, Y.

Expression of an acid urease with urethanase activity in E. coli and analysis of urease gene

Mol. Biotechnol.

84-97

2017

Providencia rettgeri, Providencia rettgeri JN-B815, Providencia rettgeri CGMCC 8326

28197768

brenda

Branson, Y.; Soeltl, S.; Buchmann, C.; Wei, R.; Schaffert, L.; Badenhorst, C.P.S.; Reisky, L.; Jaeger, G.; Bornscheuer, U.T.

Urethanases for the enzymatic hydrolysis of low molecular weight carbamates and the recycling of polyurethanes

Angew. Chem. Int. Ed. Engl.

e202216220

2023

metagenome

36591907

brenda

Bayer, T.; Palm, G.J.; Berndt, L.; Meinert, H.; Branson, Y.; Schmidt, L.; Cziegler, C.; Somvilla, I.; Zurr, C.; Graf, L.G.; Janke, U.; Badenhorst, C.P.S.; Koenig, S.; Delcea, M.; Garscha, U.; Wei, R.; Lammers, M.; Bornscheuer, U.T.

Structural elucidation of a metagenomic urethanase and its engineering towards enhanced hydrolysis profiles

Angew. Chem. Int. Ed. Engl.

e202404492

2024

metagenome

38948941

brenda

Maheswaran, B.; Sebastin Raj, J.; Pandiyarajan, P.; Jaya Santhi, R.; Mythili, R.; K S, V.; Kim, W.; Karmegam, N.; Govarthanan, M.

Polyurethane degradation by extracellular urethanase producing bacterial isolate Moraxella catarrhalis strain BMPPS3

Environ. Res.

251

118631

2024

Moraxella catarrhalis

38452914

brenda

Yang, L.; Zhao, T.; Zhang, X.; Fan, T.; Zhang, Y.; Feng, Z.; Liu, J.

Crystal structure of urethanase from Candida parapsilosis and insights into the substrate-binding through in silico mutagenesis and improves the catalytic activity and stability

Int. J. Biol. Macromol.

134763

2024

Candida parapsilosis (A0A679EIJ6)

39151849

brenda

Yao, X.; Kang, T.; Pu, Z.; Zhang, T.; Lin, J.; Yang, L.; Yu, H.; Wu, M.

Sequence and structure-guided engineering of urethanase from Agrobacterium tumefaciens d3 for improved catalytic activity

J. Agric. Food Chem.

7267-7278

2022

Agrobacterium radiobacter (Q9AHE8)

35653287

brenda