Information on EC 3.5.1.100 - (R)-amidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.100
-
RECOMMENDED NAME
GeneOntology No.
(R)-amidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-piperazine-2-carboxamide + H2O = (R)-piperazine-2-carboxylate + NH3
show the reaction diagram
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-
-
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beta-alaninamide + H2O = beta-alanine + NH3
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
(R)-piperazine-2-carboxamide amidohydrolase
In addition (R)-piperidine-3-carboxamide is hydrolysed to (R)-piperidine-3-carboxylic acid and NH3, and (R)-N-tert-butylpiperazine-2-carboxamide is hydrolysed to (R)-piperazine-2-carboxylic acid and tert-butylamine with lower activity. The enzyme does not act on the other amide substrates which are hydrolysed by EC 3.5.1.4 (amidase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2,2-dimethylcyclopropane carboxamide + H2O
(R)-2,2-dimethylcyclopropane carboxylic acid + NH3
show the reaction diagram
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-
-
-
?
(R)-2,2-dimethylcyclopropanecarboxamide + H2O
(R)-2,2-dimethylcyclopropanecarboxylic acid
show the reaction diagram
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amidase exhibits strict R-selectivity towards 2,2-dimethylcyclopropanecarboxamide
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?
(R)-piperazine-2-carboxamide + H2O
(R)-piperazine-2-carboxylic acid + NH3
show the reaction diagram
(R)-piperazine-2-tert-butylcarboxamide + H2O
(R)-piperazine-2-carboxylate + tert-butylamine
show the reaction diagram
(R)-piperidine-3-carboxamide + H2O
(R)-piperidine-3-carboxylic acid + NH3
show the reaction diagram
beta-alaninamide + H2O
beta-alanine + NH3
show the reaction diagram
D-glutamine amide + H2O
D-glutamic acid + NH3
show the reaction diagram
no formation of glutamine, 27% of the activity with (R)-piperazine-2-carboxamide
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?
L-glutamine amide + H2O
L-glutamic acid + NH3
show the reaction diagram
no formation of glutamine, 0.35% of the activity with (R)-piperazine-2-carboxamide
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?
piperidine-4-carboxamide + H2O
piperidine-4-carboxylic acid + NH3
show the reaction diagram
0.23% of the activity with (R)-piperazine-2-carboxamide
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-
?
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AgNO3
1 mM, incubation at 30°C for 10 min, complete inhibition
CdCl2
1 mM, incubation at 30°C for 10 min, complete inhibition
CoCl2
1 mM, incubation at 30°C for 10 min, complete inhibition
CuCl2
1 mM, incubation at 30°C for 10 min, complete inhibition
CuSO4
1 mM, incubation at 30°C for 10 min, complete inhibition
Fe(NH4)2(SO4)2
1 mM, incubation at 30°C for 10 min, 67% inhibition
FeCl3
1 mM, incubation at 30°C for 10 min, 78% inhibition
HgCl2
1 mM, incubation at 30°C for 10 min, complete inhibition
MnCl2
1 mM, incubation at 30°C for 10 min, complete inhibition
MnSO4
1 mM, incubation at 30°C for 10 min, complete inhibition
N-ethylmaleimide
1 mM, incubation at 30°C for 10 min, complete inhibition
NiCl2
1 mM, incubation at 30°C for 10 min, complete inhibition
p-chloromercuribenzoate
1 mM, incubation at 30°C for 10 min, complete inhibition
PbCl2
1 mM, incubation at 30°C for 10 min, complete inhibition
ZnCl2
1 mM, incubation at 30°C for 10 min, complete inhibition
ZnSO4
1 mM, incubation at 30°C for 10 min, complete inhibition
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0242
R-amidase from Pseudomonas sp. MCI3434
4.59
RamA from Escherichia coli JM109 harboring pRTB1EX
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
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calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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optimization of R-amidase production by a newly isolated strain of Delftia tsuruhatensis ZJB-05174. Effect of carbon sources, nitrogen sources, and inducers is analyzed. The maximal R-amidase production is achieved when glucose is tested as carbon source, yeast extract as nitrogen source and (R,S)-2,2-dimethylcyclopropane carboxamide as inducer
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29500
1 * 29500, SDS-PAGE
30128
1 * 30128, calculated from sequence
36000
gel filtration
49990
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x * 50000, SDS-PAGE, x * 49990, calculated
50000
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x * 50000, SDS-PAGE, x * 49990, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 50000, SDS-PAGE, x * 49990, calculated
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
30°C, 10 min, most stable in pH-range 6.0-9.0
664820
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
10 min, stable
40
10 min, stable
45
10 min, 13% loss of activity
50
10 min, 97% loss of activity
55
10 min, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for more than 2 months in the buffer containing 50% glycerol
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (968 entries)
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