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
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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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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
strain MCI3434
SwissProt
Manually annotated by BRENDA team
strain MCI3434
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
-
-
amidase exhibits strict R-selectivity towards 2,2-dimethylcyclopropanecarboxamide
-
?
(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 30C for 10 min, complete inhibition
CdCl2
1 mM, incubation at 30C for 10 min, complete inhibition
CoCl2
1 mM, incubation at 30C for 10 min, complete inhibition
CuCl2
1 mM, incubation at 30C for 10 min, complete inhibition
CuSO4
1 mM, incubation at 30C for 10 min, complete inhibition
Fe(NH4)2(SO4)2
1 mM, incubation at 30C for 10 min, 67% inhibition
FeCl3
1 mM, incubation at 30C for 10 min, 78% inhibition
HgCl2
1 mM, incubation at 30C for 10 min, complete inhibition
MnCl2
1 mM, incubation at 30C for 10 min, complete inhibition
MnSO4
1 mM, incubation at 30C for 10 min, complete inhibition
N-ethylmaleimide
1 mM, incubation at 30C for 10 min, complete inhibition
NiCl2
1 mM, incubation at 30C for 10 min, complete inhibition
p-chloromercuribenzoate
1 mM, incubation at 30C for 10 min, complete inhibition
PbCl2
1 mM, incubation at 30C for 10 min, complete inhibition
ZnCl2
1 mM, incubation at 30C for 10 min, complete inhibition
ZnSO4
1 mM, incubation at 30C 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
-
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
?
-
x * 50000, SDS-PAGE, x * 49990, calculated
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
30C, 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
-20C, 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 (835 entries)
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