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Enzyme Nomenclature
Information on EC 3.5.1.101 - L-proline amide hydrolase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.5.1.101
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RECOMMENDED NAME
GeneOntology No.
L-proline amide hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-piperidine-2-carboxamide + H2O = (S)-piperidine-2-carboxylate + NH3
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L-prolinamide + H2O = L-proline + NH3
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SYSTEMATIC NAME
IUBMB Comments
(S)-piperidine-2-carboxamide amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
79633-25-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R,S)-piperazine-2-tert-butylcarboxamide + H2O
(S)-piperazine-2-tert-butylcarboxylic acid + NH3
(S)-piperazine-2-tert-butylcarboxamide + H2O
(S)-piperazine-2-carboxylic acid + tert-butylamine
0.2% of the activity with L-proline amide
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?
(S)-piperidine-2-carboxamide + H2O
(S)-piperidine-2-carboxylic acid + NH3
32% of the activity with L-proline amide
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?
L-alanine amide + H2O
L-alanine + NH3
10.6% of the activity with L-proline amide
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?
L-isoleucine amide + H2O
L-isoleucine + NH3
0.17% of the activity with L-proline amide
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?
L-methionine amide + H2O
L-methionine + NH3
4.2% of the activity with L-proline amide
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?
L-proline-p-nitroanilide + H2O
? + NH3
40.9% of the activity with L-proline amide
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?
L-serine amide + H2O
L-serine + NH3
0.43% of the activity with L-proline amide
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-
?
L-threonine amide + H2O
L-threonine + NH3
0.12% of the activity with L-proline amide
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?
L-tryptophan amide + H2O
L-tryptophan + NH3
0.2% of the activity with L-proline amide
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?
L-tyrosine amide + H2O
L-tyrosine + NH3
0.086% of the activity with L-proline amide
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?
(R,S)-piperazine-2-tert-butylcarboxamide + H2O
(S)-piperazine-2-tert-butylcarboxylic acid + NH3
% of the activity with L-proline amide
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?
(R,S)-piperazine-2-tert-butylcarboxamide + H2O
(S)-piperazine-2-tert-butylcarboxylic acid + NH3
% of the activity with L-proline amide
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?
(S)-piperazine-2-carboxamide + H2O
(S)-piperazine-2-carboxylic acid + NH3
3.7% of the activity with L-proline amide
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?
(S)-piperazine-2-carboxamide + H2O
(S)-piperazine-2-carboxylic acid + NH3
3.7% of the activity with L-proline amide
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?
L-leucine amide + H2O
L-leucine + NH3
0.46% of the activity with L-proline amide
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?
L-leucine amide + H2O
L-leucine + NH3
0.46% of the activity with L-proline amide
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?
L-phenylalanine amide + H2O
L-phenylalanine + NH3
0.97% of the activity with L-proline amide
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?
L-phenylalanine amide + H2O
L-phenylalanine + NH3
0.97% of the activity with L-proline amide
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?
additional information
?
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the following compounds are not substrates for the amidase: L-arginine amide, L-asparagine amide, L-isoasparagine, L-glutaminamide, L-isoglutamine, glycine amide, L-histidine amide, L-lysine amide, L-valine amide, D-proline amide, L-alanyl-L-alanine, L-alanylglycine, glycylglycine, L-prolyl-L-alanine and L-prolylglycine. LaaA can not act on the peptide substrates such as L-prolyl-L-alanine, L-prolylglycine, L-alanyl-L-alanine, L-alanylglycine and glycylglycine
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additional information
?
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the following compounds are not substrates for the amidase: L-arginine amide, L-asparagine amide, L-isoasparagine, L-glutaminamide, L-isoglutamine, glycine amide, L-histidine amide, L-lysine amide, L-valine amide, D-proline amide, L-alanyl-L-alanine, L-alanylglycine, glycylglycine, L-prolyl-L-alanine and L-prolylglycine. LaaA can not act on the peptide substrates such as L-prolyl-L-alanine, L-prolylglycine, L-alanyl-L-alanine, L-alanylglycine and glycylglycine
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000894
S-stereoselective amidase from Pseudomonas azotoformans IAM 1603
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stored without loss of activity for more than six months in the buffer containing 50% glycerol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
Escherichia coli cells overexpressing the laaA gene have been demonstrated to be applicable to the S-stereoselective hydrolysis of (R,S)-piperazine-2-tert-butylcarboxamide to produce (S)-piperazine-2-carboxylic acid with high optical purity. Enantiomerically pure piperazine-2-carboxylic acid and its tert-butylcarboxamide derivative are important chiral building blocks for some pharmacologically active compounds such as N-methyl-D-aspartate antagonist for glutamate receptor, cardioprotective nucleoside transport blocker and HIV protease inhibitor
synthesis
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Escherichia coli cells overexpressing the laaA gene have been demonstrated to be applicable to the S-stereoselective hydrolysis of (R,S)-piperazine-2-tert-butylcarboxamide to produce (S)-piperazine-2-carboxylic acid with high optical purity. Enantiomerically pure piperazine-2-carboxylic acid and its tert-butylcarboxamide derivative are important chiral building blocks for some pharmacologically active compounds such as N-methyl-D-aspartate antagonist for glutamate receptor, cardioprotective nucleoside transport blocker and HIV protease inhibitor
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LINKS TO OTHER DATABASES (specific for EC-Number 3.5.1.101)
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