HOME
login
history
all enzymes
BRENDA home
History
Information on EC 3.5.1.101 - L-proline amide hydrolase
for references in articles please use BRENDA:EC3.5.1.101Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.5.1.101 L-proline amide hydrolaseSpecify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
Synonyms
l-amino acid amidase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-amino acid amidase
LaaA
S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase
S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase
-
S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-piperidine-2-carboxamide + H2O = (S)-piperidine-2-carboxylate + NH3
-
-
-
-
L-prolinamide + H2O = L-proline + NH3
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(S)-piperidine-2-carboxamide amidohydrolase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
79633-25-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
(S)-piperidine-2-carboxamide + H2O
(S)-piperidine-2-carboxylic acid + NH3
32% of the activity with L-proline amide
-
-
?
L-alanine amide + H2O
L-alanine + NH3
10.6% of the activity with L-proline amide
-
-
?
L-isoleucine amide + H2O
L-isoleucine + NH3
0.17% of the activity with L-proline amide
-
-
?
L-methionine amide + H2O
L-methionine + NH3
4.2% of the activity with L-proline amide
-
-
?
L-proline-p-nitroanilide + H2O
? + NH3
40.9% of the activity with L-proline amide
-
-
?
L-serine amide + H2O
L-serine + NH3
0.43% of the activity with L-proline amide
-
-
?
L-threonine amide + H2O
L-threonine + NH3
0.12% of the activity with L-proline amide
-
-
?
L-tryptophan amide + H2O
L-tryptophan + NH3
0.2% of the activity with L-proline amide
-
-
?
L-tyrosine amide + H2O
L-tyrosine + NH3
0.086% of the activity with L-proline amide
-
-
?
(R,S)-piperazine-2-tert-butylcarboxamide + H2O
(S)-piperazine-2-tert-butylcarboxylic acid + NH3
% of the activity with L-proline amide
-
-
?
(R,S)-piperazine-2-tert-butylcarboxamide + H2O
(S)-piperazine-2-tert-butylcarboxylic acid + NH3
% of the activity with L-proline amide
-
-
?
(S)-piperazine-2-carboxamide + H2O
(S)-piperazine-2-carboxylic acid + NH3
3.7% of the activity with L-proline amide
-
-
?
(S)-piperazine-2-carboxamide + H2O
(S)-piperazine-2-carboxylic acid + NH3
3.7% of the activity with L-proline amide
-
-
?
L-leucine amide + H2O
L-leucine + NH3
0.46% of the activity with L-proline amide
-
-
?
L-leucine amide + H2O
L-leucine + NH3
0.46% of the activity with L-proline amide
-
-
?
L-phenylalanine amide + H2O
L-phenylalanine + NH3
0.97% of the activity with L-proline amide
-
-
?
L-phenylalanine amide + H2O
L-phenylalanine + NH3
0.97% of the activity with L-proline amide
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000894
S-stereoselective amidase from Pseudomonas azotoformans IAM 1603
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
LAAA_PSEFS
Pseudomonas fluorescens (strain SBW25)
310
0
34481
Swiss-Prot
A0A0P9MN23_PSESX
307
0
34315
TrEMBL
H8FM75_XANCI
313
0
34556
TrEMBL
A0A2K4WJI9_9PSED
313
0
34958
TrEMBL
A0A0U1FAH6_SALTM
297
0
33012
TrEMBL
A0A379XQR7_SALER
297
0
33157
TrEMBL
A0A085AGE1_9ENTR
297
0
33049
TrEMBL
A0A0T9WCU3_SALET
303
0
33842
TrEMBL
A0A0B4XDZ6_9RHIZ
304
0
34470
TrEMBL
A0A2C9ETL7_PSEPH
Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CHA0)
296
0
32976
TrEMBL
A0A0J6W8Y6_9MYCO
310
0
33857
TrEMBL
A0A2H1T5T9_XANCH
313
0
34557
TrEMBL
A0A0A6WC33_XANCH
313
0
34530
TrEMBL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stored without loss of activity for more than six months in the buffer containing 50% glycerol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Komeda, H.; Harada, H.; Washika, S.; Sakamoto, T.; Ueda, M.; Asano, Y.
S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase from Pseudomonas azotoformans IAM 1603 is a novel L-amino acid amidase
Eur. J. Biochem.
271
1465-1475
2004
Pseudomonas azotoformans (Q76KX0), Pseudomonas azotoformans IAM 1603 (Q76KX0)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.5.1.101)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
