Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.1.101 - L-proline amide hydrolase and Organism(s) Pseudomonas azotoformans and UniProt Accession Q76KX0

for references in articles please use BRENDA:EC3.5.1.101
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas azotoformans
UNIPROT: Q76KX0 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Pseudomonas azotoformans
The enzyme appears in selected viruses and cellular organisms
Synonyms
l-amino acid amidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-amino acid amidase
-
S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase
-
SYSTEMATIC NAME
IUBMB Comments
(S)-piperidine-2-carboxamide amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
79633-25-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R,S)-piperazine-2-tert-butylcarboxamide + H2O
(S)-piperazine-2-tert-butylcarboxylic acid + NH3
show the reaction diagram
% of the activity with L-proline amide
-
-
?
(S)-piperazine-2-carboxamide + H2O
(S)-piperazine-2-carboxylic acid + NH3
show the reaction diagram
3.7% of the activity with L-proline amide
-
-
?
(S)-piperazine-2-tert-butylcarboxamide + H2O
(S)-piperazine-2-carboxylic acid + tert-butylamine
show the reaction diagram
0.2% of the activity with L-proline amide
-
-
?
(S)-piperidine-2-carboxamide + H2O
(S)-piperidine-2-carboxylic acid + NH3
show the reaction diagram
32% of the activity with L-proline amide
-
-
?
L-alanine amide + H2O
L-alanine + NH3
show the reaction diagram
10.6% of the activity with L-proline amide
-
-
?
L-isoleucine amide + H2O
L-isoleucine + NH3
show the reaction diagram
0.17% of the activity with L-proline amide
-
-
?
L-leucine amide + H2O
L-leucine + NH3
show the reaction diagram
0.46% of the activity with L-proline amide
-
-
?
L-methionine amide + H2O
L-methionine + NH3
show the reaction diagram
4.2% of the activity with L-proline amide
-
-
?
L-phenylalanine amide + H2O
L-phenylalanine + NH3
show the reaction diagram
0.97% of the activity with L-proline amide
-
-
?
L-proline amide + H2O
L-proline + NH3
show the reaction diagram
-
-
-
?
L-proline-p-nitroanilide + H2O
? + NH3
show the reaction diagram
40.9% of the activity with L-proline amide
-
-
?
L-serine amide + H2O
L-serine + NH3
show the reaction diagram
0.43% of the activity with L-proline amide
-
-
?
L-threonine amide + H2O
L-threonine + NH3
show the reaction diagram
0.12% of the activity with L-proline amide
-
-
?
L-tryptophan amide + H2O
L-tryptophan + NH3
show the reaction diagram
0.2% of the activity with L-proline amide
-
-
?
L-tyrosine amide + H2O
L-tyrosine + NH3
show the reaction diagram
0.086% 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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
1 mM, complete inhibition
Cd2+
1 mM, complete inhibition
CoCl2
1 mM, 52% inhibition
Hg2+
1 mM, complete inhibition
iodoacetate
1 mM, 40% inhibition
NEM
1 mM, 24% inhibition
NiCl2
1 mM, 70% inhibition
p-chloromercuribenzoate
1 mM, 67% inhibition
PbCl2
1 mM, 73% inhibition
phenylhydrazine
1 mM, complete inhibition
Zn2+
1 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.58
L-proline-p-nitroanilide
30°C, pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000894
S-stereoselective amidase from Pseudomonas azotoformans IAM 1603
192
LaaA from Escharichia coli JM109 harboring pSTB20
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
IAM 1603
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LAAA_PSEAZ
310
0
34514
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
gel filtration
34000
1 * 34000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 34000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stored without loss of activity for more than six 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
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
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)
Manually annotated by BRENDA team