Information on EC 3.5.1.30 - 5-aminopentanamidase

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The expected taxonomic range for this enzyme is: Pseudomonas putida

EC NUMBER
COMMENTARY hide
3.5.1.30
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RECOMMENDED NAME
GeneOntology No.
5-aminopentanamidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-aminopentanamide + H2O = 5-aminopentanoate + NH3
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amide bond
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-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine degradation IV
-
-
Lysine degradation
-
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lysine metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
5-aminopentanamide amidohydrolase
The enzyme from Pseudomonas putida also acts on 4-aminobutanamide and, more slowly, on 6-aminohexanamide.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-60-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P2-ATCC*25571
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-
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
4-aminobutyramide + H2O
4-aminobutanoate + NH3
show the reaction diagram
5-aminopentanamide + H2O
5-aminopentanoate + NH3
show the reaction diagram
5-aminopentanamide + H2O
?
show the reaction diagram
6-aminohexanamide + H2O
6-aminohexanoate + NH3
show the reaction diagram
methyl-delta-aminovalerate + H2O
5-aminopentanoate + methanol
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-aminopentanamide + H2O
5-aminopentanoate + NH3
show the reaction diagram
5-aminopentanamide + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
-
0.125 mM stimulates activity 37%
Fe3+
-
0.125 mM stimulates activity 25%
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AgNO3
-
0.00125 mM, 100% inhibition
arsenite
Ba2+
-
5 mM, inhibition from 10-40%
Ca2+
-
5 mM, inhibition from 10-40%
Cd(acetate)2
-
0.00125 mM, 94% inhibition
Cd2+
-
0.5 mM, complete inhibition , characteristic of enzymes with essential vicinal sulfhydryl groups
Co2+
-
5.0 mM,75% inhibition
Cu2+
-
5.0 mM, complete inhibition
Fe2+
-
5 mM, inhibition from 10-40%
Hg2+
-
0.5 mM, complete inhibition
HgCl2
HgNO3
-
0.187 mM, 100% inhibition
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Mg2+
-
5 mM, inhibition from 10-40%
NaAsO2
-
0.0125 mM, 47% inhibition
p-hydroxymercuribenzoate
Pb2+
-
5.0 mM, complete inhibition
Sn2+
-
5.0 mM, complete inhibition
Zn2+
-
0.5 mM, complete inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithioerythritol
-
effectively reverses heavy metal inactivation
L-lysine
-
induces enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
5-Aminopentanamide
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-
12
6-Aminohexanamide
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-
4.1
gamma-aminobutyramide
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-
6
methyl-delta-aminovalerate
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
stable below pH 6.5, irreversibly inactivated above pH 9
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67000
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gel filtration
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA and dithioerythritol required for optimum stability, enzyme stored in their absence rapidly deteriorates
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified 400fold from the soluble fraction of cell-free extract
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene davA, functional recombinant expression in Escherichia coli strains WL3110 and XQ56 from vector pKE112-MCS, co-expression with gene davB from Pseudomnas putida, encoding lysine 2-monooxygenase, as well as with gabTD genes encoding 5AVA aminotransferase and glutarate semialdehyde dehydrogenase, addition of L-lysine and 2-oxoglutarate results in synthesis of 5-aminovalerate and glutrate, overview