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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.4.3.10 - putrescine oxidase and Organism(s) Kocuria rosea and UniProt Accession P40974

for references in articles please use BRENDA:EC1.4.3.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.10 putrescine oxidase
IUBMB Comments
A flavoprotein (FAD). 4-Aminobutanal condenses non-enzymically to 1-pyrroline.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Kocuria rosea
UNIPROT: P40974
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Kocuria rosea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
putrescine oxidase, putox, adenine dinucleotide-containing putrescine oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidase, putrescine
-
-
-
-
PO
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
putrescine + O2 + H2O = 4-aminobutanal + NH3 + H2O2
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative deamination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
putrescine:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD). 4-Aminobutanal condenses non-enzymically to 1-pyrroline.
CAS REGISTRY NUMBER
COMMENTARY hide
9076-87-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
1,6-diaminohexane + O2 + H2O
?
show the reaction diagram
-
1% of the activity with putrescine
-
-
?
cadaverine + O2 + H2O
5-aminopentanal + NH3 + H2O2
show the reaction diagram
histamine + O2 + H2O
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
show the reaction diagram
-
1.7% activity compared to putrescine
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
show the reaction diagram
spermidine + O2 + H2O
4-aminobutyraldehyde + 1,3-diaminopropane + H2O2
show the reaction diagram
tryptamine + O2 + H2O
1H-indol-3-yl-acetaldehyde + NH3 + H2O2
show the reaction diagram
-
5.2% activity compared to putrescine
-
-
?
tyramine + O2 + H2O
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
show the reaction diagram
-
2.0% activity compared to putrescine
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
putrescine + O2 + H2O
4-aminobutanal + NH3 + H2O2
show the reaction diagram
-
100% activity
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,1,4,4-tetramethyl-1,4-diaminobutane
-
-
1,10-Diaminodecane
-
-
1,12-diaminododecane
-
-
1,3-diaminopropane
-
-
1,6-diaminohexane
-
-
1,7-Diaminoheptane
-
-
1,8-diaminooctane
-
-
1-aminoethanol
-
-
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
the activity of the modified enzyme towards putrescine is 5.6% of that of the native enzyme. The modified enzyme shows activity towards monoamines such as n-butylamine, n-hexylamine and n-octylamine, which are not substrates of the native enzyme
2-Aminoethanol
-
-
3-Amino-1-propanol
-
-
4-amino-1-butanoic acid
-
-
5-amino-1-pentanoic acid
-
-
5-amino-1-pentanol
-
-
6-amino-1-hexanoic acid
-
-
6-amino-1-hexanol
-
-
8-amino-1-octanoic acid
-
-
agmatine
-
-
allylamine
-
-
ammonium
-
-
benzylamine
-
-
Butylamine
-
-
cadaverine
-
noncompetitive against putrescine
Cd2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Co2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
Cu2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
cyanide
-
-
dodecylamine
-
-
ethylamine
-
-
ethylenediamine
-
-
heptylamine
-
-
Hexylamine
-
-
Hg2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
hydroxylamine
-
-
Iproniazid
-
-
methylamine
-
-
N,N,N',N'-tetramethyl-1,4-diaminobutane
-
-
Ni2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
pentylamine
-
-
Phenylethylamine
-
-
Propylamine
-
-
spermidine
-
competitive inhibition of putrescine oxidation
spermine
-
competitive inhibition of putrescine oxidation
tyramine
-
-
Zn2+
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.038
putrescine
0.124
O2
-
-
0.038 - 0.23
putrescine
0.23
spermidine
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
1,1,4,4-tetramethyl-1,4-diaminobutane
-
-
0.003
1,10-Diaminodecane
-
-
0.002
1,12-diaminododecane
-
-
0.12
1,3-diaminopropane
-
-
0.023
1,6-diaminohexane
-
-
0.0082
1,7-Diaminoheptane
-
-
0.0032
1,8-diaminooctane
-
-
3
2-Aminoethanol
-
-
0.5 - 0.67
3-Amino-1-propanol
440
4-amino-1-butanoic acid
-
-
59
5-amino-1-pentanoic acid
-
-
0.088
5-amino-1-pentanol
-
-
300
6-amino-1-hexanoic acid
-
-
0.31
6-amino-1-hexanol
-
-
160
8-amino-1-octanoic acid
-
-
0.036
agmatine
-
-
0.013
allylamine
-
-
20
ammonium
-
-
0.047
benzylamine
-
-
0.46
Butylamine
-
-
0.28
cadaverine
-
-
0.0082
dodecylamine
-
-
2.3
ethylamine
-
-
0.95
ethylenediamine
-
-
0.014
heptylamine
-
-
0.039
Hexylamine
-
-
3.4
methylamine
-
-
0.14
N,N,N',N'-tetramethyl-1,4-diaminobutane
-
-
0.24
pentylamine
-
-
0.087
Phenylethylamine
-
-
0.62
Propylamine
-
-
0.181
spermidine
-
-
0.0581
spermine
-
-
0.039
tyramine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59.16
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
putrescine
8 - 8.6
-
-
8.5
-
spermidine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PUO_KOCRO
478
0
51914
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
-
2 * 46000, SDS-PAGE
50000
83400 - 87000
-
calculation from sedimentation data
90000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 50000, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
homodimer
-
2 * 50000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
stable up to
50
-
rapid inactivation at
additional information
-
the enzyme is resistant to heat denaturation as long as it is maintained in a fully reduced state
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
photoreduction of the enzyme in presence of EDTA
-
395438
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-22°C, stable for months
-
5°C, 0.01 M phosphate buffer, pH 6.0-8.0, little loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three-phase partitioning and DEAE Sephadex gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
diagnostics
-
enzyme can be used as biosensor for putrescine using dispersed multiwalled carbon nanotubes as ultra-microelectrodes ensuring a good electron transfer from the enzyme, method optimization, overview
food industry
-
the immobilized enzyme may be used as a sensor for analysis of beer samples
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okada, M.; Kawashima, S.; Imahori, K.
Purification of putrescine oxidase from Micrococcus rubens by affinity chromatography
Methods Enzymol.
94
301-303
1983
Kocuria rosea
Manually annotated by BRENDA team
Yamada, H.
Putrescine oxidase (Micrococcus rubens)
Methods Enzymol.
17B
726-730
1971
Kocuria rosea
-
Manually annotated by BRENDA team
Desa, R.J.
Putrescine oxidase from Micrococcus rubens. Purification and properties of the enzyme
J. Biol. Chem.
247
5527-5534
1972
Kocuria rosea
Manually annotated by BRENDA team
Ishizuka, H.; Horinouchi, S.; Beppu, T.
Putrescine oxidase of Micrococcus rubens: primary structure and Escherichia coli
J. Gen. Microbiol.
139
425-432
1993
Kocuria rosea
Manually annotated by BRENDA team
Isobe, K.; Tani, Y.; Yamada, H.
Differential determination procedure for putrescine, spermidine and spermine with polyamine oxidase from fungi and putrescine oxidase
Agric. Biol. Chem.
45
727-733
1981
Kocuria rosea
-
Manually annotated by BRENDA team
Swain, W.F.; Desa, R.J.
Mechanism of action of putrescine oxidase. Binding characteristics of the active site of putrescine oxidase from Micrococcus rubens
Biochim. Biophys. Acta
429
331-341
1976
Kocuria rosea
Manually annotated by BRENDA team
Okada, M.; Kawashima, S.; Imahori, K.
Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions
J. Biochem.
88
481-488
1980
Kocuria rosea
Manually annotated by BRENDA team
Adachi, O.; Yamada, H.; Ogata, K.
Purification and properties of putrescine oxidase of Micrococcus rubens
Agric. Biol. Chem.
30
1202-1210
1966
Kocuria rosea
-
Manually annotated by BRENDA team
Rochette, J.F.; Sacher, E.; Meunier, M.; Luong, J.H.
A mediatorless biosensor for putrescine using multiwalled carbon nanotubes
Anal. Biochem.
336
305-311
2005
Kocuria rosea
Manually annotated by BRENDA team
Boka, B.; Adanyi, N.; Szamos, J.; Virag, D.; Kiss, A.
Putrescine biosensor based on putrescine oxidase from Kocuria rosea
Enzyme Microb. Technol.
51
258-262
2012
Kocuria rosea, Kocuria rosea K22
Manually annotated by BRENDA team
Henao-Escobar, W.; Dominguez-Renedo, O.; Alonso-Lomillo, M.; Cascalheira, J.; Dias-Cabral, A.; Arcos-Martinez, M.
Characterization of a disposable electrochemical biosensor based on putrescine oxidase from Micrococcus rubens for the determination of putrescine
Electroanalysis
27
368-377
2015
Kocuria rosea (P40974)
-
Manually annotated by BRENDA team