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Information on EC 1.4.3.22 - diamine oxidase and Organism(s) Sus scrofa and UniProt Accession Q9TRC7

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EC Tree
     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.22 diamine oxidase
IUBMB Comments
A group of enzymes that oxidize diamines, such as histamine, and also some primary monoamines but have little or no activity towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, like EC 1.4.3.21 (primary-amine oxidase) but unlike EC 1.4.3.4 (monoamine oxidase), they are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide.
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This record set is specific for:
Sus scrofa
UNIPROT: Q9TRC7
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Word Map
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
diamine oxidase, amine oxidase, histaminase, histamine dehydrogenase, histamine oxidase, amiloride-binding protein, dao-1, n-methylputrescine oxidase, rhdao, methylputrescine oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Amine oxidase
-
-
DAO
-
-
PKAO
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
mechanism
-
SYSTEMATIC NAME
IUBMB Comments
histamine:oxygen oxidoreductase (deaminating)
A group of enzymes that oxidize diamines, such as histamine, and also some primary monoamines but have little or no activity towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, like EC 1.4.3.21 (primary-amine oxidase) but unlike EC 1.4.3.4 (monoamine oxidase), they are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-aminomethylpyridine dihydrochloride + H2O + O2
?
show the reaction diagram
8% substrate activity of 1 mM 4-aminomethylpyridine dihydrochloride as percentage of the activity of the best substrate (putrescine, 1 mM) for various amine oxidases
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
putrescine + H2O + O2
?
show the reaction diagram
-
-
-
?
1,3-diaminopropane + H2O + O2
3-aminopropanal + NH3 + H2O2
show the reaction diagram
-
30% activity compared to activity with putrescine
-
-
?
1,4-diaminobutane + H2O + O2
4-aminobutanal + NH3 + H2O2
show the reaction diagram
1,5-diaminopentane + H2O + O2
5-aminopentanal + NH3 + H2O2
show the reaction diagram
2-hydroxycadaverine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
2-hydroxyputrescine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
3-hydroxycadaverine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
butylamine + H2O + O2
butanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
r
cadaverine + H2O + O2
5-aminopentanal + NH3 + H2O2
show the reaction diagram
cadaverine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
r
ethylenediamine + H2O + O2
?
show the reaction diagram
-
-
-
-
r
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
L-lysine methyl ester + H2O + O2
?
show the reaction diagram
-
-
-
-
?
N-methyl-1,3-diaminopropane + H2O + O2
N-methyl-3-aminopropanal + NH3 + H2O2
show the reaction diagram
-
40% activity compared to activity with putrescine
-
-
?
N-methylputrescine + H2O + O2
4-(methylamino)butanal + NH3 + H2O2
show the reaction diagram
-
75% activity compared to activity with putrescine
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
propylamine + H2O + O2
propanal + NH3 + H2O2
show the reaction diagram
-
-
-
-
r
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
additional information
?
-
-
low activity with n-butylamine or 1,6-diaminohexane as substrate
-
-
?
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
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
-
enzyme plays a protective role against histamine in diseases such as ischaemic bowel syndrome, mesenteric infarction and ulcerative colitis
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
enzyme may contain pyridoxal phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
-
1-[3,5-bis(ethylsulfanyl)pyridin-4-yl]methanamine dihydrochloride
-
1-[3,5-bis(tert-butylsulfanyl)pyridin-4-yl]methanamine dihydrochloride
-
1-[3-(benzyloxy)-5-ethoxypyridin-4-yl]methanamine dihydrochloride
-
2-ethylaminobenzylamine dihydrochloride
-
2-methylaminobenzylamine dihydrochloride
-
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
-
3-(1-piperidinyl)-4-aminomethylpyridine dihydrochloride hemihydrate
-
3-amino-4-aminomethylpyridine dihydrochloride
-
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
-
3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate
-
3-ethylamino-4-aminomethylpyridine dihydrochloride
-
3-methylamino-4-aminomethylpyridine dihydrochloride
-
3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride
-
4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
-
4-(aminomethyl)-N,N'-bis(1-methylethyl)pyridine-3,5-diamine dihydrochloride
-
4-(aminomethyl)-N,N'-dibutylpyridine-3,5-diamine dihydrochloride
-
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
-
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
-
4-(aminomethyl)-N-methylpyridine-3,5-diamine dihydrochloride
-
histamine
substrate inhibition at 0.5 mM
1,3-diaminopropane
-
10 mM with 2 mM N-methylputrescine as substrate, 93% relative inhibition
1,4-Diamino-2-butanone
-
potent reversible inhibitors
1,4-diamino-2-butyne
-
-
1,5-Diamino-3-pentanone
-
potent reversible inhibitors
adenosine 3',5'-AMP
-
-
amiloride
-
diuretic drug, competitive vs. agmatine and putrescine oxidation
aminoguanidine
clonidine
-
antihypertensive drug, competitive vs. agmatine and putrescine oxidation
cyanide
-
-
diaminoacetone
-
0.1 mM, significant inhibition
gabexate mesylate
-
anti coagulant drug, competitive vs. agmatine and putrescine oxidation
H2O2
-
uncompetitive vs. p-dimethylaminomethylbenzylamine
Isonicotinic acid hydrazide
-
-
KCN
-
-
m-phenylenediamine
-
competitive vs. cadaverine
n-butylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 60% relative inhibition
N-methyl-1,3-diamonopropane
-
10 mM with 2 mM N-methylputrescine as substrate, 61% relative inhibition
N-methylbutylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 19% relative inhibition
N-methylpropylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 22% relative inhibition
n-Propylamine
-
10 mM with 2 mM N-methylputrescine as substrate, 48% relative inhibition
N3-
-
-
NaN3
-
uncompetitive vs. p-dimethylaminomethylbenzylamine, N3- is equatorially coordinated to a tetragonal Cu(II) center
NH3
-
competitive vs. p-dimethylaminomethylbenzylamine, uncompetitive vs. O2
o-phenyldiamine
-
-
o-phenylenediamine
-
competitive vs. cadaverine
phenylhydrazine
-
-
SCN-
-
-
Semicarbazide
-
-
thiocyanate
-
uncompetitive vs. p-dimethylaminomethylbenzylamine, SCN- is equatorially coordinated to a tetragonal Cu(II) center
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
4-aminomethylpyridine dihydrochloride
-
0.557
benzylamine
-
0.31
1,4-diaminobutane
-
pH 7.9, 30°C, higher KM-value compared with N-methylputrescine or cadaverine as substrates, Vmax: 21.9 pkat
0.12 - 0.25
benzaldehyde
3 - 5
Butylamine
0.1 - 8.1
cadaverine
66
ethylamine
-
at pH 7.4
66
ethylenediamine
-
at pH 7.4
0.013 - 1.8
histamine
6.5
lysine methylester
-
at pH 7.4
0.82
N-methylputrescine
-
pH 7.9, 30°C, lowest KM-value compared with putrescine or cadaverine as substrates, Vmax: 23.3 pkat
6.6
Propylamine
-
at pH 7.4
0.87 - 1.8
putrescine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046 - 0.23
benzaldehyde
0.9 - 4.5
cadaverine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0001
1,4-Diamino-2-butanone
-
-
0.0018
1,5-Diamino-3-pentanone
-
-
0.01
adenosine 3',5'-AMP
-
-
0.9
clonidine
-
-
0.027
gabexate mesylate
-
-
0.3 - 0.5
H2O2
10
m-phenyldiamine
-
-
2
N3-
-
-
33.8 - 36
NH3
10
o-phenyldiamine
-
-
22.4
SCN-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
1-[3,5-bis(ethylsulfanyl)pyridin-4-yl]methanamine dihydrochloride
Sus scrofa
-
0.00003
3-amino-4-aminomethylpyridine dihydrochloride
Sus scrofa
-
0.018
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
Sus scrofa
-
0.016
3-cyclohexylamino-4-aminomethylpyridine dihydrochloride monohydrate
Sus scrofa
-
0.05
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
Sus scrofa
-
0.019
3-cyclopentylamino-4-aminomethylpyridine dihydrochloride hemihydrate
Sus scrofa
-
0.05
3-cyclopropylamino-4-aminomethylpyridine dihydrochloride sesquihydrate
Sus scrofa
-
0.00005
3-ethylamino-4-aminomethylpyridine dihydrochloride
Sus scrofa
-
0.000016
3-methylamino-4-aminomethylpyridine dihydrochloride
Sus scrofa
-
0.016
3-[(1-methylethyl)amino]-4-aminomethylpyridine dihydrochloride
Sus scrofa
-
0.001
4-(aminomethyl)-N,N'-bis(1-methylethyl)pyridine-3,5-diamine dihydrochloride
Sus scrofa
-
0.01
4-(aminomethyl)-N,N'-dibutylpyridine-3,5-diamine dihydrochloride
Sus scrofa
-
0.0025
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
Sus scrofa
-
0.000061
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
Sus scrofa
-
0.00012
4-(aminomethyl)-N-methylpyridine-3,5-diamine dihydrochloride
Sus scrofa
-
0.21
KCN
Sus scrofa
-
-
additional information
additional information
Sus scrofa
above 1.0 mM for 1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride, 3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride, 4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride, 1-[3-(benzyloxy)-5-ethoxypyridin-4-yl]methanamine dihydrochloride, 1-[3,5-bis(tert-butylsulfanyl)pyridin-4-yl]methanamine dihydrochloride and above 0.1 mM for 3-(1-piperidinyl)-4-aminomethylpyridine dihydrochloride hemihydrate, 2-methylaminobenzylamine dihydrochloride, and 2-ethylaminobenzylamine dihydrochloride
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.046
-
oxidation of histamine, H2S treated enzyme
0.054
-
oxidation of tyramine, H2S treated enzyme
0.058
-
oxidation of serotonine creatine sulfate, H2S treated enzyme
0.11
-
oxidation of tryptamine, H2S treated enzyme
0.13
-
oxidation of putrescine, H2S treated enzyme
0.21
-
oxidation of cadeverine, H2S treated enzyme
0.216
-
oxidation of N-methyl-beta-phenylethylamine, H2S treated enzyme
0.31
-
oxidation of histamine
0.38
-
oxidation of putrescine
0.51
-
oxidation of cadeverine
1.27
-
-
1.44
-
-
1.6
-
-
3.2
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in histamine metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AOC1_PIG
755
0
85475
Swiss-Prot
Secretory Pathway (Reliability: 2)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme shows weak stability under simulated intestinal conditions with a half-life period of around 19 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 100 mM sodium-potassium phosphate, pH 7.4, stable for at least one year
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on AH-Sepharose
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
improved food supplements must be developed to help histamine intolerant humans. At least 50 nkat free porcine diamine oxidase are required to convert 75 mg histamine to (imidazol-4-yl)acetaldehyde in an in vitro test system. This results in a reduction of histamine by 90%. The enzyme showes weak stability under simulated intestinal conditions with a half-life period of around 19 min. Therefore, a lot more exogenous diamine oxidase would be required for efficient histamine degradation in the human intestine
biotechnology
-
supramolecular tandem assays exploit the dynamic binding of a fluorescent dye with a macrocyclic host in competition with the binding of the substrate and product. Two examples of enzymatic reactions were investigated: the hydrolysis of arginine to ornithine catalyzed by arginase and the oxidation of cadaverine to 5-aminopentanal by diamine oxidase, in which the substrates have a higher affinity to the macrocycle than the products (substrate-selective assays). The depletion of the substrate allows the fluorescent dye to enter the macrocycle in the course of the enzymatic reaction, which leads to the desired fluorescence response. For arginase, p-sulfonatocalix[4]arene is used as the macrocycle, and for diamine oxidase, cucurbit[7]uril (CB7) is used. An additional reporter pair, namely cucurbit[7]uril (CB7)/acridine orange (AO) is applied and the potential of tandem assays for inhibitor screening is demonstrated
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mondovi, B.; Costa, M.T.; Agro, A.F.; Rotilio, G.
Pyridoxal phosphate as a prosthetic group of pig kidney diamine oxidase
Arch. Biochem. Biophys.
119
373-381
1967
Sus scrofa
Manually annotated by BRENDA team
Floris, G.; Fadda, M.B.; Pellegrini, M.; Corda, M.; Agro, A.F.
Purification of pig kidney diamine oxidase by gel-exclusion chromatography
FEBS Lett.
72
179-181
1976
Sus scrofa
Manually annotated by BRENDA team
Bardsley, W.G.; Crabbe, M.J.C.; Shindler, J.S.
Kinetics of the diamine oxidase reaction
Biochem. J.
131
459-469
1973
Sus scrofa
Manually annotated by BRENDA team
Costa, M.T.; Rotilio, G.; Agro, A.F.; Vallogini, M.P.; Mondovi, B.
On the active site of diamine oxidase: kinetic studies
Arch. Biochem. Biophys.
147
8-13
1971
Sus scrofa
Manually annotated by BRENDA team
Stesina, L.N.; Akopyan, Z.I.; Gorkin, V.Z.
Modification of catalytic properties of amine oxidases
FEBS Lett.
16
349-351
1971
Sus scrofa
Manually annotated by BRENDA team
Stevanato, R.; Porchia, M.; Befani, O.; Mondovi, B.; Rigo, A.
Characterization of free and immobilized amine oxidases
Biotechnol. Appl. Biochem.
11
266-272
1989
Bos taurus, Sus scrofa
Manually annotated by BRENDA team
Bieganski, T.; Kusche, J.; Lorenz, W.; Hesterberg, R.; Stahlknecht, C.D.; Feussner, K.D.
Distribution and properties of human intestinal diamine oxidase and its relevance for the histamine catabolism
Biochim. Biophys. Acta
756
196-203
1983
Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Tamura, H.; Horiike, K.; Fukuda, H.; Watanabe, T.
Kinetic studies on the inhibition mechanism of diamine oxidase from porcine kidney by aminoguanidine
J. Biochem.
105
299-306
1989
Sus scrofa
Manually annotated by BRENDA team
Dooley, D.M.; Golnik, K.C.
Spectroscopic and kinetics studies of the inhibition of pig kidney diamine oxidase by anions
J. Biol. Chem.
258
4245-4248
1983
Sus scrofa
Manually annotated by BRENDA team
Federico, R.; Angelini, R.; Ercolini, L.; Venturini, G.; Mattevi, A.; Ascenzi, P.
Competitive inhibition of swine kidney copper amine oxidase by drugs: amiloride, clonidine, and gabexate mesylate
Biochem. Biophys. Res. Commun.
240
150-152
1997
Sus scrofa
Manually annotated by BRENDA team
Bertini, V.; Buffoni, F.; Ignesti, G.; Picci, N.; Trombino, S.; Iemma, F.; Alfei, S.; Pocci, M.; Lucchesini, F.; De Munno, A.
Alkylamino derivatives of 4-aminomethylpyridine as inhibitors of copper-containing amine oxidases
J. Med. Chem.
48
664-670
2005
Sus scrofa (Q9TRC7)
Manually annotated by BRENDA team
Mura, A.; Anedda, R.; Pintus, F.; Casu, M.; Padiglia, A.; Floris, G.; Medda, R.
An important lysine residue in copper/quinone-containing amine oxidases
FEBS J.
274
2585-2595
2007
Bos taurus, Euphorbia characias, Lens culinaris, Pisum sativum, Sus scrofa
Manually annotated by BRENDA team
Sebela, M.; Tylichova, M.; Pec, P.
Inhibition of diamine oxidases and polyamine oxidases by diamine-based compounds
J. Neural Transm.
114
793-798
2007
Pisum sativum, Sus scrofa
Manually annotated by BRENDA team
Nau, W.M.; Ghale, G.; Hennig, A.; Bakirci, H.; Bailey, D.M.
Substrate-selective supramolecular tandem assays: monitoring enzyme inhibition of arginase and diamine oxidase by fluorescent dye displacement from calixarene and cucurbituril macrocycles
J. Am. Chem. Soc.
131
11558-11570
2009
Sus scrofa
Manually annotated by BRENDA team
Hashimoto, T.; Mitani, A.; Yamada, Y.
Diamine oxidase from cultured roots of Hyoscyamus niger: its function in tropane alkaloid biosynthesis
Plant Physiol.
93
216-221
1990
Hyoscyamus niger, Pisum sativum, Sus scrofa
Manually annotated by BRENDA team
Gludovacz, E.; Maresch, D.; Lopes de Carvalho, L.; Puxbaum, V.; Baier, L.J.; Suetzl, L.; Guedez, G.; Gruenwald-Gruber, C.; Ulm, B.; Pils, S.; Ristl, R.; Altmann, F.; Jilma, B.; Salminen, T.A.; Borth, N.; Boehm, T.
Oligomannosidic glycans at Asn-110 are essential for secretion of human diamine oxidase
J. Biol. Chem.
293
1070-1087
2018
Homo sapiens (P19801), Homo sapiens, Sus scrofa (Q9TRC7)
Manually annotated by BRENDA team
Kettner, L.; Seitl, I.; Fischer, L.
Evaluation of porcine diamine oxidase for the conversion of histamine in food-relevant amounts
J. Food Sci.
85
843-852
2020
Sus scrofa (Q9TRC7), Sus scrofa
Manually annotated by BRENDA team