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Information on EC 1.4.3.22 - diamine oxidase and Organism(s) Homo sapiens

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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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The taxonomic range for the selected organisms is: Homo sapiens
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
ABP1
-
-
Amiloride-binding protein
-
-
Diamine oxidase
histaminase
-
-
rhDAO
-
-
additional information
the enzyme is a member of the copper-containing amine oxidase, CAO, family of enzymes
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
(8-arginine)-vasopressin + H2O + O2
?
show the reaction diagram
-
-
-
-
?
(8-lysine)-vasopressin + H2O + O2
?
show the reaction diagram
-
-
-
-
?
1,10-diaminodecane + H2O + O2
10-aminodecanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
1,2-diaminoethane + H2O + O2
2-aminoethanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
1,3-diaminopropane + H2O + O2
3-aminopropanal + NH3 + H2O2
show the reaction diagram
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
1,6-diaminohexane + H2O + O2
6-aminohexanal + NH3 + H2O2
show the reaction diagram
1,7-diaminoheptane + H2O + O2
7-aminoheptanal + NH3 + H2O2
show the reaction diagram
1,8-diaminooctane + H2O + O2
8-aminooctanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
1,9-diaminononane + H2O + O2
9-aminononanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
1-methylhistamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
2-methylhistamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
5-methylhistamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
agmatine
?
show the reaction diagram
-
14% of activity with putrescine
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
show the reaction diagram
butylamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
cadaverine + H2O + O2
5-aminopentanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
cadaverine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
collagen + H2O + O2
?
show the reaction diagram
-
-
-
-
?
ethylenediamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
histamine + H2O + O2
?
show the reaction diagram
-
48% activity compared to putrescine
-
-
?
L-lysine methyl ester + H2O + O2
?
show the reaction diagram
-
-
-
-
?
methylhistamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
N(pi)-methylhistamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
N(tau)-methylhistamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
N-acetyl-1,4-diaminobutane + H2O + O2
N-acetyl-aminobutanal + acetylamine + H2O2
show the reaction diagram
-
8.6% of activity with putrescine
-
?
N-acetyl-1,5-diaminopentane + H2O + O2
N-acetyl-aminopentanal + acetylamine + H2O2
show the reaction diagram
-
3.8% of activity with putrescine
-
?
N-acetylcadaverine + H2O + O2
?
show the reaction diagram
-
-
-
-
r
N1-acetyl-spermidine + H2O + O2
?
show the reaction diagram
-
8.6% of activity with putrescine
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
?
show the reaction diagram
-
-
-
-
?
p-dimethylaminomethylbenzylamine + H2O + O2
p-dimethylaminomethylbenzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
?
putrescine + H2O + O2
4-aminobutanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
putrescine + H2O + O2
?
show the reaction diagram
putrescine + H2O + O2
gamma-aminobutyraldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
RCH2NH2 + H2O + O2
RCHO + NH3 + H2O2
show the reaction diagram
spermidine + H2O + O2
?
show the reaction diagram
spermine + H2O + O2
?
show the reaction diagram
tropocollagen + H2O + O2
?
show the reaction diagram
-
-
-
-
?
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
cadaverine + H2O + O2
5-aminopentanal + NH3 + H2O2
show the reaction diagram
-
-
-
?
histamine + H2O + O2
(imidazol-4-yl)acetaldehyde + NH3 + H2O2
show the reaction diagram
putrescine + H2O + O2
4-aminobutanal + 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
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,5-trihydroxyphenylalanine quinone
2,4,5-trihydroxyphenylalaninequinone
-
1.1 mol per mol of dimer
L-topaquinone
-
-
topaquinone
-
trihydroxyphenylalanine quinone
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
Manganese
-
enzyme contains 1.2 gatom of manganese per 70000 Da subunit
Zn2+
the metal site is occupied approximately 25% by zinc
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
-
i.e. LJP 1586. Potent, specific, and orally available inhibitor of SSAO activity is an effective anti-inflammatory compound in vivo
4,4'-(pentane-1,5-diylbis(oxy))dibenzimidamide
noncompetitive inhibition
8-hydroxyquinoline
-
1 mM, 49.3% inhibition
aminoguanidine
azide
-
partially competitive with respect to oxidative half-reaction, competitive with respect to reductive half-reaction
Berenil
mixed inhibition
cimetidine
mixed inhibition
clonidine
mixed inhibition
Cuprizone
-
-
cyanide
-
1 mM, 76% inhibition
diethyldithiocarbamate
-
1 mM, complete inhibition
diminazene aceturate
-
-
Iproniazid
-
0.1 mM, 68% inhibition
isoniazid
noncompetitive inhibition
NaCl
-
200 mM, approx. 50% inhibition, almost complete inhibition of the purified enzyme with 1 M NaCl
NaN3
-
-
Pentamidine
mixed inhibition
Quinacrine
-
1 mM, complete inhibition
Semicarbazide
tranylcypromine
-
slight
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13
1,3-diaminopropane
-
pH 7.2, 37°C
0.15
1,6-diaminohexane
-
pH 7.2, 37°C
0.0034
1-Methylhistamine
-
pH 7.2, 37°C
9.71
acetylputrescine
-
-
0.877 - 2.032
Butylamine
0.0279 - 0.03
cadaverine
0.63
ethylenediamine
-
pH 7.2, 37°C
0.0028 - 0.124
histamine
2.8
L-Lysine methyl ester
-
pH 7.2, 37°C
0.075 - 0.158
Methylhistamine
0.097
N(tau)-methylhistamine
-
-
3.28
N-acetylcadaverine
-
-
-
0.625
N1-acetylspermidine
-
-
0.014
O2
-
30°C, pH 7.2
0.11
p-dimethylaminomethylbenzylamine
-
pH 7.2, 37°C
0.02 - 0.094
putrescine
0.033 - 9.52
spermidine
0.031 - 5.71
spermine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29220
1,3-diaminopropane
-
pH 7.2, 37°C
17580
1,6-diaminohexane
-
pH 7.2, 37°C
6180
1-Methylhistamine
-
pH 7.2, 37°C
27180
cadaverine
-
pH 7.2, 37°C
7560
ethylenediamine
-
pH 7.2, 37°C
8340
histamine
-
pH 7.2, 37°C
20700
L-Lysine methyl ester
-
pH 7.2, 37°C
4
O2
-
30°C, pH 7.2, per dimer
32880
p-dimethylaminomethylbenzylamine
-
pH 7.2, 37°C
5.5 - 28500
putrescine
11220
spermidine
-
pH 7.2, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011
4,4'-(pentane-1,5-diylbis(oxy))dibenzimidamide
-
37 - 92
azide
0.013
Berenil
-
0.09
cimetidine
-
0.1
clonidine
-
0.9
isoniazid
-
0.29
Pentamidine
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.096
(Z)-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride
Homo sapiens
-
-
0.000153
aminoguanidine
Homo sapiens
in 100 mM potassium phosphate buffer (pH 7.2), at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
-
-
0.141
-
unpurified enzyme, at 37°C, pH not specified in the publication
0.22
-
enzyme from seminal plasma
0.73
-
-
32.7
-
after 233fold purification, at 37°C, pH not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 11
-
acetylputrescine
6 - 6.5
-
histane
6.4 - 6.6
-
histamine
6.5
-
putrescine and cadaverine
6.6 - 7
-
putrescine
7.2
assay at
8
-
N1-acetylspermidine
8.5
-
acetylcadaverine
9.5
-
spermidine and spermine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 7.8
-
pH 6.2 and pH 7.8: about 75% activity, putrescine
6.2 - 8.2
-
pH 6.2: about 75% of maximal activity, pH 8.2: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
ascending, descending and transverse
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
mainly in cytoplasm but to a considerable extent also in mitochondrial fraction
Manually annotated by BRENDA team
-
mainly in cytoplasm but to a considerable extent also in mitochondrial fraction
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
high evolutionary conservation of all four glycosylation sites
malfunction
-
the serum diamine oxidase is responsible for the symptoms of histamine intolerance
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AOC1_HUMAN
751
0
85378
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
102000
-
2 * 102000, SDS-PAGE
105000
-
2 * 105000, SDS-PAGE
200000
-
gel filtration
235000
-
sedimentation equilibrium
80000
-
gel filtration, variable PAGE, ultracentrifugation
90000
-
2 * 90000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
monomer
-
1 * 70000-80000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with aminoguanidine, hanging drop vapor diffusion method, using 0.1M bis-Tris propane (pH 7.5), 20% (w/v) PEG3350, and 0.2 M sodium sulfate at 20°C
purified recombinant wild-type hDAO, hanging drop vapour diffusion, 200 nl protein solution, containing 10 mg/ml protein in 100 mM HEPES, pH 7.2, and 150 mM KCl, and 200 nl crystallant solution, containing 0.1 M MES, pH 6.5, and 12% w/v PEG 20000, are equilibrated over 0.075 ml reservoir solution at room temperature, eight weeks, method optimization using manually dispensed hanging-drop crystallization experiments containing 0.002 ml each of protein and crystallant equilibrated over 0.5 ml reservoir solution, best diffracting crystals grow using 0.1 M MES pH 6.1 and 12% w/v PEG at room temperature over a period of two months, X-ray diffraction structure determination and analysis at 2.1 A resolution
the structure of the native enzyme is determined by X-ray crystallography to a resolution of 1.8 A. The homodimeric structure has the archetypal amine oxidase fold. Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed. Substrate binding pocket and entry channel of hDAO are distinctly different from other amine oxidases in accord with the different substrate specificities. The structures of two inhibitor complexes of hDAO, berenil and pentamidine, are refined to resolutions of 2.1 and 2.2 A, respectively. They bind noncovalently in the active-site channel. The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N168Q/N538Q/N745Q
the secretion of the recombinant enzyme is reduced by 94%
N538Q/N745Q
the secretion of the recombinant enzyme is reduced by 85%
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in dilute solution or in frozen state
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 24 h, 90% loss of activity
-
500 mM ammonium sulfate, 500 mM potassium phosphate, pH 7.4, stable for at least 3 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on AH-Sepharose
-
affinity chromatography on cadaverine-Sepharose
-
heparin-Sepharose column chromatography, phenyl-Sepharose column chromatography, CIM-QA column chromatography, and Superdex 200 gel filtration
-
recombinant enzyme
-
recombinant secreted hDAO from Drosophila S2 cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Drosophila S2 cells
expressed in CHO-K1 cells
-
expressed in Drosophila melanogaster Schneider-2 cells
expressed in two different HEK293 cell lines
gene AOC1, expression of hDAO as a secreted enzyme in Drosophila S2 cells
overexpressed as a secreted enzyme under the control of a metallothionein promoter in Drosophila S2 cell culture
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
-
the balance between histamine and DAO seems to be crucial for an uncomplicated course of pregnancy. Reduced DAO activities are found in multiple heterogeneous complications of pregnancy such as diabetes, threatened and missed abortion and trophoblastic disorders. Low activities of the histamine-degrading enzyme DAO might indicate high-risk pregnancies, although high intra- and interindividual variations limit its value as a screening tool
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Crabbe, M.J.; Kavanagh, J.P.
The purification and preliminary investigation of fumarase, peroxidase, diamine oxidase and adenosine deaminase from human seminal plasma
Biochem. Soc. Trans.
5
735-737
1977
Homo sapiens
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
Baylin, S.B.; Margolis, S.
Purification of histaminase (diamine oxidase) from human pregnancy plasma by affinity chromatography
Biochim. Biophys. Acta
397
294-306
1975
Homo sapiens
Manually annotated by BRENDA team
Crabbe, M.J.C.; Waight, R.D.; Bardsley, W.G.; Barker, R.W.; Kelly, I.D.; Knowles, P.F.
Human placental diamine oxidase. Improved purification and characterization of a copper- and manganese-containing amine oxidase with novel substrate specificity
Biochem. J.
155
679-687
1976
Homo sapiens
Manually annotated by BRENDA team
Suzuki, O.; Matsumoto, T.
Purification and properties of diamine oxidase from human kidney
Biogenic Amines
4
237-245
1987
Homo sapiens
-
Manually annotated by BRENDA team
Elmore, B.O.; Bollinger, J.A.; Dooley, D.M.
Human kidney diamine oxidase: heterologous expression, purification, and characterization
J. Biol. Inorg. Chem.
7
565-579
2002
Homo sapiens
Manually annotated by BRENDA team
Juda, G.A.; Shepard, E.M.; Elmore, B.O.; Dooley, D.M.
A comparative study of the binding and inhibition of four copper-containing amine oxidases by azide: implications for the role of copper during the oxidative half-reaction
Biochemistry
45
8788-8800
2006
Arthrobacter globiformis, Homo sapiens, Komagataella pastoris, Pisum sativum
Manually annotated by BRENDA team
Garcia-Martin, E.; Ayuso, P.; Martinez, C.; Agundez, J.A.
Improved analytical sensitivity reveals the occurrence of gender-related variability in diamine oxidase enzyme activity in healthy individuals
Clin. Biochem.
40
1339-1341
2007
Homo sapiens
Manually annotated by BRENDA team
Maintz, L.; Schwarzer, V.; Bieber, T.; van der Ven, K.; Novak, N.
Effects of histamine and diamine oxidase activities on pregnancy: a critical review
Hum. Reprod. Update
14
485-495
2008
Homo sapiens
Manually annotated by BRENDA team
ORourke, A.M.; Wang, E.Y.; Miller, A.; Podar, E.M.; Scheyhing, K.; Huang, L.; Kessler, C.; Gao, H.; Ton-Nu, H.T.; Macdonald, M.T.; Jones, D.S.; Linnik, M.D.
Anti-inflammatory effects of LJP 1586 [Z-3-fluoro-2-(4-methoxybenzyl)allylamine hydrochloride], an amine-based inhibitor of semicarbazide-sensitive amine oxidase activity
J. Pharmacol. Exp. Ther.
324
867-875
2008
Homo sapiens
Manually annotated by BRENDA team
Ayuso, P.; Garcia-Martin, E.; Martinez, C.; Agundez, J.A.
Genetic variability of human diamine oxidase: occurrence of three nonsynonymous polymorphisms and study of their effect on serum enzyme activity
Pharmacogenet. Genomics
17
687-693
2007
Homo sapiens
Manually annotated by BRENDA team
Kofler, H.; Aberer, W.; Deibl, M.; Hawranek, T.; Klein, G.; Reider, N.; Fellner, N.
Diamine oxidase (DAO) serum activity: Not a useful marker for diagnosis of histamine intolerance
Allergo J.
32
105-109
2009
Homo sapiens
-
Manually annotated by BRENDA team
McGrath, A.P.; Hilmer, K.M.; Collyer, C.A.; Shepard, E.M.; Elmore, B.O.; Brown, D.E.; Dooley, D.M.; Guss, J.M.
Structure and inhibition of human diamine oxidase
Biochemistry
48
9810-9822
2009
Homo sapiens (P19801), Homo sapiens
Manually annotated by BRENDA team
McGrath, A.P.; Hilmer, K.M.; Collyer, C.A.; Dooley, D.M.; Guss, J.M.
A new crystal form of human diamine oxidase
Acta Crystallogr. Sect. F
66
137-142
2010
Homo sapiens (P19801), Homo sapiens
Manually annotated by BRENDA team
McGrath, A.P.; Caradoc-Davies, T.; Collyer, C.A.; Guss, J.M.
Correlation of active site metal content in human diamine oxidase with trihydroxyphenylalanine quinone cofactor biogenesis
Biochemistry
49
8316-8324
2010
Homo sapiens (P19801), Homo sapiens
Manually annotated by BRENDA team
Schwelberger, H.G.; Feurle, J.; Ahrens, F.
Characterization of diamine oxidase from human seminal plasma
J. Neural Transm.
120
983-986
2013
Homo sapiens
Manually annotated by BRENDA team
Bartko, J.; Gludovacz, E.; Petroczi, K.; Borth, N.; Jilma, B.; Boehm, T.
Recombinant human diamine oxidase activity is not inhibited by ethanol, acetaldehyde, disulfiram, diethyldithiocarbamate or cyanamide
Alcohol
54
51-59
2016
Homo sapiens
Manually annotated by BRENDA team
Gludovacz, E.; Maresch, D.; Bonta, M.; Szoelloesi, H.; Furtmueller, P.G.; Weik, R.; Altmann, F.; Limbeck, A.; Borth, N.; Jilma, B.; Boehm, T.
Characterization of recombinant human diamine oxidase (rhDAO) produced in Chinese Hamster Ovary (CHO) cells
J. Biotechnol.
227
120-130
2016
Homo sapiens
Manually annotated by BRENDA team
Kacik, J.; Wroblewska, B.; Lewicki, S.; Zdanowski, R.; Kalicki, B.
Serum diamine oxidase in pseudoallergy in the pediatric population
Adv. Exp. Med. Biol.
1039
35-44
2018
Homo sapiens
Manually annotated by BRENDA team
Boehm, T.; Pils, S.; Gludovacz, E.; Szoelloesi, H.; Petroczi, K.; Majdic, O.; Quaroni, A.; Borth, N.; Valent, P.; Jilma, B.
Quantification of human diamine oxidase
Clin. Biochem.
50
444-451
2017
Homo sapiens (P19801), Homo sapiens
Manually annotated by BRENDA team
Boehm, T.; Karer, M.; Gludovacz, E.; Petroczi, K.; Resch, M.; Schuetzenberger, K.; Klavins, K.; Borth, N.; Jilma, B.
Simple, sensitive and specific quantification of diamine oxidase activity in complex matrices using newly discovered fluorophores derived from natural substrates
Inflamm. Res.
69
937-950
2020
Homo sapiens (P19801), Homo sapiens
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