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Information on EC 1.5.3.16 - spermine oxidase and Organism(s) Homo sapiens

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EC Tree
     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.3 With oxygen as acceptor
                1.5.3.16 spermine oxidase
IUBMB Comments
The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency . The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming) and EC 1.5.3.17 (non-specific polyamine oxidase).
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
spermine oxidase, smo(paoh1), atpao1, paoh1/smo, smo/paoh1, msmoalpha, msmomu, ghpao, fms1 protein, spm oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hSMO
-
-
PAOh1/SMO
-
SMO(PAOh1)
-
-
SMO/PAOh1
-
-
SMO5
splice variant protein
spermine oxidase
-
-
Spm oxidase
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
spermidine:oxygen oxidoreductase (spermidine-forming)
The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency [3]. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming) and EC 1.5.3.17 (non-specific polyamine oxidase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,16-diamino-4,8,13-triazahexadecane + O2 + H2O
?
show the reaction diagram
-
increased activity compared to spermine
-
-
?
1,16-diamino-4,8,13-triazahexadecane pentahydrochloride + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-methylspermine + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
N,N'-bis-(3-benzylaminopropyl)butane-1,4-diamine + O2 + H2O
N-(3-aminopropyl)-N'-(3-benzylaminopropyl)butane-1,4-diamine + N1-(3-benzylaminopropyl)butane-1,4-diamine + H2O2 + ?
show the reaction diagram
-
-
main products
-
?
N,N'-bis-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-ethylaminopropyl)butane-1,4-diamine + H2O2 + ?
show the reaction diagram
-
minor N4-endo cleavage pathways resulting in formation of EtDAP
-
-
?
N-(3-aminopropyl)-N-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O
spermine + H2O2 + ?
show the reaction diagram
-
-
i.e. N,N'-bis-(3-aminopropyl)butane-1,4-diamine
-
?
N-(3-benzylaminopropyl)-N'-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-ethylaminopropyl)butane-1,4-diamine + H2O2 + ?
show the reaction diagram
-
-
-
-
?
N1-acetylspermine + O2 + H2O
?
show the reaction diagram
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
show the reaction diagram
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
show the reaction diagram
-
low activity
-
-
?
N1-ethyl-spermine + O2 + H2O
spermidine + N-ethyl-3-aminopropanal + H2O2
show the reaction diagram
-
good substrate
-
-
?
N1-monoethylspermine + O2 + H2O
spermidine + ?
show the reaction diagram
98% of the activity with spermine
-
-
?
spermine + O2 + H2O
?
show the reaction diagram
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
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
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
-
flavoprotein
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bis(ethyl)norspermine
-
structure modeling analysis of complex formed with SMO
MDL-72527
0.2 mM, 41% inhibition
N-(3-aminopropyl)-N-2,3-butadienyl-1,4-butanediamine
potent inhibition
N-(3-[[3-(dimethylamino)propyl]amino]propyl)-8-quinolinecarboxamide
i.e. SI-4650, inhibits spermine oxidase enzyme activity, increases substrate spermine content and reduces product spermidine content. Treatment suppresses cell proliferation and migration, the inhibitor causes cell cycle arrest, induces cell apoptosis, and promotes autophagy
-
N-[3-(2,3-butadienylamino)propyl]-1,4-butanediamine
moderate inhibition
N1,N11-diethylnorspermine
0.2 mM, 21% inhibition
N1,N12-diethylspermine
0.2 mM, 15% inhibition
N1,N14-diethylhomospermine
0.2 mM, 49% inhibition
N1,N4-bis(2,3-butadienyl)-1,4 butanediamine
-
i.e. MDL72527
N1,N4-bis(2,3-butadienyl)-1,4-butanediamine
N1-(n-octanesulfonyl)spermine
0.2 mM, 86% inhibition
N1-ethyl-N11-(cyclopropyl)-methyl-4,8-diazaundecane
-
structure modeling analysis of complex formed with SMO
SL-11144
potent inhibitor of PAOh1/SMO, IC50 below 0.01 mM
SL-11150
potent inhibitor of PAOh1/SMO, IC50 below 0.01 mM
SL-11158
potent inhibitor of PAOh1/SMO, IC50 below 0.01 mM
spermidine
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HIV-1 Tat
-
Tat-induced SMO activation, involving the polyamine-sensitive subtype of the NMDA receptor, the activation is completely prevented by the NMDAR antagonist MK-801. Mechanism, overview
-
N1,N11-diethylnorspermine
-
polyamine analogue with clinical relevance as an experimental anticancer agent. Treatment of human C-28/I2 chondrocytes rapidly induces spermidine/spermine N1-acetyltransferase and spermine oxidase activities, and down-regulates ornithine decarboxylase. The treatment does not provoke cell death and caspase activation when given alone for 24 h, but causes a caspase-3 and -9 dependent apoptosis in chondrocytes further exposed to cycloheximide. The simultaneous addition of N1,N11-diethylnorspermine and cycloheximide rapidly increases caspase activity in C-28/I2 cells in the absence of spermidine/spermineN1-acetyltransferase and spermine oxidase induction or significant reduction of polyamine levels
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034 - 0.067
alpha-methylspermine
0.051 - 2
N1-acetylspermine
0.0005 - 0.19
spermine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28
N1-acetylspermine
3.11 - 7.55
spermine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
N1-acetylspermine
37
spermine
-
pH 8.3, 25Ā°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
the activity markedly decreases from pH 9.0 to pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the antiproliferative effects of analogue N1,N1-bis(ethyl)norspermine in MDA-MB-231 cells are mediated in part through the production of H2O2 by SMO(PAOh1) and by the export of acetylated polyamines formed by the activity of spermidine/spermine N1-acetyltransferase
Manually annotated by BRENDA team
hepatocellular carcinoma cell
Manually annotated by BRENDA team
-
mononuclear inflammatory cells
Manually annotated by BRENDA team
-
tissues from patients diagnosed with prostate cancer and prostatic intraepithelial neoplasia exhibit, on average, locally increased spermine oxidase (SMO) expression in regions of prostatic disease and higher overall SMO expression in prostatic epithelial cells compared to healthy individuals
Manually annotated by BRENDA team
monocytic cell line
Manually annotated by BRENDA team
additional information
-
immunohistochemic detection of enzyme expression in different tissue during inflammation, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SMOX localizes to the bile canalicular lumen of hepatocytes
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
phylogenetic analysis and structure-function relationships of spermine oxidases among vertebrates, overview. Polar residues (His82, Gln200, Glu224, Tyr482, Ser527, Thr528) and hydrophobic residues (Trp80 and Trp427), hypothesized to bind spermine in the correct position, are strictly conserved in all SMOs
malfunction
-
decreased expression of SMO is observed in brains of suicide completers. SMO dysregulation can alter polyamine homeostasis affecting polyamine catabolism, which has been observed to be often associated with several disease states. The late induction of SMO correlates very well with Spm increase in the ipsilateral injured regions compared to equivalent controlateral regions, suggesting that SMO activity might be elevated at later times post-injury. Spermine oxidation may also be considered a source of secondary tissue damage, increased inflammation and apoptotic cell death in the injured brain
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SMOX_HUMAN
555
0
61819
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61900
x * 61900, SMO/PAOh1, SDS-PAGE
62000
x * 62000, SDS-PAGE
64000
x * 64000, SDS-PAGE
65000
x * 65000, SMO5, SDS-PAGE
68000
-
x * 68000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
melting temperature, presence of dithiothreitol
56
meling temperature
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
recombinant enzyme, SMO/PAOh1
recombinant enzyme, SMO5
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA is transiently transfected into HEK-293 cells
expressed in HEK 293 cells
expression in Escherichia coli
expression in HEK-293 cells
-
gene hSMO, expression in Escherichia coli strain BL21(DE3)
-
gene SMOX, phylogenetic analysis
-
SMO/PAOh1 cDNA is subcloned into the pET15b bacterial expression vector, expression in Escherichia coli. NCI-H157 human non-small cell lung carcinoma cells are stably transfected, and individual clones selected that overexpress the enzyme
SMO5 cDNA is subcloned into the pET15b bacterial expression vector, expression in Escherichia coli. NCI-H157 human non-small cell lung carcinoma cells are stably transfected, and individual clones selected that overexpress the enzyme
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ability of Tat to upregulate the activity of spermine oxidase, the polyamine catabolic enzyme that specifically oxidizes spermine, with the production of spermidine, H2O2, and 3-aminopropanal, through stimulation of the NMDA receptor, mechanism, overview
-
both the expression level of SMO mRNA and SMO enzyme activity are significantly lower in breast cancer samples compared to nontumor samples
-
increased expression of spermine oxidase in ulcerative colitis and in prostate cancer and prostate intraepithelial neoplasia tissues. SMO expression is upregulated in gastritis tissues from patients with Helicobacter pylori infection, it is upregulated in both macrophages and epithelial cells
-
no induction of SMO activity by N-alkylated polyamine analogues
-
SMO is a highly inducible enzyme by a variety of stressful stimuli, including several antitumor polyamine analogues. Tumor-necrosis factor-alpha can induce H2O2 production via SMO gene upregulation
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
protein is first purified from the cell lysate under denaturing conditions and renatured by dialysis against decreasing concentrations of urea
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Y.; Devereux, W.; Woster, P.M.; Stewart, T.M.; Hacker, A.; Casero, R.A., Jr.
Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure
Cancer Res.
61
5370-5373
2001
Homo sapiens (Q9NWM0)
Manually annotated by BRENDA team
Wang, Y.; Murray-Stewart, T.; Devereux, W.; Hacker, A.; Frydman, B.; Woster, P.M.; Casero, R.A.Jr.
Properties of purified human polyamine oxidase, PAOh1/SMO
Biochem. Biophys. Res. Commun.
304
605-611
2003
Homo sapiens (Q9NWM0), Homo sapiens
Manually annotated by BRENDA team
Vujcic, S.; Diegelman, P.; Bacchi, C.J.; Kramer, D.L.; Porter, C.W.
Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin
Biochem. J.
367
665-675
2002
Homo sapiens (Q9NWM0), Homo sapiens, Mus musculus (Q99K82), Mus musculus
Manually annotated by BRENDA team
Wang, Y.; Hacker, A.; Murray-Stewart, T.; Fleischer, J.G.; Woster, P.M.
Induction of human spermine oxidase SMO(PAOh1) is regulated at the levels of new mRNA synthesis, mRNA stabilization and newly synthesized protein
Biochem. J.
386
543-547
2005
Homo sapiens
Manually annotated by BRENDA team
Babbar, N.; Casero, R.A.
Tumor necrosis factor-alpha increases reactive oxygen species by inducing spermine oxidase in human lung epithelial cells: a potential mechanism for inflammation-induced carcinogenesis
Cancer Res.
66
11125-11130
2006
Homo sapiens
Manually annotated by BRENDA team
Murray-Stewart, T.; Wang, Y.; Goodwin, A.; Hacker A.; Meeker, A.; casero, R.A.
Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology
FEBS J.
275
2795-2806
2008
Homo sapiens, Homo sapiens (Q9NWM0)
Manually annotated by BRENDA team
Pledgie, A.; Huang, Y.; Hacker, A.; Zhang, Z.; Woster, P.M.; Davidson, N.E.; Casero, R.A.
Spermine oxidase SMO(PAOh1), not N1-acetylpolyamine oxidase PAO, is the primary source of cytotoxic H2O2 in polyamine analogue-treated human breast cancer cell lines
J. Biol. Chem.
280
39843-39851
2005
Homo sapiens
Manually annotated by BRENDA team
Järvinen, A.; Grigorenko, N.; Khomutov, A.R.; Hyvönen, M.T.; Uimari, A.; Vepsäläinen, J.; Sinervirta, R.; Keinänen, T.A.; Vujcic, S.; Alhonen, L.; Porter, C.W.; Jänne, J.
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural polyamines.
J. Biol. Chem.
280
6595-6601
2005
Homo sapiens
Manually annotated by BRENDA team
Goodwin, A.C.; Jadallah, S.; Toubaji, A.; Lecksell, K.; Hicks, J.L.; Kowalski, J.; Bova, G.S.; de Marzo, A.M.; Netto, G.J.; Casero, R.A.
Increased spermine oxidase expression in human prostate cancer and prostatic intraepithelial neoplasia tissues
Prostate
68
766-772
2008
Homo sapiens
Manually annotated by BRENDA team
Adachi, M.S.; Juarez, P.R.; Fitzpatrick, P.F.
Mechanistic studies of human spermine oxidase: kinetic mechanism and pH effects
Biochemistry
49
386-392
2010
Homo sapiens
Manually annotated by BRENDA team
Cervelli, M.; Bellavia, G.; Fratini, E.; Amendola, R.; Polticelli, F.; Barba, M.; Federico, R.; Signore, F.; Gucciardo, G.; Grillo, R.; Woster, P.; Casero Jr, R.; Mariottini, P.
Spermine oxidase (SMO) activity in breast tumor tissues and biochemical analysis of the anticancer spermine analogues BENSpm and CPENSpm
BMC Cancer
10
555
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Fiori, L.M.; Turecki, G.
Genetic and epigenetic influences on expression of spermine synthase and spermine oxidase in suicide completers
Int. J. Neuropsychopharmacol.
13
725-736
2010
Homo sapiens
Manually annotated by BRENDA team
Stanic, I.; Facchini, A.; Borzi, R.; Stefanelli, C.; Flamigni, F.
The polyamine analogue N1,N11-diethylnorspermine can induce chondrocyte apoptosis independently of its ability to alter metabolism and levels of natural polyamines
J. Cell. Physiol.
219
109-116
2009
Homo sapiens
Manually annotated by BRENDA team
Häkkinen, M.; Hyönen, M.; Auriola, S.; Casero Jr., R.; Vepsäläinen, J.; Khomutov, A.; Alhonen, L.; Keinänen, T.
Metabolism of N-alkylated spermine analogues by polyamine and spermine oxidases
Amino Acids
38
369-381
2010
Homo sapiens
Manually annotated by BRENDA team
Cervelli, M.; Amendola, R.; Polticelli, F.; Mariottini, P.
Spermine oxidase: ten years after
Amino Acids
42
441-450
2012
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Moriya, S.; Iwasaki, K.; Samejima, K.; Takao, K.; Kohda, K.; Hiramatsu, K.; Kawakita, M.
A mass spectrometric method to determine activities of enzymes involved in polyamine catabolism
Anal. Chim. Acta
748
45-52
2012
Homo sapiens
Manually annotated by BRENDA team
Takao, K.; Shirahata, A.; Samejima, K.; Casero, R.A.; Igarashi, K.; Sugita, Y.
Pentamines as substrate for human spermine oxidase
Biol. Pharm. Bull.
36
407-411
2013
Homo sapiens
Manually annotated by BRENDA team
Capone, C.; Cervelli, M.; Angelucci, E.; Colasanti, M.; Macone, A.; Mariottini, P.; Persichini, T.
A role for spermine oxidase as a mediator of reactive oxygen species production in HIV-Tat-induced neuronal toxicity
Free Radic. Biol. Med.
63
99-107
2013
Homo sapiens
Manually annotated by BRENDA team
Hong, S.K.; Chaturvedi, R.; Piazuelo, M.B.; Coburn, L.A.; Williams, C.S.; Delgado, A.G.; Casero, R.A.; Schwartz, D.A.; Wilson, K.T.
Increased expression and cellular localization of spermine oxidase in ulcerative colitis and relationship to disease activity
Inflamm. Bowel Dis.
16
1557-1566
2010
Homo sapiens
Manually annotated by BRENDA team
Cervelli, M.; Salvi, D.; Polticelli, F.; Amendola, R.; Mariottini, P.
in the evolutionary framework of spermine oxidase
J. Mol. Evol.
76
365-370
2013
Homo sapiens, vertebrata, Mus musculus (Q99K82)
Manually annotated by BRENDA team
Chaturvedi, R.; Asim, M.; Barry, D.P.; Frye, J.W.; Casero, R.A.; Wilson, K.T.
Spermine oxidase is a regulator of macrophage host response to Helicobacter pylori enhancement of antimicrobial nitric oxide generation by depletion of spermine
Amino Acids
46
531-542
2014
Homo sapiens (Q9NWM0), Homo sapiens, Mus musculus (Q99K82), Mus musculus
Manually annotated by BRENDA team
Moriya, S.S.; Miura, T.; Takao, K.; Sugita, Y.; Samejima, K.; Hiramatsu, K.; Kawakita, M.
Development of irreversible inactivators of spermine oxidase and N1-acetylpolyamine oxidase
Biol. Pharm. Bull.
37
475-480
2014
Homo sapiens (Q9NWM0), Homo sapiens
Manually annotated by BRENDA team
Leonetti, A.; Cervoni, L.; Polticelli, F.; Kanamori, Y.; Yurtsever, Z.N.; Agostinelli, E.; Mariottini, P.; Stano, P.; Cervelli, M.
Spectroscopic and calorimetric characterization of spermine oxidase and its association forms
Biochem. J.
474
4253-4268
2017
Homo sapiens (Q9NWM0), Homo sapiens
Manually annotated by BRENDA team
Hu, T.; Sun, D.; Zhang, J.; Xue, R.; Janssen, H.L.A.; Tang, W.; Dong, L.
Spermine oxidase is upregulated and promotes tumor growth in hepatocellular carcinoma
Hepatol. Res.
48
967-977
2018
Homo sapiens (Q9NWM0), Homo sapiens
Manually annotated by BRENDA team
Sun, L.; Yang, J.; Qin, Y.; Wang, Y.; Wu, H.; Zhou, Y.; Cao, C.
Discovery and antitumor evaluation of novel inhibitors of spermine oxidase
J. Enzyme Inhib. Med. Chem.
34
1140-1151
2019
Homo sapiens (Q9NWM0)
Manually annotated by BRENDA team
Uemura, T.; Takasaka, T.; Igarashi, K.; Ikegaya, H.
Spermine oxidase promotes bile canalicular lumen formation through acrolein production
Sci. Rep.
7
14841
2017
Homo sapiens (Q9NWM0)
Manually annotated by BRENDA team