Primary amine oxidase (P46883)

Identification
Name:Primary amine oxidase
Synonyms:
  • 2-phenylethylamine oxidase
  • Copper amine oxidase
  • Tyramine oxidase
Gene Name:tynA
Enzyme Class:
Biological Properties
General Function:Involved in copper ion binding
Specific Function:The enzyme prefers aromatic over aliphatic amines
Cellular Location:Periplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Tyramine + 1.0Water + 1.0Oxygen ↔ 1.04-Hydroxyphenylacetaldehyde + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Aminoacetone + 1.0Water + 1.0Oxygen ↔ 1.0Pyruvaldehyde + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Phenylethylamine + 1.0Oxygen + 1.0Water ↔ 1.0Phenylacetaldehyde + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.01,3-Diaminopropane+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.01,3-Diaminopropane + 1.0Oxygen + 1.0Water ↔ 1.03-Aminopropionaldehyde + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Dopamine + 1.0Water + 1.0Oxygen ↔ 1.03,4-Dihydroxyphenylacetaldehyde + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Aminoacetone + 1.0Water + 1.0Oxygen → 1.0Hydrogen ion + 1.0Pyruvaldehyde + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0Oxygen + 1.0Phenylethylamine → 1.0Hydrogen ion + 1.0Hydrogen peroxide + 1.0Ammonia + 1.0Phenylacetaldehyde
ReactionCard
1.0Primary amine+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Primary amine + 1.0Water + 1.0Oxygen ↔ 1.0Aldehyde + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Aminoacetone + 1.0Oxygen + 1.0Water → 1.0Hydrogen peroxide + 1.0Ammonium + 1.0Pyruvaldehyde
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Aminoacetone + 1.0Water + 1.0Oxygen → 1.0Hydrogen ion + 1.0Pyruvaldehyde + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0Oxygen + 1.0Phenylethylamine → 1.0Hydrogen ion + 1.0Hydrogen peroxide + 1.0Ammonia + 1.0Phenylacetaldehyde
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Dopamine + 1.0Water + 1.0Oxygen → 1.03,4-Dihydroxyphenylacetaldehyde + 1.0Hydrogen peroxide + 1.0Ammonium
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0Oxygen + 1.0Tyramine → 1.04-Hydroxyphenylacetaldehyde + 1.0Hydrogen peroxide + 1.0Ammonium
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0Oxygen + 1.0Phenylethylamine → 1.0Hydrogen peroxide + 1.0Ammonium + 1.0Phenylacetaldehyde
ReactionCard
1.0RCH(2)NH(2)+1.0Thumb+1.0Thumb → 1.0RCHO+1.0Thumb+1.0Thumb
1.0RCH(2)NH(2) + 1.0Water + 1.0Oxygen → 1.0RCHO + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Phenylethylamine + 1.0Water + 1.0Oxygen → 1.0Phenylacetaldehyde + 1.0Ammonia + 1.0Hydrogen peroxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB037913,4-DihydroxyphenylacetaldehydeMetaboCard
ECMDB011063-AminopropionaldehydeMetaboCard
ECMDB200934-HydroxyphenylacetaldehydeMetaboCard
ECMDB02134AminoacetoneMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB02322CadaverineMetaboCard
ECMDB00073DopamineMetaboCard
ECMDB01426FormaldehydeMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21232Hydrogen peroxideMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB06236PhenylacetaldehydeMetaboCard
ECMDB02654PhenylethylamineMetaboCard
ECMDB01167PyruvaldehydeMetaboCard
ECMDB00306TyramineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
cofactor binding
copper ion binding
ion binding
metal ion binding
oxidoreductase activity
oxidoreductase activity, acting on the CH-NH2 group of donors
oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
primary amine oxidase activity
quinone binding
transition metal ion binding
Process
amine metabolic process
metabolic process
nitrogen compound metabolic process
oxidation reduction
Gene Properties
Blattner:b1386
Gene OrientationCounterclockwise
Centisome Percentage:31.19
Left Sequence End1447100
Right Sequence End1449373
Gene Sequence:
>2274 bp
ATGGGAAGCCCCTCTCTGTATTCTGCCCGTAAAACAACCCTGGCGTTGGCAGTCGCCTTA
AGTTTCGCCTGGCAAGCGCCGGTATTTGCCCACGGTGGTGAAGCGCATATGGTGCCAATG
GATAAAACGCTTAAAGAATTTGGTGCCGATGTGCAGTGGGACGACTACGCCCAGCTCTTT
ACCCTGATTAAAGATGGCGCGTACGTGAAAGTGAAGCCTGGTGCGCAAACAGCAATTGTT
AATGGTCAGCCTCTGGCACTGCAAGTACCGGTAGTGATGAAAGACAATAAAGCCTGGGTT
TCTGACACCTTTATTAACGATGTTTTCCAGTCCGGGCTGGATCAAACCTTTCAGGTAGAA
AAGCGCCCTCACCCACTTAATGCGCTAACTGCGGACGAAATTAAACAGGCCGTTGAAATT
GTTAAAGCTTCCGCGGACTTCAAACCCAATACCCGTTTTACTGAGATCTCCCTGCTACCG
CCAGATAAAGAAGCTGTCTGGGCGTTTGCGCTGGAAAACAAACCGGTTGACCAGCCGCGC
AAAGCCGACGTCATTATGCTCGACGGCAAACATATCATCGAAGCGGTGGTGGATCTGCAA
AACAACAAACTGCTCTCCTGGCAACCCATTAAAGACGCCCACGGTATGGTGTTGCTGGAT
GATTTCGCCAGTGTGCAGAACATTATTAACAACAGTGAAGAATTTGCCGCTGCCGTGAAG
AAACGCGGTATTACTGATGCGAAAAAAGTGATTACCACGCCGCTGACCGTAGGTTATTTC
GATGGTAAAGATGGCCTGAAACAAGATGCCCGGTTGCTCAAAGTCATCAGCTATCTTGAT
GTCGGTGATGGCAACTACTGGGCACATCCCATCGAAAACCTGGTGGCGGTCGTTGATTTA
GAACAGAAAAAAATCGTTAAGATTGAAGAAGGTCCGGTAGTTCCGGTGCCAATGACCGCA
CGCCCATTTGATGGCCGTGACCGCGTTGCTCCGGCAGTTAAGCCTATGCAAATCATTGAG
CCTGAAGGTAAAAATTACACCATTACTGGCGATATGATTCACTGGCGGAACTGGGATTTT
CACCTCAGCATGAACTCTCGCGTCGGGCCGATGATCTCCACCGTGACTTATAACGACAAT
GGCACCAAACGCAAAGTCATGTACGAAGGTTCTCTCGGCGGCATGATTGTGCCTTACGGT
GATCCTGATATTGGCTGGTACTTTAAAGCGTATCTGGACTCTGGTGACTACGGTATGGGC
ACGCTAACCTCACCAATTGCTCGTGGTAAAGATGCCCCGTCTAACGCAGTGCTCCTTAAT
GAAACCATCGCCGACTACACTGGCGTGCCGATGGAGATCCCTCGCGCTATCGCGGTATTT
GAACGTTATGCCGGGCCGGAGTATAAGCATCAGGAAATGGGCCAGCCCAACGTCAGTACC
GAACGCCGGGAGTTAGTGGTGCGCTGGATCAGTACAGTGGGTAACTATGACTACATTTTT
GACTGGATCTTCCATGAAAACGGCACTATTGGCATCGATGCCGGTGCTACGGGCATCGAA
GCGGTGAAAGGTGTTAAAGCGAAAACCATGCACGATGAGACGGCGAAAGATGACACGCGC
TACGGCACGCTTATCGATCACAATATCGTGGGTACTACACACCAACATATTTATAATTTC
CGCCTCGATCTGGATGTAGATGGCGAGAATAACAGCCTGGTGGCGATGGACCCAGTGGTA
AAACCGAATACTGCCGGTGGCCCACGCACCAGTACCATGCAAGTTAATCAGTACAACATC
GGCAATGAACAGGATGCCGCACAGAAATTTGATCCGGGCACGATTCGTCTGTTGAGTAAC
CCGAACAAAGAGAACCGCATGGGCAATCCGGTTTCCTATCAAATTATTCCTTATGCAGGT
GGTACTCACCCGGTAGCAAAAGGTGCCCAGTTCGCGCCGGACGAGTGGATCTATCATCGT
TTAAGCTTTATGGACAAGCAGCTCTGGGTAACGCGTTATCATCCTGGCGAGCGTTTCCCG
GAAGGCAAATATCCGAACCGTTCTACTCATGACACCGGTCTTGGACAATACAGTAAGGAT
AACGAGTCGCTGGACAACACCGACGCCGTTGTCTGGATGACCACCGGCACCACACATGTG
GCCCGCGCCGAAGAGTGGCCGATTATGCCGACCGAATGGGTACATACTCTGCTGAAACCA
TGGAACTTCTTTGACGAAACGCCAACGCTAGGGGCGCTGAAGAAAGATAAGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:757
Protein Molecular Weight:84378
Protein Theoretical pI:6
PDB File:1DYU
Signaling Regions:
  • 1-30
Transmembrane Regions:
  • None
Protein Sequence:
>Primary amine oxidase
MGSPSLYSARKTTLALAVALSFAWQAPVFAHGGEAHMVPMDKTLKEFGADVQWDDYAQLF
TLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVE
KRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPR
KADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAAVK
KRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDL
EQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHWRNWDF
HLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMG
TLTSPIARGKDAPSNAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVST
ERRELVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAKDDTR
YGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNI
GNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGAQFAPDEWIYHR
LSFMDKQLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHV
ARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKKDK
References
External Links:
ResourceLink
Uniprot ID:P46883
Uniprot Name:AMO_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742266
PDB ID:1DYU
Ecogene ID:EG13140
Ecocyc:EG13140
ColiBase:b1386
Kegg Gene:b1386
EchoBASE ID:EB2934
CCDB:AMO_ECOLI
BacMap:162135920
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Ferrandez, A., Minambres, B., Garcia, B., Olivera, E. R., Luengo, J. M., Garcia, J. L., Diaz, E. (1998). "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway." J Biol Chem 273:25974-25986. Pubmed: 9748275
  • Ferrandez, A., Prieto, M. A., Garcia, J. L., Diaz, E. (1997). "Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli." FEBS Lett 406:23-27. Pubmed: 9109378
  • Hanlon, S. P., Hill, T. K., Flavell, M. A., Stringfellow, J. M., Cooper, R. A. (1997). "2-phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression." Microbiology 143 ( Pt 2):513-518. Pubmed: 9043126
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Murray, J. M., Saysell, C. G., Wilmot, C. M., Tambyrajah, W. S., Jaeger, J., Knowles, P. F., Phillips, S. E., McPherson, M. J. (1999). "The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants." Biochemistry 38:8217-8227. Pubmed: 10387067
  • Parsons, M. R., Convery, M. A., Wilmot, C. M., Yadav, K. D., Blakeley, V., Corner, A. S., Phillips, S. E., McPherson, M. J., Knowles, P. F. (1995). "Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution." Structure 3:1171-1184. Pubmed: 8591028
  • Steinebach, V., Benen, J. A., Bader, R., Postma, P. W., De Vries, S., Duine, J. A. (1996). "Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme." Eur J Biochem 237:584-591. Pubmed: 8647101
  • Wilmot, C. M., Hajdu, J., McPherson, M. J., Knowles, P. F., Phillips, S. E. (1999). "Visualization of dioxygen bound to copper during enzyme catalysis." Science 286:1724-1728. Pubmed: 10576737
  • Wilmot, C. M., Murray, J. M., Alton, G., Parsons, M. R., Convery, M. A., Blakeley, V., Corner, A. S., Palcic, M. M., Knowles, P. F., McPherson, M. J., Phillips, S. E. (1997). "Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction." Biochemistry 36:1608-1620. Pubmed: 9048544
  • Yamashita, M., Azakami, H., Yokoro, N., Roh, J. H., Suzuki, H., Kumagai, H., Murooka, Y. (1996). "maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli." J Bacteriol 178:2941-2947. Pubmed: 8631685