Primary amine oxidase

Details

Name
Primary amine oxidase
Synonyms
  • 1.4.3.21
  • 2-phenylethylamine oxidase
  • Copper amine oxidase
  • maoA
  • Tyramine oxidase
Gene Name
tynA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0010851|Primary amine oxidase
MGSPSLYSARKTTLALAVALSFAWQAPVFAHGGEAHMVPMDKTLKEFGADVQWDDYAQLF
TLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVE
KRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPR
KADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAAVK
KRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDL
EQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHWRNWDF
HLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMG
TLTSPIARGKDAPSNAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVST
ERRELVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAKDDTR
YGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNI
GNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGAQFAPDEWIYHR
LSFMDKQLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHV
ARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKKDK
Number of residues
757
Molecular Weight
84378.17
Theoretical pI
5.71
GO Classification
Functions
aliphatic-amine oxidase activity / aminoacetone / calcium ion binding / copper ion binding / phenethylamine / primary amine oxidase activity / quinone binding / tryptamine
Processes
L-phenylalanine catabolic process / oxidation-reduction process / phenylethylamine catabolic process
Components
periplasmic space
General Function
Tryptamine:oxygen oxidoreductase (deaminating) activity
Specific Function
The enzyme prefers aromatic over aliphatic amines.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0010852|Primary amine oxidase (tynA)
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
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP46883
UniProtKB Entry NameAMO_ECOLI
GenBank Protein ID809499
GenBank Gene IDD23670
General References
  1. Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF: Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution. Structure. 1995 Nov 15;3(11):1171-84. [Article]
  2. Steinebach V, Benen JA, Bader R, Postma PW, De Vries S, Duine JA: Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme. Eur J Biochem. 1996 May 1;237(3):584-91. [Article]
  3. 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 al.: 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. 1996 Dec 31;3(6):363-77. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E: Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J Biol Chem. 1998 Oct 2;273(40):25974-86. [Article]
  7. Ferrandez A, Prieto MA, Garcia JL, Diaz E: Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli. FEBS Lett. 1997 Apr 7;406(1-2):23-7. [Article]
  8. Yamashita M, Azakami H, Yokoro N, Roh JH, Suzuki H, Kumagai H, Murooka Y: maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli. J Bacteriol. 1996 May;178(10):2941-7. [Article]
  9. Hanlon SP, Hill TK, Flavell MA, Stringfellow JM, Cooper RA: 2-phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression. Microbiology. 1997 Feb;143 ( Pt 2):513-8. [Article]
  10. Wilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, Corner AS, Palcic MM, Knowles PF, McPherson MJ, Phillips SE: Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction. Biochemistry. 1997 Feb 18;36(7):1608-20. [Article]
  11. Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SE, McPherson MJ: The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants. Biochemistry. 1999 Jun 29;38(26):8217-27. [Article]
  12. Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE: Visualization of dioxygen bound to copper during enzyme catalysis. Science. 1999 Nov 26;286(5445):1724-8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB016342-Oxy-4-Hydroxy-5-(2-Hydrazinopyridine)PhenylalanineexperimentalunknownDetails
DB016572-amino-3-[4-hydroxy-6-oxo-3-(2-phenyl-cyclopropylimino)-cyclohexa-1,4-dienyl]-propionic acidexperimentalunknownDetails
DB02178PhenylacetaldehydeexperimentalunknownDetails
DB029283-Amino-6-Hydroxy-TyrosineexperimentalunknownDetails
DB036313-(4-hydroxy-3-imino-6-oxo-cyclohexa-1,4-dienyl)-alanineexperimentalunknownDetails
DB04325PhenethylamineexperimentalunknownDetails
DB043346-hydroxydopa quinoneexperimentalunknownDetails
DB01576Dextroamphetamineapproved, illicitnosubstrateDetails