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
- Functionsaliphatic-amine oxidase activity / aminoacetone / calcium ion binding / copper ion binding / phenethylamine / primary amine oxidase activity / quinone binding / tryptamineProcessesL-phenylalanine catabolic process / oxidation-reduction process / phenylethylamine catabolic processComponentsperiplasmic 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
Resource Link UniProtKB ID P46883 UniProtKB Entry Name AMO_ECOLI GenBank Protein ID 809499 GenBank Gene ID D23670 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB01634 2-Oxy-4-Hydroxy-5-(2-Hydrazinopyridine)Phenylalanine experimental unknown Details DB01657 2-amino-3-[4-hydroxy-6-oxo-3-(2-phenyl-cyclopropylimino)-cyclohexa-1,4-dienyl]-propionic acid experimental unknown Details DB02178 Phenylacetaldehyde experimental unknown Details DB02928 3-Amino-6-Hydroxy-Tyrosine experimental unknown Details DB03631 3-(4-hydroxy-3-imino-6-oxo-cyclohexa-1,4-dienyl)-alanine experimental unknown Details DB04325 Phenethylamine experimental unknown Details DB04334 6-hydroxydopa quinone experimental unknown Details DB01576 Dextroamphetamine approved, illicit no substrate Details