Sequence of AMO_ECOLI
EC Number:1.4.3
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Other sequences found for EC No. 1.4.3
EC Number:1.4.3.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2
Other sequences found for EC No. 1.4.3.4
EC Number:1.4.3.6
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Other sequences found for EC No. 1.4.3.6
EC Number:1.4.3.21
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
Other sequences found for EC No. 1.4.3.21
General information:
Sequence
0 MGSPSLYSAR KTTLALAVAL SFAWQAPVFA HGGEAHMVPM DKTLKEFGAD VQWDDYAQLF
60 TLIKDGAYVK VKPGAQTAIV NGQPLALQVP VVMKDNKAWV SDTFINDVFQ SGLDQTFQVE
120 KRPHPLNALT ADEIKQAVEI VKASADFKPN TRFTEISLLP PDKEAVWAFA LENKPVDQPR
180 KADVIMLDGK HIIEAVVDLQ NNKLLSWQPI KDAHGMVLLD DFASVQNIIN NSEEFAAAVK
240 KRGITDAKKV ITTPLTVGYF DGKDGLKQDA RLLKVISYLD VGDGNYWAHP IENLVAVVDL
300 EQKKIVKIEE GPVVPVPMTA RPFDGRDRVA PAVKPMQIIE PEGKNYTITG DMIHWRNWDF
360 HLSMNSRVGP MISTVTYNDN GTKRKVMYEG SLGGMIVPYG DPDIGWYFKA YLDSGDYGMG
420 TLTSPIARGK DAPSNAVLLN ETIADYTGVP MEIPRAIAVF ERYAGPEYKH QEMGQPNVST
480 ERRELVVRWI STVGNYDYIF DWIFHENGTI GIDAGATGIE AVKGVKAKTM HDETAKDDTR
540 YGTLIDHNIV GTTHQHIYNF RLDLDVDGEN NSLVAMDPVV KPNTAGGPRT STMQVNQYNI
600 GNEQDAAQKF DPGTIRLLSN PNKENRMGNP VSYQIIPYAG GTHPVAKGAQ FAPDEWIYHR
660 LSFMDKQLWV TRYHPGERFP EGKYPNRSTH DTGLGQYSKD NESLDNTDAV VWMTTGTTHV
720 ARAEEWPIMP TEWVHTLLKP WNFFDETPTL GALKKDK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
388999
Parsons M.R.,Convery M.A.,Wilmot C.M.,Yadav K.D.S.,Blakeley V.,Corner A.S.,Phillips S.E.V.,McPherson M.J.,Knowles P.F.
Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2-A resolution.
Structure
3
1171-1184
1995
389000
Steinebach V.,Benen J.A.E.,Bader R.,Postma P.W.,De Vries S.,Duine J.A.
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
1996
389001
Aiba H.,Baba T.,Fujita K.,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.,Seki Y.,Sivasundaram S.,Tagami H.,Takeda J.,Takemoto K.,Takeuchi Y.,Wada C.,Yamamoto Y.,Horiuchi T.
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
1996
389002
Blattner F.R.,Plunkett G. III,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.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
389003
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
389004
Ferrandez A.,Minambres B.,Garcia B.,Olivera E.R.,Luengo J.M.,Garcia J.L.,Diaz E.
Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.
J. Biol. Chem.
273
25974-25986
1998
389005
Ferrandez A.,Prieto M.A.,Garcia J.L.,Diaz E.
Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli.
FEBS Lett.
406
23-27
1997
389006
Yamashita M.,Azakami H.,Yokoro N.,Roh J.-H.,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.
178
2941-2947
1996
389007
Hanlon S.P.,Hill T.K.,Flavell M.A.,Stringfellow J.M.,Cooper R.A.
2-phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression.
Microbiology
143
513-518
1997
389008
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.V.
Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.
Biochemistry
36
1608-1620
1997
389009
Murray J.M.,Saysell C.G.,Wilmot C.M.,Tambyrajah W.S.,Jaeger J.,Knowles P.F.,Phillips S.E.V.,McPherson M.J.
The active site base controls cofactor reactivity in Escherichia coli amine oxidase: X-ray crystallographic studies with mutational variants.
Biochemistry
38
8217-8227
1999
389010
Wilmot C.M.,Hajdu J.,McPherson M.J.,Knowles P.F.,Phillips S.E.
Visualization of dioxygen bound to copper during enzyme catalysis.
Science
286
1724-1728
1999
