Sequence of OXDA_PIG
EC Number:1.4.3.3
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a D-amino acid + H2O + O2 = a 2-oxo carboxylate + NH3 + H2O2
Other sequences found for EC No. 1.4.3.3
General information:
Sequence
0 MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DVKVYADRFT PFTTTDVAAG LWQPYTSEPS
60 NPQEANWNQQ TFNYLLSHIG SPNAANMGLT PVSGYNLFRE AVPDPYWKDM VLGFRKLTPR
120 ELDMFPDYRY GWFNTSLILE GRKYLQWLTE RLTERGVKFF LRKVESFEEV ARGGADVIIN
180 CTGVWAGVLQ PDPLLQPGRG QIIKVDAPWL KNFIITHDLE RGIYNSPYII PGLQAVTLGG
240 TFQVGNWNEI NNIQDHNTIW EGCCRLEPTL KDAKIVGEYT GFRPVRPQVR LEREQLRFGS
300 SNTEVIHNYG HGGYGLTIHW GCALEVAKLF GKVLEERNLL TMPPSHL
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
70724
Ronchi S.,Minchiotti L.,Galliano M.,Curti B.,Swenson R.P.,Williams C.H. Jr.,Massey V.
The primary structure of D-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence.
J. Biol. Chem.
257
8824-8834
1982
70725
Fukui K.,Watanabe F.,Shibata T.,Miyake Y.
Molecular cloning and sequence analysis of cDNAs encoding porcine kidney D-amino acid oxidase.
Biochemistry
26
3612-3618
1987
70726
Jacobs P.,Brockly F.,Massaer M.,Loriau R.,Guillaume J.P.,Ciccarelli E.,Heinderyckx M.,Cravador A.,Biemans R.,van Elsen A.,Herzog A.,Bollen A.
Porcine D-amino acid oxidase: determination of the mRNA nucleotide sequence by the characterization of genomic and cDNA clones.
Gene
59
55-61
1987
70727
Nicholson B.H.,Batra S.P.
Structural interpretation of the binding of 9-azidoacridine to D-amino acid oxidase.
Biochem. J.
255
907-912
1988
70728
Watanabe F.,Fukui K.,Momoi K.,Miyake Y.
Expression of normal and abnormal porcine kidney D-amino acid oxidase in Escherichia coli: purification and characterization of the enzymes.
Biochem. Biophys. Res. Commun.
165
1422-1427
1989
70729
Swenson R.P.,Williams C.H. Jr.,Massey V.
Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene.
J. Biol. Chem.
257
1937-1944
1982
70730
Swenson R.P.,Williams C.H. Jr.,Massey V.
Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride.
J. Biol. Chem.
258
497-502
1983
70731
Watanabe F.,Fukui K.,Momoi K.,Miyake Y.
Effect of site-specific mutagenesis of tyrosine-55, methionine-110 and histidine-217 in porcine kidney D-amino acid oxidase on its catalytic function.
FEBS Lett.
238
269-272
1988
70732
Miyano M.,Fukui K.,Watanabe F.,Takahashi S.,Tada M.,Kanashiro M.,Miyake Y.
Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization.
J. Biochem.
109
171-177
1991
70733
Mizutani H.,Miyahara I.,Hirotsu K.,Nishima Y.,Shiga K.,Setoyama C.,Miura R.
Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0-A resolution.
J. Biochem.
120
14-17
1996
70734
Mattevi A.,Vanoni M.A.,Todone F.,Rizzi M.,Teplyakov A.,Coda A.,Bolognesi M.,Curti B.
Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2.
Proc. Natl. Acad. Sci. U.S.A.
93
7496-7501
1996
70735
Todone F.,Vanoni M.A.,Mozzarelli A.,Bolognesi M.,Coda A.,Curti B.,Mattevi A.
Active site plasticity in D-amino acid oxidase: a crystallographic analysis.
Biochemistry
36
5853-5860
1997
