Cytosine deaminase Recombinant Protein | codA recombinant protein

Recombinant Escherichia coli (strain K12) Cytosine deaminase

Cat. Num. AAA114845

• Gene Names: codA; ECK0334; JW0328
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Cytosine deaminase; N/A; Recombinant Escherichia coli (strain K12) Cytosine deaminase; Cytosine aminohydrolaseIsoguanine deaminase1; codA recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 2-427aa; Full Length of Mature Protein
• Sequence: SNNALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITENSLDAEQGLVIPPFVEPHIHLDTTQTAGQPNWNQSGTLFEGIERWAERKALLTHDDVKQRAWQTLKWQIANGIQHVRTHVDVSDATLTALKAMLEVKQEVAPWIDLQIVAFPQEGILSYPNGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKTFALAQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMGARVTASHTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQGRFDTYPKRRGITRVKEMLESGINVCFGHDDVFDPWYPLGTANMLQVLHMGLHVCQLMGYGQINDGLNLITHHSARTLNLQDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKVIASTQPAQTTVYLEQPEAIDYKR

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for codA recombinant protein

Catalyzes the hydrolytic deamination of cytosine to uracil. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis. Is also able to catalyze deamination of isoguanine, a mutagenic oxidation product of adenine in DNA, and of isocytosine. To a lesser extent, also catalyzes the conversion of 5-fluorocytosine (5FC) to 5-fluorouracil (5FU); this activity allows the formation of a cytotoxic chotherapeutic agent from a non-cytotoxic precursor.

References

Characterization of the Escherichia coli codBA operon encoding cytosine permease and cytosine deaminase.Danielsen S., Kilstrup M., Barilla K., Jochimsen B., Neuhard J.Mol. Microbiol. 6:1335-1344(1992) A first step in the development of gene therapy for colorectal carcinoma cloning, sequencing, and expression of Escherichia coli cytosine deaminase.Austin E.A., Huber B.E.Mol. Pharmacol. 43:380-387(1993) Sequence of minutes 4-25 of Escherichia coli.Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. The complete genome sequence of Escherichia coli K-12.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.Science 277:1453-1462(1997) Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.Mol. Syst. Biol. 2:E1-E5(2006) Cytosine deaminase. The roles of divalent metal ions in catalysis.Porter D.J., Austin E.A.J. Biol. Chem. 268:24005-24011(1993) Crystallization and preliminary X-ray analysis of bacterial cytosine deaminase.Ireton G.C., Black M.E., Stoddard B.L.Acta Crystallogr. D 57:1643-1645(2001) Gene-directed enzyme prodrug therapy.Zhang J., Kale V., Chen M.AAPS J. 17:102-110(2015) The structure of Escherichia coli cytosine deaminase.Ireton G.C., McDermott G., Black M.E., Stoddard B.L.J. Mol. Biol. 315:687-697(2002) Random mutagenesis and selection of Escherichia coli cytosine deaminase for cancer gene therapy.Mahan S.D., Ireton G.C., Knoeber C., Stoddard B.L., Black M.E.Protein Eng. Des. Sel. 17:625-633(2004) Bacterial cytosine deaminase mutants created by molecular engineering show improved 5-fluorocytosine-mediated cell killing in vitro and in vivo.Fuchita M., Ardiani A., Zhao L., Serve K., Stoddard B.L., Black M.E.Cancer Res. 69:4791-4799(2009) Three-dimensional structure and catalytic mechanism of cytosine deaminase.Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.Biochemistry 50:5077-5085(2011) Rescue of the orphan enzyme isoguanine deaminase.Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C., Raushel F.M.Biochemistry 50:5555-5557(2011) Crystal structure of cytosine deaminase from Escherichia coli complexed with two zinc atoms in the active site.Fedorov A.A., Fedorov E.V., Kamat S., Hitchcock D., Raushel F.M., Almo S.C.Submitted (MAR-2011) to the PDB data bank

NCBI and Uniprot Product Information

• NCBI GI #: 16128322
• NCBI GeneID: 944996
• NCBI Accession #: NP_414871.1
• NCBI GenBank Nucleotide #: NC_000913.3
• UniProt Accession #: P25524; Q2MC87
• Molecular Weight: 49.5 kDa
• NCBI Official Full Name: cytosine/isoguanine deaminase
• NCBI Official Symbol: codA
• NCBI Official Synonym Symbols: ECK0334; JW0328
• NCBI Protein Information: cytosine/isoguanine deaminase
• UniProt Protein Name: Cytosine deaminase
• UniProt Gene Name: codA
• UniProt Synonym Gene Names: CDase
• UniProt Entry Name: CODA_ECOLI