[1]
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PROTEIN SEQUENCE.
DOI=10.1016/0006-291X(84)90439-X; PubMed=6378205 [NCBI, ExPASy, EBI, Israel, Japan]
Kondo K.,
Wakabayashi S.,
Yagi T.,
Kagamiyama H.;
"The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes.";
Biochem. Biophys. Res. Commun. 122:62-67(1984).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3897210 [NCBI, ExPASy, EBI, Israel, Japan]
Kuramitsu S.,
Okuno S.,
Ogawa T.,
Ogawa H.,
Kagamiyama H.;
"Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene.";
J. Biochem. 97:1259-1262(1985).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3521591 [NCBI, ExPASy, EBI, Israel, Japan]
Fotheringham I.G.,
Dacey S.A.,
Taylor P.P.,
Smith T.J.,
Hunter M.G.,
Finlay M.E.,
Primrose S.B.,
Parker D.M.,
Edwards R.M.;
"The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes.";
Biochem. J. 234:593-604(1986).
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[4]
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PROTEIN SEQUENCE.
PubMed=3298240 [NCBI, ExPASy, EBI, Israel, Japan]
Kondo K.,
Wakabayashi S.,
Kagamiyama H.;
"Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure.";
J. Biol. Chem. 262:8648-8657(1987).
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima T.,
Aiba H.,
Baba T.,
Fujita K.,
Hayashi K.,
Honjo A.,
Ikemoto K.,
Inada T.,
Itoh T.,
Kajihara M.,
Kanai K.,
Kashimoto K.,
Kimura S.,
Kitagawa M.,
Makino K.,
Masuda S.,
Miki T.,
Mizobuchi K.,
Mori H.,
Motomura K.,
Nakamura Y.,
Nashimoto H.,
Nishio Y.,
Saito N.,
Sampei G.,
Seki Y.,
Tagami H.,
Takemoto K.,
Wada C.,
Yamamoto Y.,
Yano M.,
Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
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[6]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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 277:1453-1474(1997).
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[7]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
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:E1-E5(2006).
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[8]
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PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J.,
Robison K.,
Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
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[9]
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MUTAGENESIS OF TYR-65.
DOI=10.1021/bi00245a019; PubMed=1868057 [NCBI, ExPASy, EBI, Israel, Japan]
Inoue K.,
Kuramitsu S.,
Okamoto A.,
Hirotsu K.,
Higuchi T.,
Kagamiyama H.;
"Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes.";
Biochemistry 30:7796-7801(1991).
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[10]
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MUTAGENESIS OF HIS-133.
PubMed=2007566 [NCBI, ExPASy, EBI, Israel, Japan]
Yano T.,
Kuramitsu S.,
Tanase S.,
Morino Y.,
Hiromi K.,
Kagamiyama H.;
"The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.";
J. Biol. Chem. 266:6079-6085(1991).
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[11]
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X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-246.
DOI=10.1021/bi00446a030; PubMed=2513875 [NCBI, ExPASy, EBI, Israel, Japan]
Smith D.L.,
Almo S.C.,
Toney M.D.,
Ringe D.;
"2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.";
Biochemistry 28:8161-8167(1989).
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[12]
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X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND MUTAGENESIS OF ARG-374.
DOI=10.1021/bi00221a035; PubMed=1993208 [NCBI, ExPASy, EBI, Israel, Japan]
Danishefsky A.T.,
Onnufer J.J.,
Petsko G.A.,
Ringe D.;
"Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase.";
Biochemistry 30:1980-1985(1991).
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[13]
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X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT.
DOI=10.1074/jbc.274.4.2344; PubMed=9891001 [NCBI, ExPASy, EBI, Israel, Japan]
Oue S.,
Okamoto A.,
Yano T.,
Kagamiyama H.;
"Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues.";
J. Biol. Chem. 274:2344-2349(1999).
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