k12 Dihydrodipicolinate synthase Recombinant Protein | dapA recombinant protein

Recombinant E Coli-k12 Dihydrodipicolinate synthase

Cat. Num. AAA1265355

• Gene Names: dapA; ECK2474; JW2463
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: k12 Dihydrodipicolinate synthase; Recombinant E Coli-k12 Dihydrodipicolinate synthase; dapA recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 1-292aa; Full Length
• Sequence: MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIKEATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL
• Sequence Length: 292

• 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 dapA recombinant protein

Catalyzes the condensation of (S)-aspartate-beta-sialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).

References

Chromosomal location and nucleotide sequence of the Escherichia coli dapA gene.Richaud F., Richaud C., Ratet P., Patte J.-C.J. Bacteriol. 166:297-300(1986) Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.DNA Res. 4:91-113(1997) 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) Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.Submitted (FEB-1996) to UniProtKB Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.Link A.J., Robison K., Church G.M.Electrophoresis 18:1259-1313(1997) Protein identification with N and C-terminal sequence tags in proteome projects.Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.J. Mol. Biol. 278:599-608(1998) Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization.Laber B., Gomis-Rueth F.-X., Romao M.J., Huber R.Biochem. J. 288:691-695(1992) DNA sequence of the purC gene encoding 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide synthetase and organization of the dapA-purC region of Escherichia coli K-12.Tiedemann A.A., Demarini D.J., Parker J., Smith J.M.J. Bacteriol. 172:6035-6041(1990) A gene for a new lipoprotein in the dapA-purC interval of the Escherichia coli chromosome.Bouvier J., Pugsley A.P., Stragier P.J. Bacteriol. 173:5523-5531(1991) Escherichia coli proteome analysis using the gene-protein database.VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.Electrophoresis 18:1243-1251(1997) Dihydrodipicolinate synthase from Escherichia coli pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by L-lysine.Karsten W.E.Biochemistry 36:1730-1739(1997) Dihydrodipicolinate synthase is not inhibited by its substrate, (S) -aspartate beta-semialdehyde.Dobson R.C., Gerrard J.A., Pearce F.G.Biochem. J. 377:757-762(2004) Irreversible inhibition of dihydrodipicolinate synthase by 4-oxo-heptenedioic acid analogues.Boughton B.A., Griffin M.D., O'Donnell P.A., Dobson R.C., Perugini M.A., Gerrard J.A., Hutton C.A.Bioorg. Med. Chem. 16:9975-9983(2008) NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase.Devenish S.R., Blunt J.W., Gerrard J.A.J. Med. Chem. 53:4808-4812(2010) 1,3-Phenylene bis(ketoacid) derivatives as inhibitors of Escherichia coli dihydrodipicolinate synthase.Boughton B.A., Hor L., Gerrard J.A., Hutton C.A.Bioorg. Med. Chem. 20:2419-2426(2012) The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5-A resolution.Mirwaldt C., Korndoerfer I., Huber R.J. Mol. Biol. 246:227-239(1995) Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy.Blicking S., Renner C., Laber B., Pohlenz H.-D., Holak T.A., Huber R.Biochemistry 36:24-33(1997) The crystal structure of three site-directed mutants of Escherichia coli dihydrodipicolinate synthase further evidence for a catalytic triad.Dobson R.C.J., Valegaard K., Gerrard J.A.J. Mol. Biol. 338:329-339(2004) The crystal structures of native and (S) -lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance.Dobson R.C.J., Griffin M.D.W., Jameson G.B., Gerrard J.A.Acta Crystallogr. D 61:1116-1124(2005) Role of arginine 138 in the catalysis and regulation of Escherichia coli dihydrodipicolinate synthase.Dobson R.C.J., Devenish S.R.A., Turner L.A., Clifford V.R., Pearce F.G., Jameson G.B., Gerrard J.A.Biochemistry 44:13007-13013(2005) The co-crystallisation of (S) -lysine-bound dihydrodipicolinate synthase from E. coli indicates that domain movements are not responsible for (S) -lysine inhibition.Devenish S.R.A., Dobson R.C.J., Jameson G.B., Gerrard J.A.Submitted (AUG-2005) to the PDB data bankThe high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate.Devenish S.R., Gerrard J.A., Jameson G.B., Dobson R.C.Acta Crystallogr. F 64:1092-1095(2008) Mutating the tight-dimer interface of dihydrodipicolinate synthase disrupts the enzyme quaternary structure toward a monomeric enzyme.Pearce F.G., Dobson R.C., Weber A., Lane L.A., McCammon M.G., Squire M.A., Perugini M.A., Jameson G.B., Robinson C.V., Gerrard J.A.Biochemistry 47:12108-12117(2008) Evolution of quaternary structure in a homotetrameric enzyme.Griffin M.D., Dobson R.C., Pearce F.G., Antonio L., Whitten A.E., Liew C.K., Mackay J.P., Trewhella J., Jameson G.B., Perugini M.A., Gerrard J.A.J. Mol. Biol. 380:691-703(2008) Conserved main-chain peptide distortions a proposed role for Ile203 in catalysis by dihydrodipicolinate synthase.Dobson R.C., Griffin M.D., Devenish S.R., Pearce F.G., Hutton C.A., Gerrard J.A., Jameson G.B., Perugini M.A.Protein Sci. 17:2080-2090(2008) Specificity versus catalytic potency The role of threonine 44 in Escherichia coli dihydrodipicolinate synthase mediated catalysis.Dobson R.C., Perugini M.A., Jameson G.B., Gerrard J.A.Biochimie 91:1036-1044(2009) How essential is the 'essential' active-site lysine in dihydrodipicolinate synthase?Soares da Costa T.P., Muscroft-Taylor A.C., Dobson R.C., Devenish S.R., Jameson G.B., Gerrard J.A.Biochimie 92:837-845(2010) The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semialdehyde unambiguous resolution of the stereochemistry of the condensation product.Boughton B.A., Dobson R.C., Hutton C.A.Proteins 80:2117-2122(2012)

NCBI and Uniprot Product Information

• NCBI GI #: 16130403
• NCBI GeneID: 946952
• NCBI Accession #: NP_416973.1
• NCBI GenBank Nucleotide #: NC_000913.3
• UniProt Accession #: P0A6L2; P05640; P78223
• Molecular Weight: 35.3 kDa
• NCBI Official Full Name: dihydrodipicolinate synthase
• NCBI Official Symbol: dapA
• NCBI Official Synonym Symbols: ECK2474; JW2463
• NCBI Protein Information: dihydrodipicolinate synthase
• UniProt Protein Name: 4-hydroxy-tetrahydrodipicolinate synthase
• Protein Family: 4-hydroxy-tetrahydrodipicolinate synthase
• UniProt Gene Name: dapA
• UniProt Synonym Gene Names: HTPA synthase
• UniProt Entry Name: DAPA_ECOLI

NCBI Description

DapA levels may be influenced by GroES and GroEL. [More information is available at EcoGene: EG10205]. Lys-161 is the active-site lysine residue of DHDPS. [More information is available at EcoCyc: EG10205].

Uniprot Description

Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).