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K12 Dihydrodipicolinate Synthase (dapA) E Coli Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS1265355

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

$315 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Testing Data View PDF
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Certificate of Analysis (COA) View PDF
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QC Report View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Protocol View PDF

Product Overview

Online Datasheet in PDF
Product Name
k12 Dihydrodipicolinate synthase (dapA), Recombinant Protein
Full Product Name
Recombinant E Coli-k12 Dihydrodipicolinate synthase
Product Gene Name
Sequence
MFTGSIVAIV TPMDEKGNVC RASLKKLIDY HVASGTSAIV SVGTTGESAT LNHDEHADVV MMTLDLADGR IPVIAGTGAN ATAEAISLTQ RFNDSGIVGC LTVTPYYNRP SQEGLYQHFK AIAEHTDLPQ ILYNVPSRTG CDLLPETVGR LAKVKNIIGI KEATGNLTRV NQIKELVSDD FVLLSGDDAS ALDFMQLGGH GVISVTANVA ARDMAQMCKL AAEGHFAEAR VINQRLMPLH NKLFVEPNPI PVKWACKELG LVATDTLRLP MTPITDSGRE TVRAALKHAG LL
Host
E Coli
Form/Format
Liquid containing glycerol
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
35.3 kDa
Sequence Positions
1-292aa; Full Length
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
3D Structure
ModBase 3D Structure for P0A6L2
ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for dapA recombinant protein

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)

Other Notes

Small volumes of dapA recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for dapA purchase

MBS1265355 is a recombinant protein targeting dapA. Also known as Recombinant E Coli-k12 Dihydrodipicolinate synthase. Host: E Coli.

Additional Details

NCBI/Uniprot data below describe general gene information for dapA. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
GenBank Nucleotide #
NCBI Official Full Name
dihydrodipicolinate synthase
NCBI Official Symbol
dapA
NCBI Official Synonym Symbols
ECK2474; JW2463
UniProt Protein Name
4-hydroxy-tetrahydrodipicolinate synthase
UniProt Gene Name
dapA
UniProt Synonym Gene Names
HTPA synthase
UniProt Entry Name
DAPA_ECOLI
NCBI Protein Information
dihydrodipicolinate synthase

NCBI Summary for dapA

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 Comments for dapA

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

Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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