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P0A6L2

- DAPA_ECOLI

UniProt

P0A6L2 - DAPA_ECOLI

Protein

4-hydroxy-tetrahydrodipicolinate synthase

Gene

dapA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (10 May 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).2 PublicationsUniRule annotation

    Catalytic activityi

    Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O.2 PublicationsUniRule annotation

    Enzyme regulationi

    Is allosterically regulated by the feedback inhibitor (S)-lysine. Is inhibited by pyruvate analogs such as 3-fluoropyruvate, 2-ketobutyrate, glyoxylate, and beta-hydroxypyruvate. Is not inhibited by its substrate, (S)-ASA.3 Publications

    Kineticsi

    kcat is 124 sec(-1).

    1. KM=0.26 mM for pyruvate2 Publications
    2. KM=0.11 mM for L-aspartate-4-semialdehyde2 Publications

    Vmax=0.58 µmol/sec/mg enzyme2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei44 – 441Part of a proton relay during catalysis
    Binding sitei45 – 451Pyruvate2 PublicationsUniRule annotation
    Sitei49 – 491L-lysine inhibitor binding; via carbonyl oxygen
    Sitei80 – 801L-lysine inhibitor binding
    Sitei84 – 841L-lysine inhibitor binding
    Sitei106 – 1061L-lysine inhibitor binding
    Sitei107 – 1071Part of a proton relay during catalysis
    Active sitei133 – 1331Proton donor/acceptor
    Active sitei161 – 1611Schiff-base intermediate with substrate
    Binding sitei203 – 2031Pyruvate; via carbonyl oxygen2 PublicationsUniRule annotation

    GO - Molecular functioni

    1. 4-hydroxy-tetrahydrodipicolinate synthase Source: EcoCyc
    2. amine-lyase activity Source: UniProtKB-HAMAP
    3. identical protein binding Source: IntAct

    GO - Biological processi

    1. diaminopimelate biosynthetic process Source: EcoliWiki
    2. lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    BioCyciEcoCyc:DIHYDRODIPICSYN-MONOMER.
    ECOL316407:JW2463-MONOMER.
    MetaCyc:DIHYDRODIPICSYN-MONOMER.
    SABIO-RKP0A6L2.
    UniPathwayiUPA00034; UER00017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxy-tetrahydrodipicolinate synthaseUniRule annotation (EC:4.3.3.7UniRule annotation)
    Short name:
    HTPA synthaseUniRule annotation
    Gene namesi
    Name:dapAUniRule annotation
    Ordered Locus Names:b2478, JW2463
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10205. dapA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441T → S: 8% of wild-type activity. 4-fold decrease in affinity for pyruvate, but nearly no change in that for (S)-ASA. 2 Publications
    Mutagenesisi44 – 441T → V: Reduced kcat by 99.9%. 2 Publications
    Mutagenesisi107 – 1071Y → F: Reduced kcat by 90%. 2 Publications
    Mutagenesisi107 – 1071Y → W: Reduced activity by 95%. Reduced affinity for both substrates. Exists as a mixture of monomer, dimer and tetramer in solution. Has significantly lower thermal stability than the wild-type enzyme. 2 Publications
    Mutagenesisi133 – 1331Y → F: Reduced kcat by 99.7%. Reduced affinity for both substrates. 1 Publication
    Mutagenesisi138 – 1381R → A or H: Strongly increased KM for L-aspartate 4-semialdehyde. No effect on KM for pyruvate. Reduced activity by 99.7%. 1 Publication
    Mutagenesisi161 – 1611K → A: 0.1% of wild-type activity. 3-fold decrease in affinity for pyruvate, and 2-fold decrease in that for (S)-ASA. 1 Publication
    Mutagenesisi161 – 1611K → R: 0.35% of wild-type activity. 3-fold decrease in affinity for pyruvate, but nearly no change in that for (S)-ASA. 1 Publication
    Mutagenesisi197 – 1971L → Y or D: 1.4 to 2.5% of wild-type activity. Decrease in affinity for pyruvate, but nearly no change in that for (S)-ASA. Exists as a dimer in solution. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2922924-hydroxy-tetrahydrodipicolinate synthasePRO_0000103110Add
    BLAST

    Proteomic databases

    PaxDbiP0A6L2.
    PRIDEiP0A6L2.

    2D gel databases

    SWISS-2DPAGEP0A6L2.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6L2.

    Interactioni

    Subunit structurei

    Homotetramer; dimer of dimers.6 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-907527,EBI-907527

    Protein-protein interaction databases

    IntActiP0A6L2. 3 interactions.
    STRINGi511145.b2478.

    Structurei

    Secondary structure

    1
    292
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi17 – 193
    Helixi21 – 3414
    Beta strandi38 – 436
    Turni44 – 474
    Helixi48 – 503
    Helixi53 – 6715
    Beta strandi73 – 764
    Helixi82 – 9110
    Turni92 – 943
    Beta strandi98 – 1036
    Helixi112 – 12312
    Beta strandi130 – 1334
    Helixi136 – 1394
    Helixi145 – 1528
    Beta strandi157 – 1604
    Helixi169 – 1746
    Beta strandi181 – 1866
    Helixi188 – 1903
    Helixi191 – 1966
    Beta strandi201 – 2055
    Helixi206 – 2083
    Helixi211 – 22212
    Helixi226 – 24217
    Beta strandi245 – 2473
    Helixi250 – 2589
    Beta strandi261 – 2633
    Helixi276 – 28813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DHPX-ray2.30A/B1-292[»]
    1S5TX-ray2.30A/B1-292[»]
    1S5VX-ray2.35A/B1-292[»]
    1S5WX-ray2.32A/B1-292[»]
    1YXCX-ray1.90A/B1-292[»]
    1YXDX-ray2.00A/B1-292[»]
    2A6LX-ray2.05A/B1-292[»]
    2A6NX-ray1.94A/B1-292[»]
    2ATSX-ray1.90A/B1-292[»]
    2OJPX-ray1.70A/B1-292[»]
    2PURX-ray1.70A/B1-292[»]
    3C0JX-ray2.40A/B1-292[»]
    3DENX-ray2.20A/B1-292[»]
    3DU0X-ray2.00A/B1-292[»]
    3I7QX-ray2.00A/B1-292[»]
    3I7RX-ray2.10A/B1-292[»]
    3I7SX-ray2.30A/B1-292[»]
    4EOUX-ray2.30A/B1-292[»]
    ProteinModelPortaliP0A6L2.
    SMRiP0A6L2. Positions 1-292.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6L2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DapA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0329.
    HOGENOMiHOG000173604.
    KOiK01714.
    OMAiMLYSGDD.
    OrthoDBiEOG6W7235.
    PhylomeDBiP0A6L2.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00418. DapA.
    InterProiIPR013785. Aldolase_TIM.
    IPR005263. DapA.
    IPR002220. DapA-like.
    IPR020625. Dihydrodipicolinate_synth_AS.
    IPR020624. Dihydrodipicolinate_synth_CS.
    [Graphical view]
    PANTHERiPTHR12128. PTHR12128. 1 hit.
    PfamiPF00701. DHDPS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001365. DHDPS. 1 hit.
    PRINTSiPR00146. DHPICSNTHASE.
    TIGRFAMsiTIGR00674. dapA. 1 hit.
    PROSITEiPS00665. DHDPS_1. 1 hit.
    PS00666. DHDPS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A6L2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFTGSIVAIV TPMDEKGNVC RASLKKLIDY HVASGTSAIV SVGTTGESAT    50
    LNHDEHADVV MMTLDLADGR IPVIAGTGAN ATAEAISLTQ RFNDSGIVGC 100
    LTVTPYYNRP SQEGLYQHFK AIAEHTDLPQ ILYNVPSRTG CDLLPETVGR 150
    LAKVKNIIGI KEATGNLTRV NQIKELVSDD FVLLSGDDAS ALDFMQLGGH 200
    GVISVTANVA ARDMAQMCKL AAEGHFAEAR VINQRLMPLH NKLFVEPNPI 250
    PVKWACKELG LVATDTLRLP MTPITDSGRE TVRAALKHAG LL 292
    Length:292
    Mass (Da):31,270
    Last modified:May 10, 2005 - v1
    Checksum:i3970543296A77C08
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071A → T in AAA23665. (PubMed:3514578)Curated
    Sequence conflicti224 – 2241G → E in AAA23665. (PubMed:3514578)Curated

    Mass spectrometryi

    Molecular mass is 31272±1 Da from positions 1 - 292. Determined by ESI. 1 Publication
    Molecular mass is 31270 Da from positions 1 - 292. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12844 Genomic DNA. Translation: AAA23665.1.
    U00096 Genomic DNA. Translation: AAC75531.1.
    AP009048 Genomic DNA. Translation: BAA16355.1.
    M33928 Genomic DNA. No translation available.
    X57402 Genomic DNA. Translation: CAA40660.1.
    PIRiE65023. SYECDP.
    RefSeqiNP_416973.1. NC_000913.3.
    YP_490706.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75531; AAC75531; b2478.
    BAA16355; BAA16355; BAA16355.
    GeneIDi12932974.
    946952.
    KEGGiecj:Y75_p2431.
    eco:b2478.
    PATRICi32120343. VBIEscCol129921_2574.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12844 Genomic DNA. Translation: AAA23665.1 .
    U00096 Genomic DNA. Translation: AAC75531.1 .
    AP009048 Genomic DNA. Translation: BAA16355.1 .
    M33928 Genomic DNA. No translation available.
    X57402 Genomic DNA. Translation: CAA40660.1 .
    PIRi E65023. SYECDP.
    RefSeqi NP_416973.1. NC_000913.3.
    YP_490706.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DHP X-ray 2.30 A/B 1-292 [» ]
    1S5T X-ray 2.30 A/B 1-292 [» ]
    1S5V X-ray 2.35 A/B 1-292 [» ]
    1S5W X-ray 2.32 A/B 1-292 [» ]
    1YXC X-ray 1.90 A/B 1-292 [» ]
    1YXD X-ray 2.00 A/B 1-292 [» ]
    2A6L X-ray 2.05 A/B 1-292 [» ]
    2A6N X-ray 1.94 A/B 1-292 [» ]
    2ATS X-ray 1.90 A/B 1-292 [» ]
    2OJP X-ray 1.70 A/B 1-292 [» ]
    2PUR X-ray 1.70 A/B 1-292 [» ]
    3C0J X-ray 2.40 A/B 1-292 [» ]
    3DEN X-ray 2.20 A/B 1-292 [» ]
    3DU0 X-ray 2.00 A/B 1-292 [» ]
    3I7Q X-ray 2.00 A/B 1-292 [» ]
    3I7R X-ray 2.10 A/B 1-292 [» ]
    3I7S X-ray 2.30 A/B 1-292 [» ]
    4EOU X-ray 2.30 A/B 1-292 [» ]
    ProteinModelPortali P0A6L2.
    SMRi P0A6L2. Positions 1-292.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0A6L2. 3 interactions.
    STRINGi 511145.b2478.

    Chemistry

    BindingDBi P0A6L2.
    ChEMBLi CHEMBL4083.

    2D gel databases

    SWISS-2DPAGE P0A6L2.

    Proteomic databases

    PaxDbi P0A6L2.
    PRIDEi P0A6L2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75531 ; AAC75531 ; b2478 .
    BAA16355 ; BAA16355 ; BAA16355 .
    GeneIDi 12932974.
    946952.
    KEGGi ecj:Y75_p2431.
    eco:b2478.
    PATRICi 32120343. VBIEscCol129921_2574.

    Organism-specific databases

    EchoBASEi EB0201.
    EcoGenei EG10205. dapA.

    Phylogenomic databases

    eggNOGi COG0329.
    HOGENOMi HOG000173604.
    KOi K01714.
    OMAi MLYSGDD.
    OrthoDBi EOG6W7235.
    PhylomeDBi P0A6L2.

    Enzyme and pathway databases

    UniPathwayi UPA00034 ; UER00017 .
    BioCyci EcoCyc:DIHYDRODIPICSYN-MONOMER.
    ECOL316407:JW2463-MONOMER.
    MetaCyc:DIHYDRODIPICSYN-MONOMER.
    SABIO-RK P0A6L2.

    Miscellaneous databases

    EvolutionaryTracei P0A6L2.
    PROi P0A6L2.

    Gene expression databases

    Genevestigatori P0A6L2.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00418. DapA.
    InterProi IPR013785. Aldolase_TIM.
    IPR005263. DapA.
    IPR002220. DapA-like.
    IPR020625. Dihydrodipicolinate_synth_AS.
    IPR020624. Dihydrodipicolinate_synth_CS.
    [Graphical view ]
    PANTHERi PTHR12128. PTHR12128. 1 hit.
    Pfami PF00701. DHDPS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001365. DHDPS. 1 hit.
    PRINTSi PR00146. DHPICSNTHASE.
    TIGRFAMsi TIGR00674. dapA. 1 hit.
    PROSITEi PS00665. DHDPS_1. 1 hit.
    PS00666. DHDPS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
      Submitted (FEB-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-11.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    7. Cited for: PROTEIN SEQUENCE OF 1-4.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 156-167, ACTIVE SITE.
    9. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 288-292.
      Strain: K12.
    10. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 288-292.
      Strain: K12.
    11. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    12. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    13. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, KINETIC PARAMETERS, MASS SPECTROMETRY.
    14. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: SYNTHETIC INHIBITORS.
    15. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF HTPA AS REACTION PRODUCT, SUBSTRATE SPECIFICITY.
    16. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: SYNTHETIC INHIBITORS.
    17. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    18. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF HTPA AS REACTION PRODUCT, CATALYTIC MECHANISM.
    19. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF MUTANTS VAL-44; PHE-107 AND PHE-133, KINETIC PARAMETERS, MUTAGENESIS OF THR-44; TYR-107 AND TYR-133, REACTION MECHANISM.
    20. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH ALLOSTERIC INHIBITOR (S)-LYSINE, SUBUNIT.
    21. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF MUTANTS ALA-138 AND HIS-138, MUTAGENESIS OF ARG-138.
    22. "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 bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH LYSINE INHIBITOR.
    23. "The 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
    24. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT TRP-107, SUBUNIT, MUTAGENESIS OF TYR-107.
    25. Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT TYR-197, SUBUNIT, MUTAGENESIS OF LEU-197.
    26. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), ENZYME REGULATION, MASS SPECTROMETRY.
    27. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT SER-44, MUTAGENESIS OF THR-44, ACTIVE SITES, REACTION MECHANISM.
    28. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANTS ALA-161 AND ARG-161 OF NATIVE PROTEIN AND IN COMPLEX WITH PYRUVATE, MUTAGENESIS OF LYS-161.
    29. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH PYRUVATE AND SUBSTRATE ANALOG INHIBITOR.

    Entry informationi

    Entry nameiDAPA_ECOLI
    AccessioniPrimary (citable) accession number: P0A6L2
    Secondary accession number(s): P05640, P78223
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB (PubMed:8993314, PubMed:20503968).2 Publications

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3