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P0A6L2

- DAPA_ECOLI

UniProt

P0A6L2 - DAPA_ECOLI

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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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 85Combined sources
Beta strandi17 – 193Combined sources
Helixi21 – 3414Combined sources
Beta strandi38 – 436Combined sources
Turni44 – 474Combined sources
Helixi48 – 503Combined sources
Helixi53 – 6715Combined sources
Beta strandi73 – 764Combined sources
Helixi82 – 9110Combined sources
Turni92 – 943Combined sources
Beta strandi98 – 1036Combined sources
Helixi112 – 12312Combined sources
Beta strandi130 – 1334Combined sources
Helixi136 – 1394Combined sources
Helixi145 – 1528Combined sources
Beta strandi157 – 1604Combined sources
Helixi169 – 1746Combined sources
Beta strandi181 – 1866Combined sources
Helixi188 – 1903Combined sources
Helixi191 – 1966Combined sources
Beta strandi201 – 2055Combined sources
Helixi206 – 2083Combined sources
Helixi211 – 22212Combined sources
Helixi226 – 24217Combined sources
Beta strandi245 – 2473Combined sources
Helixi250 – 2589Combined sources
Beta strandi261 – 2633Combined sources
Helixi276 – 28813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP0A6L2.
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

        10         20         30         40         50
MFTGSIVAIV TPMDEKGNVC RASLKKLIDY HVASGTSAIV SVGTTGESAT
60 70 80 90 100
LNHDEHADVV MMTLDLADGR IPVIAGTGAN ATAEAISLTQ RFNDSGIVGC
110 120 130 140 150
LTVTPYYNRP SQEGLYQHFK AIAEHTDLPQ ILYNVPSRTG CDLLPETVGR
160 170 180 190 200
LAKVKNIIGI KEATGNLTRV NQIKELVSDD FVLLSGDDAS ALDFMQLGGH
210 220 230 240 250
GVISVTANVA ARDMAQMCKL AAEGHFAEAR VINQRLMPLH NKLFVEPNPI
260 270 280 290
PVKWACKELG LVATDTLRLP MTPITDSGRE TVRAALKHAG LL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P0A6L2.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 95 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