2.5.1.55: 3-deoxy-8-phosphooctulonate synthase This is an abbreviated version! For detailed information about 3-deoxy-8-phosphooctulonate synthase, go to the full flat file .
Word Map on EC 2.5.1.55
Reaction
phosphoenolpyruvate +
D-arabinose 5-phosphate +
H2O =
3-deoxy-D-manno-octulosonate 8-phosphate +
phosphate
Synonyms 2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating), 2-dehydro-3-deoxyphosphooctonate aldolase, 2-keto-3-deoxy-8-phosphooctonic acid synthetase, 2-keto-3-deoxy-8-phosphooctonic synthetase, 2-keto-3-deoxy-D-manno-octulosonate-8-phosphate synthase, 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase, 3-deoxy-D-manno-2-octulosonic acid-8-phosphate synthase, 3-deoxy-D-manno-octulosonate 8-phosphate synthase, 3-deoxy-D-manno-octulosonate 8-phosphate synthetase, 3-deoxy-D-manno-octulosonate-8-phosphate synthase, 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase, 3-deoxy-D-mannooctulosonate-8-phosphate synthetase, 3-deoxyoctulosonic 8-phosphate synthetase, 3-eoxy-D-manno-octulosonate 8-phosphate synthase, 8-phospho-2-dehydro-3-deoxy-D-octonate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating), aldolase, phospho-2-keto-3-deoxyoctonate, AtkdsA1, AtkdsA2, EC 4.1.2.16, HpKDO8PS, KDO 8-phosphate synthetase, KDO-8-P synthase, KDO-8-P synthetase, Kdo-8-phosphate synthase, KDO8-P, Kdo8P synthase, KDO8PS, KDOPS, KDPO synthetase, KdsA, KdsA1, KdsA2, metal-independent 3-deoxy-D-manno-octulosonate 8-phosphate synthase, metal-independent KDO8PS, NmeKDO8PS, Phospho-2-dehydro-3-deoxyoctonate aldolase, phospho-2-keto-3-deoxyoctonate aldolase
ECTree
Subunits
Subunits on EC 2.5.1.55 - 3-deoxy-8-phosphooctulonate synthase
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homodimer
2 * 30300, SDS-PAGE, two monomers in each asymmetric unit. The monomers adopt the (beta/alpha)8 barrel topology
monomer
1 * 30845, ESI-MS, unbound enzyme with substrate phosphoenolpyruvate or product phosphate favors the formation of monomers, phosphoenolpyruvate-bound and unbound enzyme exists as monomer
oligomer
-
the enzyme structure is a prototypical alpha/beta TIM barrel structure expected from this family of enzymes and contains a tetramer in the asymmetric unit
?
-
3 * 29736, electrospray ionization mass spectrometry
?
-
x * 29348, calculation from nucleotide sequence
?
-
x * 30000, SDS-PAGE
-
?
-
x * 29348, calculation from nucleotide sequence
-
?
-
x * 30842, electrospray mass spectrometry
dimer
in solution
dimer
-
2 * 31519, MALDI-MS
dimer
2 * 33545, sequence calculation, 2 * 33500, recombinant His-tagged enzyme, SDS-PAGE
dimer
2 * 30845, ESI-MS, predominant in unbound enzyme in complex with substrate D-arabinose 5-phosphate or product 3-deoxy-D-manno-octulosonate 8-phosphate, phosphoenolpyruvate-bound and unbound enzyme exists as dimer
tetramer
-
4 * 29300, calulated from sequence
tetramer
the enzyme is a homotetramer in which each monomer has the fold of a (beta/alpha)8 barrel
tetramer
4 * 30845, ESI-MS, phosphoenolpyruvate-bound enzyme exists as tetramer to a low extent, unbound enzyme does not exist in tetrameric state, phosphoenolpyrovate stabilizes the tetrameric structure and may bind at the same position as phosphate
tetramer
-
tetrameric quaternary structure with an active site in each monomer, by NMR study and crystal structure analysis
tetramer
-
4 * 30440 (with 2 Co2+), 4 * 30440 (with 4 Zn2+ or Cu2+), 4 * 30480 (with 4 Cd2+), tetramer formed by 2 dimers each, ESI-MS
tetramer
4 * 30000, gel-filtration chromatography
tetramer
-
the enzyme adopts a homotetrameric associations with its active site close to one of the interfaces. The conserved PAFLxR motif in KDO8PS on the short beta4alpha4 loop of the (beta/alpha)8 barrel, form part of this interface and provide key contacts with substrates
trimer
-
-
trimer
-
3 * 32000, SDS-PAGE
trimer
-
3 * 32000, SDS-PAGE
-
additional information
in the substrate-bound structure, water molecules play a key role in fixing residues in the proper configuration to achieve a compact structure
additional information
-
in the substrate-bound structure, water molecules play a key role in fixing residues in the proper configuration to achieve a compact structure
additional information
-
two-dimensional structure comparison