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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

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.55 3-deoxy-8-phosphooctulonate synthase

pH Range

pH Range on EC 2.5.1.55 - 3-deoxy-8-phosphooctulonate synthase

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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8 - 9.15
50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, wild type enzyme is most active between pH 6.8 and pH 8.1
4.5 - 7.5
-
pH 4.5: about 50% of maximal activity, pH 7.5: about 50% of maximal activity
5.5 - 10
-
pH 5.5: about 35% of maximal activity, pH 10.0: about 65% of maximal activity, at 50°C
6.1 - 9
-
pH 6.1: about 35% of maximal activity, pH 9.0: about 25% of maximal activity
6.5 - 9.5
-
broad peak between pH 6.5 and 9.5 showing 90% of maximal activity