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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

Engineering

Engineering on EC 2.5.1.55 - 3-deoxy-8-phosphooctulonate synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A56P/N57DELTA
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
C21N
-
complete loss of activity
D243A
-
mutation of the absolutely conserved 243AspGlyPro245 motif, complete loss of activity
D243Q
-
mutation of the absolutely conserved 243AspGlyPro245 motif, active enzyme with altered metal-dependency
K55A
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
N57A
-
mutation in the absolutely conserved KANRS motif. About 2% of wild-type activity
N57DELTA
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
P245A
-
mutation of the absolutely conserved 243AspGlyPro245 motif, active enzyme with altered metal-dependency
C11N
mutant is not capable of binding metal and lacks the structural asymmetry among subunits with regard to substrate binding and conformation of the L7 loop, shows decreased thermal stability
C11N/S235P/Q237A
mutant is not capable of binding metal and lacks the structural asymmetry among subunits with regard to substrate binding and conformation of the L7 loop, shows decreased thermal stability
H185G
mutation decreases the affinity of the enzyme to bind Fe2+, but not Zn2+. Maximal activity, about 8-10% of the wild-type activity is obtained when the native metal is replaced with Cd2+
P10M/C11N
mutant is not capable of binding metal and lacks the structural asymmetry among subunits with regard to substrate binding and conformation of the L7 loop, shows decreased thermal stability
P10M/C11N/S235P/Q237A
mutant is not capable of binding metal and lacks the structural asymmetry among subunits with regard to substrate binding and conformation of the L7 loop, shows decreased thermal stability
R106G
the closure of the L7 loop is impaired. The mutant enzyme shows a smaller KM-value for phosphoenolpyruvate, larger Ki-value and KM-value for D-arabinose 5-phosphate and smaller Ki-values for phosphate and 2-dehydro-3-deoxy-D-octonate 8-phosphate compared ti wild-type enzyme
C11A
-
mutant enzyme retains less than 1% of the wild-type activity and is incapable of metal binding. Activity is not stimulated by Mn2+, Co2+ and Zn2+. Cd2+ stimulates 2fold at a concentration above 1 mM
C11N
enzyme retains 10% of the wild-type activity in absence of metal ions. Addition of divalent metal ions does not affect the catalytic activity of the mutant enzyme and the catalytic efficiency, i.e. the ratio of turnover number to Km-value, is reduced only 12fold, the mutant enzyme has become metal-independent
N26C
activity of the wild-type enzyme is independent of metal ions, the activity of mutant enzyme is decreased by EDTA and increased by Mn2+ and Cd2+
H204A
site-directed mutagenesis, crystal structure analysis
A56P/N57DELTA
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
F114A
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
F114R
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type, structure analysis
F114R/R117A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type, structure analysis
F114R/R117Q
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
F114R/R117Q/F139G
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
F139G
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
K57A
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
N57D
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
N59DELTA
-
mutation in the absolutely conserved KANRS motif. Less than 0.1% of wild-type activity
R117K
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
R117Q
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
P145S
-
natural mutation in the temperature-sensitive strain AG701i50 leads to an increase in Km-value for both substrates, D-arabinose 5-phosphate and phosphoenolpyruvate, this mutant enzyme also has an altered oligomeric state. Reduced activity, about 35% of the wild-type, between 15 and 30°C. Above 30°C the activity of the mutant enzyme decreases dramatically
additional information