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

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
2.5.1.55
-
RECOMMENDED NAME
GeneOntology No.
3-deoxy-8-phosphooctulonate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
stereochemistry
-
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
reaction pathway involves an acyclic bisphosphate intermediate
-
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
mechanism
-
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
steady-state kinetic mechanism, where phosphoenolpyruvate binding precedes that of D-arabinose-5-phosphate, followed by the ordered release of phosphate and 3-deoxy-D-manno-2-octulosonate 8-phosphate
-
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
bisphosphate intermediate formed during the initial step of synthesis may have the pyranose structure with the anomeric phosphate located in the beta-configuration; mechanism
-
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
the synthesis of 2-dehydro-3-deoxy-D-octonate 8-phosphate proceeds through the formation of a linear rather than a cyclic intermediate
-
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
quantum mechanical/molecular mechanical simulations of both the enzymatic and non-enzymatic synthesis of 2-dehydro-3-deoxy-D-octonate 8-phosphate reveal the mechanism underlying the switch between metal and non-metal dependent catalysis. The conversion is possible because the metal is not involved in an activation process, but primarily contributes to orienting properly the reactants to lower the activation energy, an action easily mimicked by amino acid side-chains
-
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
condensation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
CMP-KDO biosynthesis I
-
CMP-KDO biosynthesis II (from D-arabinose 5-phosphate)
-
Lipopolysaccharide biosynthesis
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:D-arabinose-5-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
-
-
-
3-deoxy-D-manno-2-octulosonate-8-phosphate synthase
-
-
3-deoxy-D-manno-2-octulosonate-8-phosphate synthase
-
-
3-deoxy-D-manno-2-octulosonate-8-phosphate synthases
Q8GLK7
-
3-deoxy-D-manno-2-octulosonate-8-phosphate synthases
-
-
3-deoxy-D-manno-2-octulosonic acid-8-phosphate synthase
-
-
3-deoxy-D-manno-octulosonate 8-phosphate synthase
O66496
-
3-deoxy-D-manno-octulosonate 8-phosphate synthase
-
-
3-deoxy-D-manno-octulosonate 8-phosphate synthase
-
-
3-deoxy-D-manno-octulosonate 8-phosphate synthase
Q9JZ55
-
3-deoxy-D-manno-octulosonate 8-phosphate synthetase
-
-
-
-
3-deoxy-D-manno-octulosonate-8-phosphate synthase
-
-
-
-
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
-
-
-
-
8-phospho-2-dehydro-3-deoxy-D-octonate D-arabinose-5-phosphate-lyase (pyruvate-phosporylating)
-
-
-
-
aldolase, phospho-2-keto-3-deoxyoctonate
-
-
-
-
AtkdsA1
Q9AV97
-
AtkdsA2
-
-
AtkdsA2
Arabidopsis sp. AtkdsA2
-
-
-
EC 4.1.2.16
-
-
formerly
-
EC 4.1.2.16
O66496
formerly
EC 4.1.2.16
Q9AV97
formerly
KDO-8-P synthase
-
-
-
-
KDO-8-P synthase
Q9AV97
-
KDO-8-P synthetase
-
-
-
-
KDO8-P
-
-
-
-
Kdo8P synthase
-
-
-
-
Kdo8P synthase
-
-
Kdo8P synthase
O66496
-
Kdo8P synthase
-
-
Kdo8P synthase
-
-
Kdo8P synthase
-
-
Kdo8P synthase
Q9JZ55
-
KDO8P synthases
Q8GLK7
-
KDO8P synthases
-
-
KDO8PS
-
-
-
-
KDO8PS
O66496
-
KDOPS
-
-
-
-
KDPO synthetase
-
-
-
-
KdsA
-
-
-
-
metal-independent 3-deoxy-D-manno-octulosonate 8-phosphate synthase
Q9JZ55
-
metal-independent KDO8PS
Q9JZ55
-
Phospho-2-dehydro-3-deoxyoctonate aldolase
-
-
-
-
phospho-2-keto-3-deoxyoctonate aldolase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9026-96-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
AtkdsA2
-
-
Manually annotated by BRENDA team
Arabidopsis sp. AtkdsA2
AtkdsA2
-
-
Manually annotated by BRENDA team
AtkdsA1
SwissProt
Manually annotated by BRENDA team
var. italica
-
-
Manually annotated by BRENDA team
strain 6BC
-
-
Manually annotated by BRENDA team
Chlamydia psittaci 6BC
strain 6BC
-
-
Manually annotated by BRENDA team
overproducing strain DH5alpha (pJU1)
-
-
Manually annotated by BRENDA team
Gram-negative bacteria
-
-
-
Manually annotated by BRENDA team
no activity in Malus sp.
-
-
-
Manually annotated by BRENDA team
parent strain PR122, and mutant strain PR32, a temperature-sensitive lethal mutant that is conditionally defective in 3-deoxy-D-manno-octulosonate-8-phosphate synthesis
-
-
Manually annotated by BRENDA team
wild-type strain AG701 and temperature-sensitive strain AG701i50
-
-
Manually annotated by BRENDA team
-
Q9ARD1
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
catalyzes the formation of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P), a key precursor in the biosynthesis of the endotoxin of Gram-negative bacteria
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate
? + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate
? + phosphate
show the reaction diagram
-
2-deoxy-D-ribose 5-phosphate is a poor substrate
-
-
?
phosphoenolpyruvate + 2-deoxyribose 5-phosphate
?
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
P0A715
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-, Q7XZC8
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Q9ARD1, -
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-, Q9ZN55
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Gram-negative bacteria
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
O66496
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
O68662
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Q9Z7I4
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Q46225
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
P0CD74
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
P45251
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Q9XB02
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Q9XAZ3
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
P95514
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Q9ZFK4
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Q9ZE84
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Q9AV97
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Q8GLK7
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
specific for D-arabinose 5-phosphate
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
His185 is necessary for the correct binding of phosphoenolpyruvate and of a catalytic water molecule
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
irreversible reaction
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
irreversible reaction
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
absolute specificity for phosphoenolpyruvate and D-arabinose-5-phosphate
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Chlamydia psittaci 6BC
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-, Q9JZ55
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
key enzyme in the lipopolysaccharide biosynthesis of gram-negative bacteria
-
-
-
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
P0A715
2-dehydro-3-deoxy-D-octonate 8-phosphate is the phosphorylated precursor of 3-deoxy-D-manno-octulosonate, an essential sugar of the liposaccharide of gram-negative bacteria
-
-
-
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Gram-negative bacteria
-
second step in the biosynthesis of 3-deoxy-D-manno-2-octulosonic acid
-
-
-
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
O66496
the enzyme catalyzes the first commited step in the production of 2-dehydro-3-deoxy-D-octonate, an integral part of the inner core region of the lipopolysaccharide layer in Gram-negative bacteria
-
-
-
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor
-
-
-
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
show the reaction diagram
-
the enzyme does not catalyze the condensation of D-erythrose 4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-ribo-heptulosonate 7-phosphate
-
-
-
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
show the reaction diagram
-
the enzyme does not catalyze the condensation of D-erythrose 4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-ribo-heptulosonate 7-phosphate
-
-
-
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
show the reaction diagram
-
24% of the activity with D-arabinose 5-phosphate
-
-
-
phosphoenolpyruvate + L-xylose 5-phosphate + H2O
?
show the reaction diagram
-, Q9JZ55
-
-
-
?
phosphoenolpyruvate + ribose 5-phosphate
?
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + ribose 5-phosphate
?
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + ribose 5-phosphate
?
show the reaction diagram
-
7% of the activity with D-arabinose 5-phosphate
-
-
-
additional information
?
-
-
in presence of D-erythrose 4-phosphate or D-ribose 5-phosphate the enzyme catalyzes the rapid consumption of approximately 1 mol of phosphoenolpyruvate per active site, after which consumption of phosphoenolpyruvate slows to a negligible but measurable rate
-
-
-
additional information
?
-
-, Q9JZ55
D-ribose 5-phosphate, D-lyxose 5-phosphate, and D-xylose 5-phosphate with altered configuration at C2, C3 or both C2 and C3 relative to D-arabinose 5-phosphate are no substrates for KDO8P synthase
-
-
-
additional information
?
-
-
D-glucose 6-phosphate and D-erythrose 4-phosphate are no substrates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
key enzyme in the lipopolysaccharide biosynthesis of gram-negative bacteria
-
-
-
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
P0A715
2-dehydro-3-deoxy-D-octonate 8-phosphate is the phosphorylated precursor of 3-deoxy-D-manno-octulosonate, an essential sugar of the liposaccharide of gram-negative bacteria
-
-
-
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
Gram-negative bacteria
-
second step in the biosynthesis of 3-deoxy-D-manno-2-octulosonic acid
-
-
-
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
O66496
the enzyme catalyzes the first commited step in the production of 2-dehydro-3-deoxy-D-octonate, an integral part of the inner core region of the lipopolysaccharide layer in Gram-negative bacteria
-
-
-
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
1 mM, 5-10% stimulation
Ba2+
-
no activation of wild type enzyme and metal-dependent mutants, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Ca2+
-
no activation of wild type enzyme and metal-dependent mutants, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Cd2+
-
in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost
Cd2+
-
the Zn2+ in the enzyme can be quantitatively replaced by Cd2+ which increases the observed turnover number and decreases the apparent Km-value for D-arabinose-5-phosphate by 6.5fold
Cd2+
-
the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+
Cd2+
-
maximal activation below 0.1 mM
Cd2+
-
stimulates sild-type enzyme above 0.4 mM, stimulation of mutant enzyme C11A above 1 mM
Cd2+
Q8GLK7
increase in steady-state rate of wild-type enzyme, Km: 0.0006 mM
Cd2+
-
0.05 mM
Cd2+
-
second in enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
Cd2+
-
activation of metal-dependent mutants, inhibition of wild type and metal-independent mutants, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Cd2+
-
4 Cd2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer, Cd2+ reconstituted enzyme is less stable than that of Zn2+, Co2+ and Cu2+ enzymes
Cd2+
-
presence of Cd2+ restores activity to metal-free enzyme, Cd2+ significantly enhances the stability of the enzyme and raises the Tm by 14C
Co2+
-
stimulates
Co2+
-
stimulates wild-type enzyme above 0.4 mM, no stimulation of mutant enzyme C11A
Co2+
-
no activation of wild type enzyme, adverse effect on mutant N23C, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Co2+
-
monomer and dimer are each bound with 1 metal ion, tetramer with 2
Co2+
-
presence of Co2+ restores activity to metal-free enzyme
Cu2+
-
inhibits at high concentrations, stimulates below 0.001 mM
Cu2+
-
maximal activation below 0.1 mM
Cu2+
-
third in enzyme activity, octahedral or distorted tetrahedral delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization, product is bound in its linear conformation in the crystal structure of the enzyme with Cu2+, greenish color of enzyme, new absorption peak at 380 nm instead of 505 nm
Cu2+
-
no activation of mutant enzymes containing the N23C substitution, slight reduction of wild type enzyme activity, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Cu2+
-
4 Cu2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer
Fe2+
-
wild-type enzyme contains Zn2+ and Fe2+ with the ratio Zn2+/Fe2+ ranging from 1 to 2 in different preparations. Mutation H185G decreases the ability 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+
Fe2+
-
contains 0.2-0.3 equivalents of iron per enzyme subunit. FeSO4 stimulates
Fe2+
-
unsubstituted enzyme with lowest enzyme activity
Fe2+
-
no activation of wild type enzyme and metal-independent mutants, activation of N23C/D247E, N23C/C246S/D247E, inhibitory for N23C, N23C/C246S/P249A, N23C/C246S/D247E/P249A, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Fe3+
-
1 mM, 5-10% stimulation
Iron
-
enzyme contains 0.19 mol of iron per mol of subunit
Iron
Q8GLK7
wild-type enzyme contains 0.19 mol of iron per mol of enzyme, mutant enzyme c11N contains 0.22 mol of iron per mol of enzyme
Li+
-
1 mM, 5-10% stimulation
Magnesium
-
wild-type enzyme contains 0.05 mol of magnesium per mol of enzyme, mutant enzyme N26C contains 0.4 mol of magnesium per mol of enzyme
Mg2+
-
1 mM, 5-10% stimulation
Mg2+
-
no activation of wild type enzyme and metal-dependent mutants, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Mn2+
-
1 mM, 5-10% stimulation
Mn2+
-
stimulates wild-type enzyme above 0.4 mM, no stimulation of mutant enzyme C11A
Mn2+
Q8GLK7
200fold increase in steady-state rate of wild-type enzyme, Km: 0.01 mM. Addition of Mn2+ up to 2 mM does not stimulate the reaction rate of C11N mutant
Mn2+
-
no activation of wild type enzyme, activation of metal-dependent mutants, 15% reduced activity above 200 microM for mutant N23C/D247E/P249A, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Ni2+
-
no activation of wild type enzyme and metal-dependent mutants, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Sr2+
-
no activation of wild type enzyme and metal-dependent mutants, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Zinc
-
enzyme contains 0.26 mol of zinc per mol of subunit
Zinc
Q8GLK7
wild-type enzyme contains 0.26 mol per mol of enzyme, mutant enzyme c11N contains 0.02 mol of zinc per mol of enzyme.
Zinc
-
wild-type enzyme contains 0.05 mol of zinc per mol of enzyme, mutant enzyme N26C contains 0.2 mol of zinc per mol of enzyme
Zn2+
-
the enzyme contains one mol of Zn per monomer, apoenzyme is catalytically inactive
Zn2+
-
wild-type enzyme contains Zn2+ and Fe2+ with the ratio Zn2+/Fe2+ ranging from 1 to 2 in different preparations
Zn2+
-
enzyme contains approximately 0.4 equivalents of zinc per enzyme subunit. Maximal activation below 0.1 mM Zn2+
Zn2+
-
dependent on
Zn2+
-
highest enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
Zn2+
-
no activation of wild type enzyme, inhibitory for all cloned enzymes, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Zn2+
-
4 Zn2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer
Mn2+
-
presence of Mn2+ restores activity to metal-free enzyme
additional information
-
no metal requirement
additional information
-
no stimulation by divalent cations
additional information
-
no metal requirement
additional information
-
non-metallo enzyme, no metal requirement
additional information
-
the type of metal bound in the active site affects the behavior of the enzyme in vivo and the rate of product release in the crystal environment
additional information
-
the metal chelator EDTA has no effect on the activity of the metal-independent wild type enzyme and on the metal-independent mutants C246S, D247E, D247E/P249A or P249A
additional information
-
divalent metal ions play an important role in the quaternary structure of the protein
additional information
-
divalent metal ion required, with Mn2+, Co2+ and Cd2+ in decreasing order being able to restore activity to metal-free enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(Z,E)-D-Glucophosphoenolpyruvate
Gram-negative bacteria
-
and its carboxylic ester derivatives
1,10-phenanthroline
Q46225
-
1,10-phenanthroline
-, Q9ZN55
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
IC50: 0.0293 mM
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
Q8GLK7
inhibits wild-type enzyme, no inhibition of mutant enzyme C11N
1-carboxyheptane-1,7-diyl bis(phosphate)
-
-
2,6-Anhydro-3-deoxy-2beta-phosphonylmethyl-8-phosphate-D-glycero-D-talo-octonate
-
most potent inhibitor
2,6-pyridine dicarboxylic acid
-
IC50: 0.0422
2-dehydro-3-deoxy-D-octonate 8-phosphate
-
mutant enzyme R106G is more severely inhibited than wild-type enzyme
2-Deoxy-2-fluoro-D-arabinoate-5-phosphate
-
-
Bromopyruvate
-
phosphoenolpyruvate, but not arabinose-5-phosphate protects
Cd2+
-
inhibition of metal-independent wild type and mutant enzymes D247E, P249A at 2 microM and above, inhibition of mutant 247E/P249A at 8 microM and above
Co2+
-
1 mM, 22% inhibition
Cu2+
-
1 mM, 80% inhibition
Cu2+
-
activity is enhanced below 0.001 mM, inhibitory at higher concentrations
Cu2+
-
slight reduction of wild type enzyme activity
D-arabinose 5-phosphate
-
mutant enzyme R106G is less severely inhibited than wild-type enzyme
D-ribose 5-phosphate
-
weak, competitive
D-ribose 5-phosphate
-
-
dipicolinic acid
Q46225
-
EDTA
-
IC50: 0.212 mM
EDTA
-
no inhibition
EDTA
-
reactivation by divalent metal ions
EDTA
Q8GLK7
inhibits wild-type enzyme, no inhibition of mutant enzyme C11N
Fe2+
-
1 mM, 30% inhibition
-
Fe2+
-
inhibitory for N23C, N23C/C246S/P249A, N23C/C246S/D247E/P249A
-
Hg2+
-
reversed by dithiothreitol
Mn2+
-
1 mM, 40% inhibition
Mn2+
-
15% reduced activity above 200 microM for mutant N23C/D247E/P249A
phosphate
-
mutant enzyme R106G is more severely inhibited than wild-type enzyme
Zn2+
-
1 mM, 34% inhibition
Zn2+
-
mild inhibitor at higher concentrations
Zn2+
-
inhibitory for all cloned enzymes
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
1 mM, 40% stimulation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.23
-
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.432
-
2-deoxy-D-ribose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
1.5
-
2-deoxy-D-ribose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
5
-
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.05
-
2-deoxyribose 5-phosphate
-
pH 7.6, 37C
0.0005
-
D-arabinose 5-phosphate
-
same enzyme preparation as following, substitution with 50 microM Zn2+, 100 mM Tris-acetate, pH 7.5, 40C
0.00123
-
D-arabinose 5-phosphate
-
recombinant enzyme produced in Escherichia coli, native Zn2+ and Fe2+ not substituted, 100 mM Tris-acetate, pH 7.5, 40C
0.00156
-
D-arabinose 5-phosphate
-
same enzyme preparation as following, substitution with 5 microM Cu2+, 100 mM Tris-acetate, pH 7.5, 40C
0.002
-
D-arabinose 5-phosphate
-
same enzyme preparation as following, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40C
0.00227
-
D-arabinose 5-phosphate
-
independently prepared enzyme, substitution with 50 microM Cd2+, pH 5.0, 40C
0.0025
-
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.00318
-
D-arabinose 5-phosphate
-
independently prepared enzyme, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40C
0.0038
-
D-arabinose 5-phosphate
-
37C
0.0044
-
D-arabinose 5-phosphate
-
pH 7.4, 25C, wild-type enzyme
0.0057
-
D-arabinose 5-phosphate
-
wild type, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.00593
-
D-arabinose 5-phosphate
-
pH 6.5, 25C, Cd2+-enzyme
0.00773
-
D-arabinose 5-phosphate
-
pH 6.5, 25C
0.0079
-
D-arabinose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.008
-
D-arabinose 5-phosphate
-
pH 7.5, 60C
0.0085
-
D-arabinose 5-phosphate
-
pH 7.4, 37C
0.0093
-
D-arabinose 5-phosphate
-
pH 7.4, 37C, wild-type enzyme
0.012
-
D-arabinose 5-phosphate
-
at 30C
0.012
-
D-arabinose 5-phosphate
-
N23C mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O; P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.012
-
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.013
-
D-arabinose 5-phosphate
-
N23C/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.014
-
D-arabinose 5-phosphate
-
pH 7.4, 25C, mutant enzyme P145S
0.015
-
D-arabinose 5-phosphate
-
pH 7.5, 70C
0.019
-
D-arabinose 5-phosphate
-
pH 7.6, 37C
0.01926
-
D-arabinose 5-phosphate
-
same enzyme preparation as before, substitution with 5 microM Cu2+, pH 5.0, 40C
0.02
-
D-arabinose 5-phosphate
-
pH 7.3, 37C
0.02
-
D-arabinose 5-phosphate
-
-
0.02
-
D-arabinose 5-phosphate
-
pH 7.5, 37C, wild-type enzyme
0.021
-
D-arabinose 5-phosphate
-
wild-type, pH 7.2, 37C
0.022
-
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.024
-
D-arabinose 5-phosphate
-
mutant P245A, pH 7.2, 37C
0.026
-
D-arabinose 5-phosphate
-
pH 7.3, 37C
0.027
-
D-arabinose 5-phosphate
-
pH 7.5, 80C
0.0385
-
D-arabinose 5-phosphate
-
pH 6.5, 25C, Zn2+-enzyme
0.043
-
D-arabinose 5-phosphate
-
mutant N59DELTA, pH 7.5, temperature not specified in the publication
0.06
-
D-arabinose 5-phosphate
-
D247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA; N23C mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.067
-
D-arabinose 5-phosphate
Q8GLK7
pH 7.5, 60C, wild-type Mn2+-enzyme
0.07
-
D-arabinose 5-phosphate
-
60C, pH 7.0, 0.48 mM Cd2+
0.07
-
D-arabinose 5-phosphate
-
pH 7.5, 37C, Mn2+ mutant enzyme N26C
0.074
-
D-arabinose 5-phosphate
-
pH 7.5, 90C
0.074
-
D-arabinose 5-phosphate
-
D247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.075
-
D-arabinose 5-phosphate
-
pH 7.5, 37C, mutant enzyme N26C, EDTA-treated
0.081
-
D-arabinose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
0.097
-
D-arabinose 5-phosphate
-
N23C/C246S mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.107
-
D-arabinose 5-phosphate
-
N23C/C247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.109
-
D-arabinose 5-phosphate
-
N23C/P249A mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.11
-
D-arabinose 5-phosphate
-
pH 7.5, 37C, Cd2+ mutant enzyme N26C
0.14
-
D-arabinose 5-phosphate
Q8GLK7
pH 7.5, 60C, mutant enzyme C11N, EDTA-treated
0.14
-
D-arabinose 5-phosphate
-
N23C/C247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.19
-
D-arabinose 5-phosphate
-
N23C/C246S/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.2
-
D-arabinose 5-phosphate
-
28C, parent strain PR122
0.213
-
D-arabinose 5-phosphate
-
C246S mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.22
-
D-arabinose 5-phosphate
-
37C, parent strain PR122
0.23
-
D-arabinose 5-phosphate
-
37C, mutant strain PR32
0.24
-
D-arabinose 5-phosphate
-
N23C/C247E mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.28
-
D-arabinose 5-phosphate
-
pH 7.4, 37C, mutant enzyme P145S
0.33
-
D-arabinose 5-phosphate
-
N23C/C247E/P249A mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.45
-
D-arabinose 5-phosphate
-
42C, mutant strain PR32
0.498
-
D-arabinose 5-phosphate
-
N23C/C246S/D247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.503
-
D-arabinose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.54
-
D-arabinose 5-phosphate
-
N23C/C246S/D247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.83
-
D-arabinose 5-phosphate
-
42C, parent strain PR122
1.04
-
D-arabinose 5-phosphate
-
N23C/C246S mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
1.1
-
D-arabinose 5-phosphate
-
mutant N59DELTA, pH 7.5, temperature not specified in the publication
2.63
-
D-arabinose 5-phosphate
-
mutant D243E, pH 7.2, 37C
6.6e-06
-
phosphoenolpyruvate
-
same enzyme preparation as before, substitution with 5 microM Cu2+, pH 5.0, 40C
4e-05
-
phosphoenolpyruvate
-
independently prepared enzyme, substitution with 50 microM Cd2+, pH 5.0, 40C
0.00014
-
phosphoenolpyruvate
-
same enzyme preparation as following, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40C
0.00015
-
phosphoenolpyruvate
-
same enzyme preparation as following, substitution with 5 microM Cu2+, 100 mM Tris-acetate, pH 7.5, 40C
0.00016
-
phosphoenolpyruvate
-
independently prepared enzyme, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40C; recombinant enzyme produced in Escherichia coli, native Zn2+ and Fe2+ not substituted, 100 mM Tris-acetate, pH 7.5, 40C
0.00028
-
phosphoenolpyruvate
-
same enzyme preparation as following, substitution with 50 microM Zn2+, 100 mM Tris-acetate, pH 7.5, 40C
0.001
-
phosphoenolpyruvate
-
Km less than 0.001 mM, in the presence of D-arabinose 5-phosphate, at 30C
0.0024
-
phosphoenolpyruvate
-
N23C/C247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.0025
-
phosphoenolpyruvate
-
in the presence of L-xylose 5-phosphate, at 30C
0.0025
-
phosphoenolpyruvate
-
wild type, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0026
-
phosphoenolpyruvate
-
pH 7.8, Zn2+-reconstituted enzyme
0.0027
-
phosphoenolpyruvate
-
N23C/C247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.0028
-
phosphoenolpyruvate
-
pH 7.4, 25C, wild-type enzyme
0.0028
-
phosphoenolpyruvate
-
N23C mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0029
-
phosphoenolpyruvate
-
mutant N57A, pH 7.5, temperature not specified in the publication
0.0031
-
phosphoenolpyruvate
-
pH 7.4, 37C
0.0033
-
phosphoenolpyruvate
-
N23C/P249A mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0036
-
phosphoenolpyruvate
-
37C
0.0038
-
phosphoenolpyruvate
-
N23C/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.0042
-
phosphoenolpyruvate
-
pH 7.4, 37C, wild-type enzyme
0.00443
-
phosphoenolpyruvate
-
pH 6.5, 25C
0.0047
-
phosphoenolpyruvate
-
P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0049
-
phosphoenolpyruvate
-
D247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0052
-
phosphoenolpyruvate
-
mutant P245A, pH 7.2, 37C
0.0053
-
phosphoenolpyruvate
-
pH 7.8, Cd2+-reconstituted enzyme
0.0054
-
phosphoenolpyruvate
-
N23C mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.0058
-
phosphoenolpyruvate
-
pH 7.8, Cu2+-reconstituted enzyme
0.0058
-
phosphoenolpyruvate
-
pH 7.5, 37C, Cd2+ mutant enzyme N26C
0.006
-
phosphoenolpyruvate
-
pH 7.3, 37C
0.006
-
phosphoenolpyruvate
-
-
0.006
-
phosphoenolpyruvate
-
pH 7.5, 37C, wild-type enzyme
0.00648
-
phosphoenolpyruvate
-
pH 6.5, 25C, Cd2+-enzyme
0.0066
-
phosphoenolpyruvate
-
N23C/C246S mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.0075
-
phosphoenolpyruvate
-
pH 6.5, 25C, Zn2+-enzyme
0.0075
-
phosphoenolpyruvate
-
pH 7.8, Co2+-reconstituted enzyme
0.0077
-
phosphoenolpyruvate
-
N23C/C247E mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0085
-
phosphoenolpyruvate
-
D247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0093
-
phosphoenolpyruvate
-
C246S mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0095
-
phosphoenolpyruvate
-
N23C/C246S/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.012
-
phosphoenolpyruvate
-
wild-type, pH 7.5, temperature not specified in the publication
0.012
-
phosphoenolpyruvate
-
wild-type, pH 7.2, 37C
0.013
-
phosphoenolpyruvate
-
mutant D243E, pH 7.2, 37C
0.0153
-
phosphoenolpyruvate
-
N23C/C246S/D247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.017
-
phosphoenolpyruvate
Q8GLK7
pH 7.5, 60C, mutant enzyme C11N, EDTA-treated
0.017
-
phosphoenolpyruvate
-
N23C/C247E/P249A mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.019
-
phosphoenolpyruvate
-
pH 7.5, 37C, Mn2+ mutant enzyme N26C
0.022
-
phosphoenolpyruvate
-
N23C/C246S/D247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.026
-
phosphoenolpyruvate
Q8GLK7
pH 7.5, 60C, wild-type Mn2+-enzyme
0.028
-
phosphoenolpyruvate
-
pH 7.5, at 90C
0.032
-
phosphoenolpyruvate
-
pH 7.5, 37C, mutant enzyme N26C, EDTA-treated
0.038
-
phosphoenolpyruvate
-
pH 7.5, at 80C
0.043
-
phosphoenolpyruvate
-
pH 7.5, at 60C or 70C
0.05
-
phosphoenolpyruvate
-
N23C/C246S mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.26
-
phosphoenolpyruvate
-
pH 7.4, 25C, mutant enzyme P145S
0.29
-
phosphoenolpyruvate
-
60C, pH 7.0, 0.48 mM Cd2+
1.65
-
phosphoenolpyruvate
-
pH 7.4, 37C, mutant enzyme P145S
0.057
-
L-xylose 5-phosphate
-
at 30C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
N23C/C246S/D247E mutant control is barely active, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA; N23C/C246S/D247E/P249A mutant control is barely active, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA; N23C/C246S/P249A mutant control is barely active, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.007
-
2-deoxy-D-ribose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.13
-
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.202
-
2-deoxy-D-ribose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
0.66
-
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.12
-
2-deoxyribose 5-phosphate
-
pH 7.6, 37C
0.149
-
D-arabinose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.178
-
D-arabinose 5-phosphate
-
mutant N59DELTA, pH 7.5, temperature not specified in the publication
0.3
-
D-arabinose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
0.32
-
D-arabinose 5-phosphate
-
mutant enzyme R1096G
0.333
-
D-arabinose 5-phosphate
-, Q9ZN55
-
0.36
-
D-arabinose 5-phosphate
-
pH 7.5, 37C, mutant enzyme N26C, EDTA-treated
0.38
-
D-arabinose 5-phosphate
-
pH 7.5, 60C
0.42
-
D-arabinose 5-phosphate
Q8GLK7
pH 7.5, 60C, mutant enzyme C11N, EDTA-treated
0.48
-
D-arabinose 5-phosphate
-
wild-type enzyme
0.49
-
D-arabinose 5-phosphate
-
pH 6.5, 25C, Zn2+-enzyme
0.74
-
D-arabinose 5-phosphate
-
pH 7.4, 25C, mutant enzyme P145S
0.87
-
D-arabinose 5-phosphate
-
pH 7.5, 70C
1
-
D-arabinose 5-phosphate
-
pH 7.4, 37C
1.08
-
D-arabinose 5-phosphate
-
pH 6.5, 25C, Cd2+-enzyme
1.47
-
D-arabinose 5-phosphate
-
pH 7.5, 80C
1.63
-
D-arabinose 5-phosphate
-
pH 7.4, 37C, mutant enzyme P145S
1.75
-
D-arabinose 5-phosphate
-
pH 7.4, 25C, wild-type enzyme
1.9
-
D-arabinose 5-phosphate
-
pH 7.5, 37C, Cd2+ mutant enzyme N26C; pH 7.5, 37C, Mn2+ mutant enzyme N26C
2
-
D-arabinose 5-phosphate
-
pH 7.5, 90C
2.7
-
D-arabinose 5-phosphate
-
at 30C
4
-
D-arabinose 5-phosphate
-
60C, pH 7.0, 0.48 mM Cd2+
4.4
-
D-arabinose 5-phosphate
-
mutant P245A, pH 7.2, 37C
4.8
-
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
4.8
-
D-arabinose 5-phosphate
-
mutant D243E, pH 7.2, 37C; wild-type, pH 7.2, 37C
5.31
-
D-arabinose 5-phosphate
-
pH 6.5, 25C
5.6
-
D-arabinose 5-phosphate
-
pH 7.4, 37C, wild-type enzyme
5.9
-
D-arabinose 5-phosphate
-
37C
6.1
-
D-arabinose 5-phosphate
-
pH 7.5, 37C, wild-type enzyme
6.8
-
D-arabinose 5-phosphate
-
pH 7.6, 37C
8
-
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
9
-
D-arabinose 5-phosphate
Q8GLK7
pH 7.5, 60C, wild-type Mn2+-enzyme
0.02
-
phosphoenolpyruvate
-
N23C/C246S mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.095
-
phosphoenolpyruvate
-, Q9ZN55
-
0.1
-
phosphoenolpyruvate
-
pH 7.8, Co2+-reconstituted enzyme; pH 7.8, Cu2+-reconstituted enzyme
0.3
-
phosphoenolpyruvate
-
pH 7.8, Zn2+-reconstituted enzyme
0.31
-
phosphoenolpyruvate
-
recombinant enzyme produced in Escherichia coli, native Zn2+ and Fe2+ not substituted, 100 mM Tris-acetate, pH 7.5, 40C
0.31
-
phosphoenolpyruvate
-
N23C/C247E/P249A mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.32
-
phosphoenolpyruvate
-
mutant enzyme R106G
0.333
-
phosphoenolpyruvate
-, Q9ZN55
-
0.34
-
phosphoenolpyruvate
-
enzyme preparation 1, substitution with 5 microM Cu2+, 100 mM Tris-acetate, pH 7.5, 40C
0.36
-
phosphoenolpyruvate
-
pH 7.5, 37C, mutant enzyme N26C, EDTA-treated
0.36
-
phosphoenolpyruvate
-
enzyme preparation 1, substitution with 5 microM Cu2+, pH 5.0, 40C
0.38
-
phosphoenolpyruvate
-
pH 7.5, 60C
0.38
-
phosphoenolpyruvate
-
N23C/C247E mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA; N23C/P249A mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.41
-
phosphoenolpyruvate
-
enzyme preparation 1, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40C
0.42
-
phosphoenolpyruvate
Q8GLK7
pH 7.5, 60C, mutant enzyme C11N, EDTA-treated
0.46
-
phosphoenolpyruvate
-
independent enzyme preparation 2, substitution with 50 microM Cd2+, pH 5.0, 40C
0.47
-
phosphoenolpyruvate
-
enzyme preparation 1, substitution with 50 microM Zn2+, 100 mM Tris-acetate, pH 7.5, 40C
0.48
-
phosphoenolpyruvate
-
wild-type enzyme
0.48
-
phosphoenolpyruvate
-
independent preparation 2 enzyme, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40C
0.49
-
phosphoenolpyruvate
-
pH 6.5, 25C, Zn2+-enzyme
0.72
-
phosphoenolpyruvate
-
pH 7.4, 25C, mutant enzyme P145S
0.87
-
phosphoenolpyruvate
-
pH 7.5, 70C
0.93
-
phosphoenolpyruvate
-
N23C mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.94
-
phosphoenolpyruvate
-
N23C/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
1
-
phosphoenolpyruvate
-
pH 7.4, 37C
1
-
phosphoenolpyruvate
-
pH 7.8, Cd2+-reconstituted enzyme
1.08
-
phosphoenolpyruvate
-
pH 6.5, 25C, Cd2+-enzyme
1.42
-
phosphoenolpyruvate
-
N23C mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
1.47
-
phosphoenolpyruvate
-
pH 7.5, 80C
1.9
-
phosphoenolpyruvate
-
pH 7.5, 37C, Cd2+ mutant enzyme N26C; pH 7.5, 37C, Mn2+ mutant enzyme N26C
2
-
phosphoenolpyruvate
-
pH 7.5, 90C
2.02
-
phosphoenolpyruvate
-
pH 7.4, 37C, mutant enzyme P145S
2.02
-
phosphoenolpyruvate
-
N23C/C247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
2.08
-
phosphoenolpyruvate
-
pH 7.4, 25C, wild-type enzyme
2.71
-
phosphoenolpyruvate
-
N23C/C246S mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
3.27
-
phosphoenolpyruvate
-
N23C/C247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
3.6
-
phosphoenolpyruvate
-
D247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
3.9
-
phosphoenolpyruvate
-
N23C/C246S/D247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
4
-
phosphoenolpyruvate
-
60C, pH 7.0, 0.48 mM Cd2+
4.4
-
phosphoenolpyruvate
-
D247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA; N23C/C246S/D247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
4.79
-
phosphoenolpyruvate
-
N23C/C246S/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
5.31
-
phosphoenolpyruvate
-
pH 6.5, 25C
5.5
-
phosphoenolpyruvate
-
C246S mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
5.9
-
phosphoenolpyruvate
-
37C
6.1
-
phosphoenolpyruvate
-
pH 7.5, 37C, wild-type enzyme
6.7
-
phosphoenolpyruvate
-
pH 7.4, 37C, wild-type enzyme
8
-
phosphoenolpyruvate
-
wild type, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
8.6
-
phosphoenolpyruvate
-
P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9
-
phosphoenolpyruvate
Q8GLK7
pH 7.5, 60C, wild-type Mn2+-enzyme
100
-
phosphoenolpyruvate
-
in 10 mM ammonium acetate buffer, pH 7.8
1.1
-
L-xylose 5-phosphate
-
at 30C
additional information
-
additional information
-
N23C/C246S/D247E mutant control is barely active, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA; N23C/C246S/D247E/P249A mutant control is barely active, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA; N23C/C246S/P249A mutant control is barely active, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.016
-
2-deoxy-D-ribose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
2423
0.13
-
2-deoxy-D-ribose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication; wild-type, pH 7.5, temperature not specified in the publication
2423
0.57
-
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
2423
0.016
-
D-arabinose 5-phosphate
-
mutant N59DELTA, pH 7.5, temperature not specified in the publication
9096
0.02
-
D-arabinose 5-phosphate
-
N23C/C246S mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9096
0.29
-
D-arabinose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
9096
0.9
-
D-arabinose 5-phosphate
-
N23C/C247E/P249A mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9096
1.6
-
D-arabinose 5-phosphate
-
N23C/C247E mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9096
1.8
-
D-arabinose 5-phosphate
-
mutant D243E, pH 7.2, 37C
9096
3.5
-
D-arabinose 5-phosphate
-
N23C/P249A mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9096
3.7
-
D-arabinose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
9096
7.9
-
D-arabinose 5-phosphate
-
N23C/C246S/D247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
9096
8.1
-
D-arabinose 5-phosphate
-
N23C/C246S/D247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
9096
16
-
D-arabinose 5-phosphate
-
N23C mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9096
19
-
D-arabinose 5-phosphate
-
N23C/C247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
9096
23
-
D-arabinose 5-phosphate
-
N23C/C247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
9096
25
-
D-arabinose 5-phosphate
-
N23C/C246S/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
9096
26
-
D-arabinose 5-phosphate
-
C246S mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9096
28
-
D-arabinose 5-phosphate
-
N23C/C246S mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
9096
49
-
D-arabinose 5-phosphate
-
D247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9096
72
-
D-arabinose 5-phosphate
-
N23C/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
9096
73
-
D-arabinose 5-phosphate
-
D247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9096
118
-
D-arabinose 5-phosphate
-
N23C mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
9096
180
-
D-arabinose 5-phosphate
-
mutant P245A, pH 7.2, 37C
9096
220
-
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
9096
230
-
D-arabinose 5-phosphate
-
wild-type, pH 7.2, 37C
9096
660
-
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
9096
717
-
D-arabinose 5-phosphate
-
P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9096
0.4
-
phosphoenolpyruvate
-
N23C/C246S mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
15572
18
-
phosphoenolpyruvate
-
N23C/C247E/P249A mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
15572
49
-
phosphoenolpyruvate
-
N23C/C247E mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
15572
115
-
phosphoenolpyruvate
-
N23C/P249A mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
15572
200
-
phosphoenolpyruvate
-
N23C/C246S/D247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
15572
247
-
phosphoenolpyruvate
-
N23C/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
15572
257
-
phosphoenolpyruvate
-
N23C/C246S/D247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
15572
263
-
phosphoenolpyruvate
-
N23C mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
15572
332
-
phosphoenolpyruvate
-
N23C mutant control, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
15572
370
-
phosphoenolpyruvate
-
mutant D243E, pH 7.2, 37C
15572
400
-
phosphoenolpyruvate
-
wild-type, pH 7.2, 37C
15572
411
-
phosphoenolpyruvate
-
N23C/C246S mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
15572
424
-
phosphoenolpyruvate
-
D247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
15572
504
-
phosphoenolpyruvate
-
N23C/C246S/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
15572
591
-
phosphoenolpyruvate
-
C246S mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
15572
748
-
phosphoenolpyruvate
-
N23C/C247E/P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
15572
850
-
phosphoenolpyruvate
-
mutant P245A, pH 7.2, 37C
15572
898
-
phosphoenolpyruvate
-
D247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
15572
1363
-
phosphoenolpyruvate
-
N23C/C247E mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
15572
1830
-
phosphoenolpyruvate
-
P249A mutant, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
15572
3200
-
phosphoenolpyruvate
-
wild type, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
15572
1400
-
D-arabinose 5-phosphate
-
wild type, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9096
additional information
-
additional information
-
N23C/C246S/D247E mutant control is barely active, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA; N23C/C246S/D247E/P249A mutant control is barely active, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA; N23C/C246S/P249A mutant control is barely active, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0079
-
1-carboxyheptane-1,7-diyl bis(phosphate)
-
pH 7.2, 37C
0.02
-
1-carboxyheptane-1,7-diyl bis(phosphate)
-
pH 7.2, 37C
0.6
-
2,6-Anhydro-3-deoxy-2beta-phosphonylmethyl-8-phosphate-D-glycero-D-talo-octonate
-
pH 7.3, 37C
1
-
D-ribose 5-phosphate
-
pH 7.3, 37C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0293
-
1,10-phenanthroline
-
IC50: 0.0293 mM
0.0422
-
2,6-pyridine dicarboxylic acid
-
IC50: 0.0422 mM
0.212
-
EDTA
-
IC50: 0.212 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.01
-
-
N23C/C246S/D247E mutant control, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA; N23C/C246S/D247E/P249A mutant control, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.06
-
-
N23C/C246S/P249A mutant control, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.19
-
-
N23C/C246S mutant control, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.3
-
-
N23C/C247E mutant control, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.35
-
-
N23C/C247E/P249A mutant control, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.6
-
-
crude cell lysate, at 25C and pH 7.5
0.76
-
-
N23C/P249A mutant control, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
1.9
-
-
N23C mutant control, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
2
-
-
purified enzyme, at 25C and pH 7.5
2.34
-
-
N23C/P249A mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
2.9
-
-
N23C mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
3.1
-
-
N23C/C247E mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
4.34
-
-
N23C/C247E/P249A mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
5
-
-
N23C/C246S mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
5.64
-
-
N23C/C246S/D247E/P249A mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
6.3
-
-
D247E/P249A mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
6.39
-
-
D247E mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
8.4
-
-
N23C/C246S/D247E mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
9.8
-
-
N23C/C246S/P249A mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
10.1
-
-
C246S mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
11.7
-
-
P249A mutant, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
12
-
-
wild type, 200 microM phosphoenolpyruvate, 37C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
6
-
and a second optimum at pH 9.0
5.5
6
-
in 10-min reaction assay
7.4
-
-
50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer
9
-
-
and a second optimum at pH 4.0-6.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 50C
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
-
-
50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.5
80
-
-
in 10-min reaction assay
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
70
-
50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.5, 20C, 25C, 30C, 35C, 40C, 45C, 50C, 60C, 70C
37
61
-
37C: about 40% of maximal activity, 61C: about 55% of maximal activity
45
70
-
45C: about 50% of maximal activity, 70C: about 55% of maximal activity
60
90
-
60C: about 30% of maximal activity, 70C: about 70% of maximal activity, 90C: about 40% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-, Q7XZC8
synchronized Bright-Yellow 2. The expression of the gene is associated with the M phase of the cell cycle
Manually annotated by BRENDA team
Q9ARD1, -
LekdsA mRNAs are preferentially expressed in dividing tissues during fruit development
Manually annotated by BRENDA team
Q9ARD1, -
in fulla differentiated leaves the basal activity is 1.5fold lower than in immature leAVES
Manually annotated by BRENDA team
-
AtkdsA2 is predominantly expressed in roots
Manually annotated by BRENDA team
Arabidopsis sp. AtkdsA2
-
AtkdsA2 is predominantly expressed in roots
-
Manually annotated by BRENDA team
Q9AV97
AtkdsA1 is predominantly expressed in shoots
Manually annotated by BRENDA team
additional information
Q9AV97
isoform AtkdsA2 gene expression is preferentially associated with plantlet organs displaying a meristematic activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Burkholderia ambifaria (strain MC40-6)
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30000
-
-
SDS-PAGE
30000
-
-
monomer, SDS-PAGE
30400
-
-
monomer with 1 Co2+, ESI-MS, 50 mM ammonium acetate solution, pH 7.5
30440
-
-
monomer with 1 Zn2+ or 1 Cu2+, ESI-MS, 50 mM ammonium acetate solution, pH 7.5
30480
-
-
monomer with 1 Cd2+, ESI-MS, 50 mM ammonium acetate solution, pH 7.5
30850
-
-
monomer, ESI-MS
60690
-
-
dimer with 1 Cd2+, ESI-MS, 50 mM ammonium acetate solution, pH 7.5
60760
-
-
dimer with 1 Co2+, ESI-MS, 50 mM ammonium acetate solution, pH 7.5
60840
-
-
dimer with 2 Zn2+ or 2 Cu2+, ESI-MS, 50 mM ammonium acetate solution, pH 7.5
62680
-
-
dimer, ESI-MS
76000
-
-
gel filtration
90000
-
-
gel filtration, non-denaturing PAGE
97000
-
-
wild-type enzyme, gel filtration
97600
-
-
gel filtration
121500
-
-
tetramer with 2 Co2+, ESI-MS, 50 mM ammonium acetate solution, pH 7.5
121600
-
-
tetramer with 4 Zn2+ or 4 Cu2+, ESI-MS, 50 mM ammonium acetate solution, pH 7.5
121800
-
-
tetramer with 4 Cd2+, ESI-MS, 50 mM ammonium acetate solution, pH 7.5
123400
-
-
tetramer, ESI-MS
130000
-
-
native protein, gel-filtration chromatography
additional information
-
-
two poorly resolved peaks are detected by gel filtration of the mutant enzyme P145S: 91000 Da and 53000 Da
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 30842, electrospray mass spectrometry
?
-
x * 29348, calculation from nucleotide sequence; x * 30000, SDS-PAGE
?
-
3 * 29736, electrospray ionization mass spectrometry
?
Chlamydia psittaci 6BC
-
x * 29348, calculation from nucleotide sequence; x * 30000, SDS-PAGE
-
dimer
-
2 * 31519, MALDI-MS
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
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
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
-
4 * 30000, gel-filtration chromatography
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
trimer
-
3 * 32000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
data reading at -173C
-
structure of the metal-free and Cd2+ forms of the enzyme are determined in the uncomplexed state and in complex with various combinations of phosphoenolpyruvate, arabinose 5-phosphate and erythrose 4-phosphate
-
X-ray structure of wild-type enzyme shows that when both phosphoenolpyruvate and D-arabinose 5-phosphate bind, the active site becomes isolated from the environment due to a conformational change of the L7 loop. The structures of the R106G mutant, without substrates, and with phosphoenolpyruvate and phosphoenolpyruvate plus D-arabinose 5-phosphate bound reveal that in R106G closure of the L7 loop is impaired
-
crystallization is performed by vapor diffusion in hanging drops
-
crystals are grown at 23C by vapor diffusion in hanging drops, crystal structures of the enzyme in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor
-
structures of apo-enzyme and of binary complexes with the substrates phosphoenolpyruvate, the product 2-dehydro-3-deoxy-D-octonate 8-phosphate and the catalytically inactive 1-deoxy analog of arabinose 5-phosphate
-
the X-ray structures, determined for the mutants with altered KANRS motif, indicate no gross structural penalty resulting from mutation, but the subtle changes observed in the active sites of these mutant proteins correlate with their altered catalytic function
-
vapor-diffusion hanging drop method, pH 4.6 and pH 5.0, no diffraction quality crystals at higher pH in the range of the active enzyme
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27
-
-
unstable in absence of phosphoenolpyruvate
37
-
-
half-life of enzyme from mutant strain PR32, without D-arabinose-5-phosphate: 4.5 min. Half-life of enzyme from mutant strain PR32, in presence of 13 mM D-arabinose 5-phosphate: 18 min. Half-life of enzyme from parent strain PR122: 31 min
37
-
-
1 h, wild-type enzyme retains full activity, 50% loss of activity of the mutant enzyme P145S
40
-
-
30 min, in absence of any substrate or in presence of D-arabinose 5-phosphate, 30% loss of activity, no inactivation in presence of phosphoenolpyruvate
42
-
-
half-life of enzyme from mutant strain PR32, without D-arabinose-5-phosphate: 2.5 min. Half-life of enzyme from mutant strain PR32, in presence of 13 mM D-arabinose 5-phosphate: 9.5 min. Half-life of enzyme from parent strain PR122: 13 min
45
-
-
15 min, 30% loss of activity
50
-
-
stable in presence of phosphoenolpyruvate
50
-
-
30 min, in absence of any substrate or in presence of D-arabinose 5-phosphate, 30% loss of activity, no inactivation in presence of phosphoenolpyruvate
60
-
-
20% incrase in activity after 7 min
68
-
-
mutant C21N, presence of Cd2+, melting temperature; mutant D243E, melting temperature; wild-type, melting temperature
69
-
-
mutant C21N, melting temperature
70
-
-
half-life: 30.3 h
70
-
-
half-life: 8.0 h
71
-
-
mutant P245A, melting temperature
78
-
-
mutant D243E, presence of Cd2+, melting temperature
79
-
-
mutant P245A, presence of Cd2+, melting temperature
80
-
-
half-life: 8.1 h
80
-
-
half-life: 2.25 h
82
-
-
wild-type, presence of Cd2+, melting temperature
90
-
-
half-life: 1.5 h
90
-
-
half-life: 0.5 h
additional information
-
-
temperature-sensitive lethal mutant of Salmonella thyphimurium that is conditionally defective in 3-deoxy-D-manno-octulosonate-8-phosphate synthesis due to temperature-sensitive phospho-2-dehydro-3-deoxyoctonate aldolase
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dialysis against 10 mM EDTA in 50 mM Tris-HCl buffer, pH 7.3, inactivates
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repeated freezing and thawing causes loss of activity
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dialysis against 0.01 M Tris-HCl, pH 7.5, containing 0.01 M thioglycerol for 4 h, less than 20% loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 50% loss of activity after 14 days
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-90C, 0.1 M potassium phosphate buffer, pH 7.2, stable for up to 1 year
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4C, in 20 mM ammonium acetate (pH 7.8), overnight, remains stable in the phosphoenol-bound state
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme purification followed by incubation with 50 microM Cd2+, Zn2+, or Cu2+ in 20 mM Tris-HCl buffer, pH 7.5, to substitute the metal ions Fe2+ or Co2+
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recombinant enzyme
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recombinant enzyme
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recombinant enzyme
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one-step purification
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overnight dialysis against 50 mM ammonium acetate, pH 7.8, 4C, reconstitution with substrates and products
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apoenzyme + 200 microM metal ion salt + 50 mM Tris-HCl buffer, pH 7.5 dialyzed against 50 mM ammonium acetate buffer, pH 7.5, 4C
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Source 15Q column chromatography and Source 15Phe column chromatography
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recombinant enzyme from wild-type strain AG701 and temperature-sensitive strain AG701i50
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
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expression in Escherichia coli
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in Escherichia coli with plasmid pet28a
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1 15.5-kb segment containing the kdsA gene, expression in Escherichia coli
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expression in Escherichia coli
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cloned into a T7-driven expression vector, overexpression in Escherichia coli
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expression in Escherichia coli
Q9AV97
expression in Escherichia coli
Q46225
expression in Salmonella enterica serovar typhimurium AG701i50
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expression in Escherichia coli
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expression in Salmonella typhimurium
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localization of the kdsA gene with the aid of the physical map of the Escherichia coli chromosome
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expression in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli BL21(DE3)
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enzyme from wild-type strain AG701 and temperature-sensitive strain AG701i50 expressed in Escherichia coli
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expression in Salmonella enterica serovar typhimurium
Q9ARD1, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A56P/N57DELTA
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mutation in the absolutely conserved KANRS motif. Complete loss of activity
C21N
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complete loss of activity
D243A
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mutation of the absolutely conserved 243AspGlyPro245 motif, complete loss of activity
D243Q
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mutation of the absolutely conserved 243AspGlyPro245 motif, active enzyme with altered metal-dependency
K55A
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mutation in the absolutely conserved KANRS motif. Complete loss of activity
N57A
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mutation in the absolutely conserved KANRS motif. About 2% of wild-type activity
N57DELTA
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mutation in the absolutely conserved KANRS motif. Complete loss of activity
P245A
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mutation of the absolutely conserved 243AspGlyPro245 motif, active enzyme with altered metal-dependency
C11N
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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
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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
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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
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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
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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
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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
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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
Q8GLK7
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
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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+
A56P/N57DELTA
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mutation in the absolutely conserved KANRS motif. Complete loss of activity
N57D
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mutation in the absolutely conserved KANRS motif. Complete loss of activity
N59A
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mutant retains less than 1% of the wild type activity
N59A
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mutation in the absolutely conserved KANRS motif. About 0.2% of wild-type activity
N59DELTA
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mutation in the absolutely conserved KANRS motif. Less than 0.1% of wild-type activity
P145S
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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 30C. Above 30C the activity of the mutant enzyme decreases dramatically
K57A
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mutation in the absolutely conserved KANRS motif. Complete loss of activity
additional information
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replacement of asparagine with metal-binding cysteine is not sufficient to produce a metal-dependent mutant, 3 to 4 mutations establish a fully functional obligate metal-dependent KDO8PS, metal-dependent mutants containing the C246S exchange are activated in the presence of Mn2+ and Cd2+ to specific activities comparable to the wild type, other metal-dependent mutations show lower activation levels, high concentrations can have inhibitory effects, Mg2+, Ca2+, Ni2+, Sr2+, and Ba2+ have little or no effect on activity, Co2+ and Fe2+ have varying effects, Zn2+ is inhibitory for all cloned enzymes
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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enzyme absent in mammals, therefore potential target for the development of new antibiotics