Information on EC 4.1.2.43 - 3-hexulose-6-phosphate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY
4.1.2.43
-
RECOMMENDED NAME
GeneOntology No.
3-hexulose-6-phosphate synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-arabino-hex-3-ulose 6-phosphate = D-ribulose 5-phosphate + formaldehyde
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldol condensation
Q9LBW4
-
aldol condensation
Mycobacterium gastri MB19
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
formaldehyde assimilation II (RuMP Cycle)
-
formaldehyde oxidation I
-
Metabolic pathways
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
Pentose phosphate pathway
-
SYSTEMATIC NAME
IUBMB Comments
D-arabino-hex-3-ulose-6-phosphate formaldehyde-lyase (D-ribulose-5-phosphate-forming)
Requires Mg2+ or Mn2+ for maximal activity [1]. The enzyme is specific for D-ribulose 5-phosphate as substrate as ribose 5-phosphate, xylulose 5-phosphate, allulose 6-phosphate and fructose 6-phosphate cannot act as substrate. In addition to formaldehyde, the enzyme can also use glycolaldehyde and methylglyoxal [7]. This enzyme, along with EC 5.3.1.27, 6-phospho-3-hexuloisomerase, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds [1]. The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of this enzyme and EC 5.3.1.27, 6-phospho-3-hexuloisomerase [6]. This enzyme is a member of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily [5].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-hexulose phosphate synthase
-
-
-
-
3-hexulose phosphate synthase
-
-
3-hexulose phosphate synthase
-
-
3-hexulose phosphate synthase
Methylomonas sp. M15
-
-
-
3-hexulose phosphate synthase
-
-
3-hexulose phosphate synthase
Mycobacterium gastri MB19
-
-
-
3-hexulose-6-phosphate formaldehyde lyase
Q9F6B7
-
3-hexulose-6-phosphate formaldehyde lyase
Aminomonas aminovorus C2A1
Q9F6B7
-
-
3-hexulose-6-phosphate synthase
Q9F6B7
-
3-hexulose-6-phosphate synthase
Aminomonas aminovorus C2A1
Q9F6B7
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
-
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
-
;
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
Brevibacillus brevis S1
-
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
Methylomonas aminofaciens 77a
-
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
Methylomonas sp. M15
-
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
Mycobacterium gastri MB19
-
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
3-hexulose-6-phosphate synthase
Pyrococcus horikoshii OT-3
-
; 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-6-phosphate synthase
-
-
3-hexulose-phosphate synthase
-
-
3-hexulose-phosphate synthase
Methylomonas sp. M15
-
-
-
3-hexulosephosphate synthase
-
-
-
-
3-hexulosephosphate synthase
-
-
3-hexulosephosphate synthase
Acetobacter sp. MB 58
-
;
-
3-hexulosephosphate synthase
-
-
3-hexulosephosphate synthase
-
-
3-hexulosephosphate synthase
Methylomonas aminofaciens 77a
-
;
-
3-hexulosephosphate synthase
-
-
3-hexulosephosphate synthase
Methylomonas sp. GBS, Methylomonas sp. GI33, Methylomonas sp. M15
-
-
-
3-hexulosephosphate synthase
-
-
3-hexulosephosphate synthase
Mycobacterium gastri MB19
-
-
-
3-hexulosephosphate synthase
-
-
3-hexulosephosphate synthase
-
-
3-hexulosephosphate synthase
-
-
-
D-arabino-3-hexulose 6-phosphate formaldehyde lyase
-
-
D-arabino-3-hexulose 6-phosphate formaldehyde lyase
-
-
D-arabino-3-hexulose 6-phosphate formaldehyde lyase
Methylomonas aminofaciens 77a
-
-
-
D-arabino-3-hexulose 6-phosphate formaldehyde-lyase
-
-
-
-
Fae-Hps
-
protein with hexulose-6-phosphate synthase and formaldehyde activating enzyme activities
Fae-Hps
Methanosarcina barkeri Fusaro
-
protein with hexulose-6-phosphate synthase and formaldehyde activating enzyme activities
-
hexose phosphate synthase
-
-
hexulose-6-phosphate synthase
-
-
hexulose-6-phosphate synthase
Methanosarcina barkeri Fusaro
-
-
-
HPS
Acetobacter sp. MB 58
-
;
-
HPS
Acidomonas methanolica MB58
-
-
-
HPS
Aminomonas aminovorus C2A1
Q9F6B7
-
-
HPS
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
HPS
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
-
HPS
Brevibacillus brevis S1
-
-
-
HPS
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
HPS
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
HPS
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
HPS
Methylomonas aminofaciens 77a
-
;
-
HPS
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
HPS
Methylomonas sp. GBS, Methylomonas sp. GI33
-
-
-
HPS
Methylomonas sp. M15
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
-
HPS
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
HPS
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
HPS
Mycobacterium gastri MB19
-
3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea
-
HPS
Mycobacterium gastri MB19
Q9LBW4
-
-
HPS
-
-
-
HPS
-
-
HPS
Pyrococcus horikoshii OT-3
-
;
-
HPS-aldolase
-
-
HPS-aldolase
Methylomonas sp. M15
-
-
-
HPS-PHI
-
bifunctional enzyme with 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities
HPS-PHI
Pyrococcus horikoshii OT-3
-
bifunctional enzyme with 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities
-
HPS/PHI
-
bifunctional fusion enzyme
CAS REGISTRY NUMBER
COMMENTARY
55576-36-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Acetobacter sp. MB 58
-
-
-
Manually annotated by BRENDA team
strain MB58
-
-
Manually annotated by BRENDA team
Acidomonas methanolica MB58
strain MB58
-
-
Manually annotated by BRENDA team
strain C2A1
UniProt
Manually annotated by BRENDA team
Aminomonas aminovorus C2A1
strain C2A1
UniProt
Manually annotated by BRENDA team
strain MGA3
-
-
Manually annotated by BRENDA team
strain C1
-
-
Manually annotated by BRENDA team
Brevibacillus brevis S1
strain S1
-
-
Manually annotated by BRENDA team
strain Fusaro
-
-
Manually annotated by BRENDA team
Methanosarcina barkeri Fusaro
strain Fusaro
-
-
Manually annotated by BRENDA team
strain KT, obligate methylotroph
-
-
Manually annotated by BRENDA team
formerly Methylococcus capsulatus
-
-
Manually annotated by BRENDA team
Methylomonas aminofaciens 77a
strain 77a
-
-
Manually annotated by BRENDA team
Methylomonas aminofaciens 77a
strain 77a
Uniprot
Manually annotated by BRENDA team
strain GBS; strain GI33; strain M15
-
-
Manually annotated by BRENDA team
strain M15 DSM 580
-
-
Manually annotated by BRENDA team
Methylomonas sp. GBS
strain GBS
-
-
Manually annotated by BRENDA team
Methylomonas sp. GI33
strain GI33
-
-
Manually annotated by BRENDA team
Methylomonas sp. M15
strain M15
-
-
Manually annotated by BRENDA team
Methylomonas sp. M15
strain M15 DSM 580
-
-
Manually annotated by BRENDA team
strain MB19, facultative methylotroph
-
-
Manually annotated by BRENDA team
Mycobacterium gastri MB19
-
-
-
Manually annotated by BRENDA team
Mycobacterium gastri MB19
-
UniProt
Manually annotated by BRENDA team
Mycobacterium gastri MB19
strain MB19
-
-
Manually annotated by BRENDA team
Mycobacterium gastri MB19
strain MB19, facultative methylotroph
-
-
Manually annotated by BRENDA team
strain W6
-
-
Manually annotated by BRENDA team
strain W6
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
Bacillus methanolicus MGA3, Brevibacillus brevis S1, Methylomonas aminofaciens 77a, Mycobacterium gastri MB19
-
phylogenetic analysis
-
physiological function
-
bifunctional enzyme
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-ribulose 5-phosphate + acetaldehyde
?
show the reaction diagram
Methylomonas sp., Methylomonas sp. M15
-
-
-
-
?
D-ribulose 5-phosphate + benzaldehyde
?
show the reaction diagram
Methylomonas sp., Methylomonas sp. M15
-
-
-
-
?
D-ribulose 5-phosphate + bromoacetaldehyde
?
show the reaction diagram
Methylomonas sp., Methylomonas sp. M15
-
-
-
-
?
D-ribulose 5-phosphate + butyraldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + chloral
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + chloroacetaldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + chloropropionaldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + dichloroacetaldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + DL-glyceraldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Q602L4
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Q48907
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-, Q9F6B7
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Q9LBW4
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
the enzyme is highly specific for D-ribulose 5-phosphate as an acceptor of aldehydes
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
the enzyme is specific for formaldehyde and D-ribulose 5-phosphate
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Methanosarcina barkeri Fusaro
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Mycobacterium gastri MB19
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Mycobacterium gastri MB19
-
the enzyme is highly specific for D-ribulose 5-phosphate as an acceptor of aldehydes
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Mycobacterium gastri MB19
Q9LBW4
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Aminomonas aminovorus C2A1
Q9F6B7
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Methylomonas sp. GI33
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Methylomonas sp. M15
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Pyrococcus horikoshii OT-3
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Acidomonas methanolica MB58
-
-
-
-
r
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Methylomonas aminofaciens 77a
-
the enzyme is specific for formaldehyde and D-ribulose 5-phosphate
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Methylomonas aminofaciens 77a, Methylomonas sp. GBS
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-3-hexulose 6-phosphate
show the reaction diagram
-
the apparent specific activity of the reverse reaction is approximately one-seventh of that of the forward reaction
-
-
r
D-ribulose 5-phosphate + formaldehyde
D-arabino-3-hexulose 6-phosphate
show the reaction diagram
Brevibacillus brevis S1, Mycobacterium gastri MB19, Methylomonas aminofaciens 77a, Bacillus methanolicus MGA3
-
-
-
-
r
D-ribulose 5-phosphate + glutaraldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + glycolaldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + glycolaldehyde
?
show the reaction diagram
Mycobacterium gastri, Mycobacterium gastri MB19
-
-
-
-
?
D-ribulose 5-phosphate + glycolaldehyde
4-heptulose 7-phosphate
show the reaction diagram
Mycobacterium gastri, Mycobacterium gastri MB19
-
-
-
-
?
D-ribulose 5-phosphate + glyoxal
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + isobutyraldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + isovaleraldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + methylglyoxal
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + methylglyoxal
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + methylglyoxal
?
show the reaction diagram
Mycobacterium gastri MB19
-
-
-
-
?
D-ribulose 5-phosphate + methylmercaptopropionaldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + propionaldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + pyridine-2-carboxaldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + pyridine-3-carboxaldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + pyridine-4-carboxaldehyde
?
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + valeraldehyde
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
key enzyme of the ribulose monophosphate pathway
-
-
-
additional information
?
-
-
does not accept D-ribose 5-phosphate, D-ribulose, D-xylose, D-xylulose 5-phosphate, D-fructose 6-phosphate, D-fructose 1-phosphate, D-fructose 1,6-bisphosphate, D-glucose 6-phosphate, D-glucose 1-phosphate, D-fructose, D-glucose, D,L-glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, hydroxypyruvate, dihydroxyacetone, D-erythrose 4-phospate, pivalaldehyde, acrolein, crotonaldehyde, glyoxalic acid, malonaldehyde, furfural as substrates
-
-
-
additional information
?
-
-
no detectable activity with D-fructose 6-phosphate, D-fructose 1,6-bisphosphate, D-glucose 1-phosphate, D-glucose 6-phosphate, lithium hydroxypyruvate, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, D-ribose 5-phosphate, and D-xylose 5-phosphate
-
-
-
additional information
?
-
Mycobacterium gastri, Mycobacterium gastri MB19
-
no detectable activity with D-ribulose 1,5-bisphosphate, D-ribose 5-phosphate, D-erythrose 4-phosphate, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate, D-glucose 6-phosphate, D-glucose 1-phosphate, and D-xyluloSe 5-phosphate
-
-
-
additional information
?
-
Methylomonas sp. M15
-
no detectable activity with D-fructose 6-phosphate, D-fructose 1,6-bisphosphate, D-glucose 1-phosphate, D-glucose 6-phosphate, lithium hydroxypyruvate, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, D-ribose 5-phosphate, and D-xylose 5-phosphate
-
-
-
additional information
?
-
Methylomonas sp. M15
-
does not accept D-ribose 5-phosphate, D-ribulose, D-xylose, D-xylulose 5-phosphate, D-fructose 6-phosphate, D-fructose 1-phosphate, D-fructose 1,6-bisphosphate, D-glucose 6-phosphate, D-glucose 1-phosphate, D-fructose, D-glucose, D,L-glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, hydroxypyruvate, dihydroxyacetone, D-erythrose 4-phospate, pivalaldehyde, acrolein, crotonaldehyde, glyoxalic acid, malonaldehyde, furfural as substrates
-
-
-
additional information
?
-
Pyrococcus horikoshii OT-3
-
key enzyme of the ribulose monophosphate pathway
-
-
-
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
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-3-hexulose 6-phosphate
show the reaction diagram
-
the apparent specific activity of the reverse reaction is approximately one-seventh of that of the forward reaction
-
-
r
D-ribulose 5-phosphate + formaldehyde
D-arabino-3-hexulose 6-phosphate
show the reaction diagram
Brevibacillus brevis S1, Mycobacterium gastri MB19
-
-
-
-
r
D-ribulose 5-phosphate + formaldehyde
D-arabino-hex-3-ulose 6-phosphate
show the reaction diagram
Methylomonas sp. M15
-
-
-
-
?
D-ribulose 5-phosphate + formaldehyde
D-arabino-3-hexulose 6-phosphate
show the reaction diagram
Methylomonas aminofaciens 77a, Bacillus methanolicus MGA3
-
-
-
-
r
additional information
?
-
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
-
key enzyme of the ribulose monophosphate pathway
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
28% stimulation of activity at 1 mM
Ca2+
-
1 mM Ca2+ is less than 50% less effective in activity stimulation than 1 mM Mg2+
Cd2+
-
the enzyme activity is also promoted with 1 mM Cd2+
Co2+
-
17% as effective as Mg2+ or Mn2+ in promoting synthase activity
Co2+
-
the enzyme activity is also promoted with 5 mM Co2+
Co2+
-
100% stimulation of activity at 1 mM
Co2+
-
1 mM Co2+ is less than 50% less effective in activity stimulation than 1 mM Mg2+
Cu2+
-
33% stimulation of activity at 1 mM
Fe2+
-
the enzyme activity is also promoted with 1 mM Fe2+
Fe2+
-
1 mM Fe2+ is less than 50% less effective in activity stimulation than 1 mM Mg2+
Mg2+
-
5 mM, essential for activity and stability, 3-hexulose phosphate synthase is rapidly and apparently irreversibly denatured by storage in the absence of one of Mg2+
Mg2+
-
1 mM Mg2+ is absolutely required for the enzyme activity and stability
Mg2+
-
required for activity
Mg2+
-
essential requirement for Mg2+ (5 mM)
Mg2+
Q602L4
dependent on
Mg2+
Q48907
dependent on
Mg2+
-
98% stimulation of activity at 1 mM
Mg2+
-
essential requirement for Mg2+
Mg2+
-
bivalent cations are essential for activity, most effective is Mg2+
Mg2+
Q9LBW4
the enzyme requires an Mg2+-assisted formation of an enediolate intermediate for catalysis of its reaction. The active site of each HPS monomer contains a magnesium ion
Mn2+
-
essential for activity and stability
Mn2+
-
Mg2+ can be replaced by Mn2+ (1 mM)
Mn2+
-
required for activity
Mn2+
-
essential requirement for Mn2+ (5 mM)
Mn2+
Q602L4
dependent on
Mn2+
Q48907
dependent on
Mn2+
-
100% stimulation of activity at 1 mM
Mn2+
-
essential requirement for Mn2+
Mn2+
-
1 mM Mn2+ is 20% less effective in activity stimulation than 1 mM Mg2+
Ni2+
-
97% stimulation of activity at 1 mM
sulfate
Q9LBW4
the active site of each HPS monomer contains a sulfate ion
Zn2+
-
10% as effective as Mg2+ or Mn2+ in promoting synthase activity
Zn2+
-
the enzyme activity is also promoted with 5 mM Zn2+
Zn2+
-
39% stimulation of activity at 1 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
49% inhibition at 1 mM
Cu2+
-
24% inhibition at 1 mM
Cu2+
-
45% inhibition with 1 mM Cu2+
Cu2+
-
1 mM Cu2+ is inhibitory, and the effect is partly abolished by Mg2+
D-ribulose 5-phosphate
-
commercial D-ribulose 5-phosphate inhibits the enzyme
EDTA
-
complete inhibition at 10 mM
EDTA
-
the enzyme is completely inhibited in the presence of EDTA, but the activity is restored depending on the amount of MgC12 supplemented
EDTA
-
the enzyme is completely inhibited by the presence of 2 mM EDTA
Glutaraldehyde
-
22% inhibition at 4 mM
glyceraldehyde
-
13% inhibition at 4 mM
glycolaldehyde
-
49% inhibition at 4 mM
glycolic acid
-
glycolic acid inhibits the enzyme competitively with respect to formaldehyde
glyoxylate
-
12% inhibition at 4 mM
Hg2+
-
81% inhibition with 1 mM Hg2+
Ni2+
-
64% inhibition at 1 mM
o-phenanthroline
-
the enzyme is completely inhibited by the presence of 2 mM o-phenanthroline
Pb2+
-
48% inhibition with 1 mM Pb2+
Tiron
-
the enzyme is completely inhibited by the presence of 2 mM tiron
Methylglyoxal
-
26% inhibition at 4 mM
additional information
-
not inhibited by ATP, ADP, AMP, NADH, D-fructose 6-phosphate, and phosphoenolpyruvate
-
additional information
-
not influenced by NaBH4
-
additional information
-
the enzyme is inactivated irreversibly on dialysis against buffer without Mg2+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
formaldehyde
-
expression of the HPS coding hxlAB operon is induced by the presence of formaldehyde
HxlR
-
necessary for formaldehyde-induced expression of the HPS coding hxlAB operon
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.075
-
D-arabino-hex-3-ulose 6-phosphate
-
in 50 mM sodium potassium phosphate buffer, 5 mM MgCl2, at pH 7.0, at 30C
0.0045
-
D-ribulose 5-phosphate
-
D-ribulose 5-phosphate generated from ribose 5-phosphate, at 50C
0.007
-
D-ribulose 5-phosphate
-
commercial D-ribulose 5-phosphate, at 50C
0.059
-
D-ribulose 5-phosphate
-
in 50 mM potassium phosphate buffer (pH 7.4), 5 mM MgCl2
0.059
-
D-ribulose 5-phosphate
Q48907
-
0.059
-
D-ribulose 5-phosphate
-
-
0.081
-
D-ribulose 5-phosphate
-
-
0.083
-
D-ribulose 5-phosphate
-
in 50 mM sodium potassium phosphate buffer, 5 mM MgCl2, at pH 7.0, at 37C
0.083
-
D-ribulose 5-phosphate
Q602L4
-
0.083
-
D-ribulose 5-phosphate
-
-
0.11
-
D-ribulose 5-phosphate
-
crude extract
0.136
-
D-ribulose 5-phosphate
-
-
0.45
-
D-ribulose 5-phosphate
-
-
1.49
-
D-ribulose 5-phosphate
Q9LBW4
pH and temperature not specified in the publication
1.6
-
D-ribulose 5-phosphate
-
-
1.6
-
D-ribulose 5-phosphate
-
in 300 mM Tris-HCI buffer (pH 7.5), at 30C
1.6
-
D-ribulose 5-phosphate
-
-
0.00147
-
formaldehyde
-
at 50C
0.15
-
formaldehyde
-
-
0.29
-
formaldehyde
-
in 50 mM potassium phosphate buffer (pH 7.4), 5 mM MgCl2
0.29
-
formaldehyde
Q48907
-
0.29
-
formaldehyde
-
-
0.49
-
formaldehyde
-
in 50 mM sodium potassium phosphate buffer, 5 mM MgCl2, at pH 7.0, at 37C
0.49
-
formaldehyde
Q602L4
-
0.49
-
formaldehyde
-
-
0.53
-
formaldehyde
-
-
0.74
-
formaldehyde
-
-
1.1
-
formaldehyde
-
-
1.1
-
formaldehyde
-
in 300 mM Tris-HCI buffer (pH 7.5), at 30C
1.1
-
formaldehyde
-
-
1.14
-
formaldehyde
-
crude extract
1.4
-
formaldehyde
-
apparent value, in 50 mM potassium phosphate, pH 7.5, with 5 mM MgCl2, at 30C
1.4
-
formaldehyde
-
in 500 mM potassium phosphate buffer, at pH 7.5, at 30C
1.5
-
formaldehyde
-
-
1.95
-
formaldehyde
-
recombinant HPS, at 80C
2.31
-
formaldehyde
-
recombinant HPS, at 60C
2.96
-
formaldehyde
-
purified recombinant enzyme, at 30C
4.3
-
glycolaldehyde
-
apparent value, in 50 mM potassium phosphate, pH 7.5, with 5 mM MgCl2, at 30C
4.3
-
glycolaldehyde
-
in 500 mM potassium phosphate buffer, at pH 7.5, at 30C
5.7
-
Methylglyoxal
-
apparent value, in 50 mM potassium phosphate, pH 7.5, with 5 mM MgCl2, at 30C
5.7
-
Methylglyoxal
-
in 500 mM potassium phosphate buffer, at pH 7.5, at 30C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
62.2
-
formaldehyde
-
recombinant HPS, at 80C
159
-
formaldehyde
-
recombinant HPS, at 60C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.4
-
-
cell free extract, at 30C
1.71
-
-
cell free extract, at 30C
3.2
-
-
cell free extract, at 30C
3.3
-
-
cell free extract
3.5
-
-
cell free extract, at 50C
4.4
-
-
hexulose-6-phosphate synthase activity of the gene product Fae-Hps, at 30C, pH 7.0
4.5
-
-
crude extract, at 30C
9.8
-
-
cell free extract
20
-
-, Q9F6B7
purified enzyme
26
-
-
crude extract
41.1
-
-
cell free extract, recombinant HPS
52
-
-
after 16fold purification
56.7
-
-
crude cell extract
64
-
-
after 18fold purification, at 50C
64
-
-
after 46fold purification, at 30C
66.5
-
-
after 14.8fold purification, at 30C
69
-
-
after 41fold purification, at 30C
70.9
-
-
after 1.73fold purification, recombinant HPS
74.2
-
-
after 23fold purification, at 30C
148
-
-
after 15.1fold purification
235
-
-
after 4.14fold purification
4100
-
-
after 161fold purification
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
8
-
in potassium phosphate buffer
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
purified recombinant enzyme
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.1
-
-
isoelectric focusing
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22000
-
-
SDS-PAGE
24000
-
-
SDS-PAGE
25000
-
-
recombinant HPS, gel filtration
27000
-
-
recombinant HPS, SDS-PAGE
27000
-
-
SDS-PAGE
32000
-
-
holenzyme
32000
-
-
gel filtration
40000
-
-
holenzyme
40000
-
-
gel filtration
42000
-
-
SDS-PAGE
43000
-
-
native enzyme, gel filtration
43000
-
-
holenzyme
43000
-
-
TSK gel G-3000SW chromatography
43000
-
-
sedimentation equilibrium method
44000
-
-
recombinant fusion enzyme HPS-PHI, SDS-PAGE
44000
-
-
holenzyme
45000
-
-
gel filtration
45000
-
-
native enzyme, gel filtration
46000
-
Q48907
holoenzyme
47000
-
-
sedimentation velocity
80000
-
-
gel filtration
162000
-
-
EDTA-solubilized HPS-PHI fusion enzyme, gel filtration
310000
-
-
gel filtration, under conditions of low pH or low ionic strength
310000
-
Q602L4
holoenzyme
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
Q9LBW4
x-ray crystallography
dimer
Mycobacterium gastri MB19
-
x-ray crystallography
-
homodimer
-
2 * 22000, SDS-PAGE
homodimer
-
2 * 23000, SDS-PAGE
homodimer
-
2 * 27000
homodimer
Q48907
2 * 23000
homodimer
-
2 * 22000
homodimer
-
2 * 22500
homodimer
-
2 * 24000
homodimer
-
2 * 48000, SDS-PAGE
homodimer
-
2 * 22000, SDS-PAGE
homodimer
-
2 * 27000
-
homodimer
Methylomonas aminofaciens 77a
-
2 * 23000, SDS-PAGE
-
homodimer
Methylomonas sp. M15
-
2 * 22000; 2 * 22000, SDS-PAGE
-
homodimer
Mycobacterium gastri MB19
-
2 * 22000, SDS-PAGE; 2 * 24000; 2 * 48000, SDS-PAGE
-
homodimer
Pyrococcus horikoshii OT-3
-
-
-
homohexamer
-
6 * 49000, gel filtration, at pH 4.6
homohexamer
Q602L4
6 * 49000
homotetramer
-
4 * 47000, HPS-PHI fusion enzyme, SDS-PAGE
homotetramer
-
4 * 20400, SDS-PAGE
homotetramer
Acidomonas methanolica MB58
-
4 * 20400, SDS-PAGE
-
homotetramer
Pyrococcus horikoshii OT-3
-
4 * 47000, HPS-PHI fusion enzyme, SDS-PAGE
-
monomer
-
1 * 27000, recombinant HPS, SDS-PAGE
monomer
-
1 * 27000, SDS-PAGE
monomer
-
1 * 27000, SDS-PAGE
-
monomer
Pyrococcus horikoshii OT-3
-
1 * 27000, recombinant HPS, SDS-PAGE
-
additional information
-
multiple forms of the enzyme may be responsible for the generation of the complex shape, and thus, the kinetic characteristic should he the sum of differing characteristics
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with a sulfate ion, sitting drop vapor diffusion method, using 18% (w/v) polyethylene glycol (PEG) 3350 and 0.2 M MgCl2
Q9LBW4
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
remains stable at pH 6.0-8.0 at 30C for 1 h, enzyme stability decreases at pH values below 6.0
7
8
-
stable in neutral to slightly alkaline solutions
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
remains stable in the pH range of 6.5-7.5 at 30C for 6 h
40
60
-
no decrease in activity is observed within 6 h at 40C in the presence of 5 mM MgCl2, at 50C and 60C the enzyme is stable for 2.5 and 0.5 h, respectively, one-half the initial activities are found after 6 and 1.5 h respectively
40
80
-
almost full activity is retained after incubation at 40C for 30 min, whereas at 80C for 10 min the enzyme is completely inactivated
55
65
-
the enzyme retains more than 50% of its activity at 55C after 1 h, the enzyme retains more than 50% of its activity at 65C after 30 min
60
-
-
3-hexulose phosphate synthase is rapidly inactivated at elevated temperatures, activity is totally lost within 5 min at 60C
90
-
-
the recombinant enzyme is stable at 90C
90
-
Q602L4
the recombinant enzyme is stable at 90C
90
-
Q48907
the recombinant enzyme is stable at 90C
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, purified enzyme, at least 1 year, no loss of activity
-
0C to -4C, purified enzyme in the presence of 3.2 M ammonium sulfate, at least 1 year, no loss of activity
-
-80C, purified enzyme, in the presence of 5 mM MgSO4, 5 mM D-ribose 5-phosphate, and 1.75 units/ml phosphoriboisomerase, at least 5 months, no loss of activity
-
-15C, in the presence of 2.5 mM MgCl2, 6 months, remains stable unless repeatedly frozen and thawed
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate fractionation, DEAE-cellulose column chromatography, and Sephadex G-100 gel filtration
-
Ni-chelating Sepharose column chromatography
-, Q9F6B7
Q-Sepharose column chromatography, phenyl-Superose column chromatography, Superose 12 chromatography, and Sephadex G-25 gel filtration
-
DEAE-Sephacel column chromatography, Q-Sepharose column chromatography, and hydroxyapatite column chromatography
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography
-
DEAE-cellulose column chromatography, hydroxylapatite column chromatography, Sephadex G-150 gel filtration, Sephadex G-100 gel filtration, and DEAE-Sephadex A-50 gel filtration
-
DEAE-cellulose column chromatography, DEAE-Sephadex A-50 gel filtration, and Sephadex G-75 gel filtration
-
polyethylene imine precipitation, S-Sepharose column chromatography, Q-Sepharose column chromatography, and Sephadex G-75 gel filtration
-
DEAE-Toyopearl column chromatography butyl-Toyopearl column chromatography
-
phenyl-Sepharose column chromatography and DEAE-Sephacel column chromatography
-
phenyl-Sepharose column chromatography, and DEAE-Sephacel column chromatography
-
DEAE-Toyopearl column chromatography, butyl-Toyopearl column chromatography, and ammonium sulfate precipitation
-
ultracentrifugation
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
-, Q9F6B7
expressed in Escherichia coli BL21 (DE3) pLysS cells
-
expression in Escherichia coli
-
3-hexulose-6-phosphate synthase/6-phosphate-3-hexuloisomerase fusion enzyme from Mycobacterium gastri is expressed in chloroplasts of Pelargonium sp.
-
expressed in Escherichia coli Rosetta (DE3) cells
Q9LBW4
expressed in Escherichia coli Rosetta (DE3) cells, HPS only, or as fusion enzyme with 6-phospho-3-hexuloisomerase
-
expression in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli Rosetta(DE3) cells
-
expression in Escherichia coli
-
expressed in Escherichia coli Rosetta(DE3) cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H134A
Q9LBW4
the mutation abolishes HPS activity
H134D
Q9LBW4
the mutation abolishes HPS activity
H134K
Q9LBW4
the mutation abolishes HPS activity
H134N
Q9LBW4
the mutation abolishes HPS activity
H134S
Q9LBW4
the mutation abolishes HPS activity
K61A
Q9LBW4
the mutant exhibits 50-90% of the activity of the wild type enzyme
K61D
Q9LBW4
the mutant exhibits 50-90% of the activity of the wild type enzyme
K61H
Q9LBW4
the mutant exhibits 50-90% of the activity of the wild type enzyme
H134A
Mycobacterium gastri MB19
-
the mutation abolishes HPS activity
-
H134D
Mycobacterium gastri MB19
-
the mutation abolishes HPS activity
-
H134K
Mycobacterium gastri MB19
-
the mutation abolishes HPS activity
-
H134N
Mycobacterium gastri MB19
-
the mutation abolishes HPS activity
-
additional information
-
the solvent-tolerant bacterium, Pseudomonas putida S12, is engineered to efficiently utilize methanol and formaldehyde as auxiliary substrates by introducing the hps and phi genes from the thermotolerant methylotrophic bacterium Bacillus brevis, by chemostat culture experiments using glucose and formaldehyde, the hps and phi-expressing strain shows both significantly improved cell mass and growth at higher formaldehyde concentrations than the control strain
additional information
Brevibacillus brevis S1
-
the solvent-tolerant bacterium, Pseudomonas putida S12, is engineered to efficiently utilize methanol and formaldehyde as auxiliary substrates by introducing the hps and phi genes from the thermotolerant methylotrophic bacterium Bacillus brevis, by chemostat culture experiments using glucose and formaldehyde, the hps and phi-expressing strain shows both significantly improved cell mass and growth at higher formaldehyde concentrations than the control strain
-
additional information
-
in order to improve the rate of vanillin degradation by Burkholderia cepacia TM1, the hps and phi genes from Methylomonas aminofaciens 77a are heterologously expressed in strain TM1, the transformant strain constitutively produces active 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase enzymes and the degradation of vanillic acid and the growth yield are significantly improved
additional information
Methylomonas aminofaciens 77a
-
in order to improve the rate of vanillin degradation by Burkholderia cepacia TM1, the hps and phi genes from Methylomonas aminofaciens 77a are heterologously expressed in strain TM1, the transformant strain constitutively produces active 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase enzymes and the degradation of vanillic acid and the growth yield are significantly improved
-
K61S
Q9LBW4
the mutant exhibits 50-90% of the activity of the wild type enzyme
additional information
-
the hps and phi genes from the methylotrophic bacterium Mycobacterium gastri MB19 are introduced into tobacco. Both genes are expressed under the control of the tomato rbcS-3C promoter, and the gene products are targeted to the chloroplasts by artificially added transit peptide sequence, the expression of both genes in plants enhances the tolerance of the transgenic plant to formaldehyde and capability of eliminating environmental formaldehyde
K61A
Mycobacterium gastri MB19
-
the mutant exhibits 50-90% of the activity of the wild type enzyme
-
additional information
Mycobacterium gastri MB19
-
the hps and phi genes from the methylotrophic bacterium Mycobacterium gastri MB19 are introduced into tobacco. Both genes are expressed under the control of the tomato rbcS-3C promoter, and the gene products are targeted to the chloroplasts by artificially added transit peptide sequence, the expression of both genes in plants enhances the tolerance of the transgenic plant to formaldehyde and capability of eliminating environmental formaldehyde
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
enzymatic preparation is suitable for the synthesis of sugars labeled with 13C at specific positions, enzymatic preparation of [1-13C]D-fructose-6-phosphate by using D-ribose-5 phosphate and [1-13C]-formaldehyde as substrates
synthesis
Methylomonas aminofaciens 77a
-
enzymatic preparation is suitable for the synthesis of sugars labeled with 13C at specific positions, enzymatic preparation of [1-13C]D-fructose-6-phosphate by using D-ribose-5 phosphate and [1-13C]-formaldehyde as substrates
-
environmental protection
-
formaldehyde is thought to be the cause of sick house syndrome, transgenic plants harboring the ribulose monophosphate pathway could be useful to improve air pollution in the indoor environment
environmental protection
Mycobacterium gastri MB19
-
formaldehyde is thought to be the cause of sick house syndrome, transgenic plants harboring the ribulose monophosphate pathway could be useful to improve air pollution in the indoor environment
-