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Literature summary extracted from

  • Orita, I.; Yurimoto, H.; Hirai, R.; Kawarabayasi, Y.; Sakai, Y.; Kato, N.
    The archaeon Pyrococcus horikoshii possesses a bifunctional enzyme for formaldehyde fixation via the ribulose monophosphate pathway (2005), J. Bacteriol., 187, 3636-3642.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.43 expressed in Escherichia coli Rosetta(DE3) cells Pyrococcus horikoshii
5.3.1.27 expression in Escherichia coli Pyrococcus horikoshii

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.27 additional information expression of the full-length gene encoding the hybrid enzyme 3-hexulose 6-phosphate synthase/6-phospho-3-hexuloisomerase, the sequence corresponding to the 3-hexulose 6-phosphate synthase region, and the sequence corresponding to the 6-phospho-3-hexuloisomerase region produces active enzymes in Escherichia coli. The bifunctional enzyme catalyzes the sequential reaction much more efficiently than a mixture of the isolated domains Pyrococcus horikoshii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.2.43 1.95
-
 formaldehyde recombinant HPS, at 80°C Pyrococcus horikoshii
4.1.2.43 2.31
-
 formaldehyde recombinant HPS, at 60°C Pyrococcus horikoshii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.2.43 25000
-
 recombinant HPS, gel filtration Pyrococcus horikoshii
4.1.2.43 27000
-
 recombinant HPS, SDS-PAGE Pyrococcus horikoshii
4.1.2.43 47000
-
 4 * 47000, HPS-PHI fusion enzyme, SDS-PAGE Pyrococcus horikoshii
4.1.2.43 162000
-
 EDTA-solubilized HPS-PHI fusion enzyme, gel filtration Pyrococcus horikoshii
5.3.1.27 21000
-
 4 * 47000, SDS-PAGE, bifunctional enzyme, 4 * 21000, SDS-PAGE, and 4 * 21475, calculated, separately expressed 6-phospho-3-hexuloisomerase domain Pyrococcus horikoshii
5.3.1.27 21475
-
 4 * 47000, SDS-PAGE, bifunctional enzyme, 4 * 21000, SDS-PAGE, and 4 * 21475, calculated, separately expressed 6-phospho-3-hexuloisomerase domain Pyrococcus horikoshii
5.3.1.27 47000
-
 4 * 47000, SDS-PAGE, bifunctional enzyme, 4 * 21000, SDS-PAGE, and 4 * 21475, calculated, separately expressed 6-phospho-3-hexuloisomerase domain Pyrococcus horikoshii
5.3.1.27 75000
-
 separately expressed 6-phospho-3-hexuloisomerase domain Pyrococcus horikoshii
5.3.1.27 162000
-
 gel filtration, bifunctional enzyme Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.2.43 additional information Pyrococcus horikoshii key enzyme of the ribulose monophosphate pathway ?
-
 ?
4.1.2.43 additional information Pyrococcus horikoshii OT-3 key enzyme of the ribulose monophosphate pathway ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.43 Pyrococcus horikoshii
-
 strain OT3
-
4.1.2.43 Pyrococcus horikoshii OT-3
-
 strain OT3
-
5.3.1.27 Pyrococcus horikoshii O59601 bifunctional 3-hexulose 6-phosphate synthase/6-phospho-3-hexuloisomerase, constitutive expression
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.43 DEAE-Toyopearl column chromatography, butyl-Toyopearl column chromatography, and ammonium sulfate precipitation Pyrococcus horikoshii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.2.43 56.7
-
 crude cell extract Pyrococcus horikoshii
4.1.2.43 235
-
 after 4.14fold purification Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.43 D-ribulose 5-phosphate + formaldehyde
-
 Pyrococcus horikoshii D-arabino-hex-3-ulose 6-phosphate
-
 ?
4.1.2.43 D-ribulose 5-phosphate + formaldehyde
-
 Pyrococcus horikoshii OT-3 D-arabino-hex-3-ulose 6-phosphate
-
 ?
4.1.2.43 additional information key enzyme of the ribulose monophosphate pathway Pyrococcus horikoshii ?
-
 ?
4.1.2.43 additional information key enzyme of the ribulose monophosphate pathway Pyrococcus horikoshii OT-3 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.2.43 homotetramer 4 * 47000, HPS-PHI fusion enzyme, SDS-PAGE Pyrococcus horikoshii
4.1.2.43 monomer 1 * 27000, recombinant HPS, SDS-PAGE Pyrococcus horikoshii
5.3.1.27 tetramer 4 * 47000, SDS-PAGE, bifunctional enzyme, 4 * 21000, SDS-PAGE, and 4 * 21475, calculated, separately expressed 6-phospho-3-hexuloisomerase domain Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
4.1.2.43 3-hexulose-6-phosphate synthase
-
 Pyrococcus horikoshii
4.1.2.43 HPS
-
 Pyrococcus horikoshii
4.1.2.43 HPS-PHI bifunctional enzyme with 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.3.1.27 60
-
 separately expressed 6-phospho-3-hexuloisomerase domain Pyrococcus horikoshii
5.3.1.27 80 85 bifunctional enzyme Pyrococcus horikoshii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.3.1.27 90
-
 half-life above 90 min, bifunctional enzyme. Half-life below 5 min, separately expressed 6-phospho-3-hexuloisomerase domain Pyrococcus horikoshii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.2.43 62.2
-
 formaldehyde recombinant HPS, at 80°C Pyrococcus horikoshii
4.1.2.43 159
-
 formaldehyde recombinant HPS, at 60°C Pyrococcus horikoshii