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Literature summary extracted from

  • Akutsu, J.; Zhang, Z.; Morita, R.; Kawarabayasi, Y.
    Identification and characterization of a thermostable bifunctional enzyme with phosphomannose isomerase and sugar-1-phosphate nucleotidylyltransferase activities from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3 (2015), Extremophiles, 19, 1077-1085.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.13
-
 Pyrococcus horikoshii
2.7.7.13 gene PH0925, recombinant expression of His-tagged enzyme PH0925 in Escherichia coli strain BL21-Codon Plus(DE3)-RIL Pyrococcus horikoshii
2.7.7.34 gene PH0925, recombinant expression of His-tagged enzyme PH0925 in Escherichia coli strain BL21-Codon Plus(DE3)-RIL Pyrococcus horikoshii
2.7.7.37 gene PH0925, recombinant expression of His-tagged enzyme PH0925 in Escherichia coli strain BL21-Codon Plus(DE3)-RIL Pyrococcus horikoshii
5.3.1.8
-
 Pyrococcus horikoshii

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.13 additional information construction of several truncated mutants of the PH0925 protein, that show altered kinetics compared to the wild-type enzyme, overview Pyrococcus horikoshii
2.7.7.34 additional information construction of several truncated mutants of the PH0925 protein, that show altered kinetics compared to the wild-type enzyme, overview Pyrococcus horikoshii
2.7.7.37 additional information construction of several truncated mutants of the PH0925 protein, that show altered kinetics compared to the wild-type enzyme, overview Pyrococcus horikoshii

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.13 EDTA complete inhibition Pyrococcus horikoshii
2.7.7.13 additional information the C-terminal 114 residue region of the PH0925 protein inhibits the Man-1-P GTase activity. The phosphomannoseisomerase activity is abolished by deletion of the C-terminal 14 residues Pyrococcus horikoshii
2.7.7.34 EDTA complete inhibition Pyrococcus horikoshii
2.7.7.37 EDTA complete inhibition Pyrococcus horikoshii
2.7.7.37 additional information the C-terminal 114 residue region of the PH0925 protein inhibits the Man-1-P GTase activity. The phosphomannose isomerase activity is abolished by deletion of the C-terminal 14 residues Pyrococcus horikoshii
5.3.1.8 EDTA 0.1 mM, about 50% inhibition Pyrococcus horikoshii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.13 0.0026
-
 GTP pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.13 0.0026
-
 GTP pH 7.6, 85°C, recombinant enzyme Pyrococcus horikoshii
2.7.7.13 0.0161
-
 alpha-D-mannose 1-phosphate pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.13 0.0161
-
 alpha-D-mannose 1-phosphate pH 7.6, 85°C, recombinant enzyme Pyrococcus horikoshii
2.7.7.37 0.0026
-
 GTP pH 7.6, 85°C, recombinant enzyme Pyrococcus horikoshii
2.7.7.37 0.0161
-
 alpha-D-mannose 1-phosphate pH 7.6, 85°C, recombinant enzyme Pyrococcus horikoshii
5.3.1.8 0.0986
-
 beta-D-mannose 6-phosphate pH 7.6, 65°C Pyrococcus horikoshii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.13 Ca2+ activates Pyrococcus horikoshii
2.7.7.13 Ca2+ 2 mM, about 50% of the activity with Cu2+ Pyrococcus horikoshii
2.7.7.13 Co2+ activates Pyrococcus horikoshii
2.7.7.13 Cu2+ best activating metal ion Pyrococcus horikoshii
2.7.7.13 Cu2+ 2 mM, maximum activity Pyrococcus horikoshii
2.7.7.13 Mg2+ 2 mM, about 80% of the activity with Cu2+ Pyrococcus horikoshii
2.7.7.13 Mg2+ highly activates sugar-1-P NTase activity with substrate Man-1-P, only slightly activating with substrates Glc-1-P and GlcN-1-P Pyrococcus horikoshii
2.7.7.13 Mn2+ activates Pyrococcus horikoshii
2.7.7.13 additional information absolute requirement for divalent cation Pyrococcus horikoshii
2.7.7.13 additional information the metal cofactor requirements of the multifunctional enzyme differ with the substrates used, overview Pyrococcus horikoshii
2.7.7.13 Ni2+ activates slightly Pyrococcus horikoshii
2.7.7.13 Zn2+ highly activating Pyrococcus horikoshii
2.7.7.13 Zn2+ 2 mM, about 80% of the activity with Cu2+ Pyrococcus horikoshii
2.7.7.34 Ca2+ activates Pyrococcus horikoshii
2.7.7.34 Co2+ activates Pyrococcus horikoshii
2.7.7.34 Cu2+ best activating metal ion Pyrococcus horikoshii
2.7.7.34 Mg2+ highly activates sugar-1-P NTase activity with substrate Man-1-P, only slightly activating with substrates Glc-1-P and GlcN-1-P Pyrococcus horikoshii
2.7.7.34 Mn2+ activates Pyrococcus horikoshii
2.7.7.34 additional information the metal cofactor requirements of the multifunctional enzyme differ with the substrates used, overview Pyrococcus horikoshii
2.7.7.34 Ni2+ activates slightly Pyrococcus horikoshii
2.7.7.34 Zn2+ highly activating Pyrococcus horikoshii
2.7.7.37 Ca2+ activates Pyrococcus horikoshii
2.7.7.37 Co2+ activates Pyrococcus horikoshii
2.7.7.37 Cu2+ best activating metal ion Pyrococcus horikoshii
2.7.7.37 Mg2+ highly activates sugar-1-P NTase activity with substrate Man-1-P, obly slightly activating with substrates Glc-1-P and GlcN-1-P Pyrococcus horikoshii
2.7.7.37 Mn2+ activates Pyrococcus horikoshii
2.7.7.37 additional information the metal cofactor requirements of the multifunctional enzyme differ with the substrates used, overview Pyrococcus horikoshii
2.7.7.37 Ni2+ activates slightly Pyrococcus horikoshii
2.7.7.37 Zn2+ highly activating Pyrococcus horikoshii
5.3.1.8 Ca2+ 2 mM, maximum activity Pyrococcus horikoshii
5.3.1.8 Co2+ 2 mM, about 80% of the activity with Cu2+ Pyrococcus horikoshii
5.3.1.8 Mn2+ 2 mM, about 55% of the activity with Cu2+ Pyrococcus horikoshii
5.3.1.8 additional information absolute requirement for divalent cation Pyrococcus horikoshii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.13 52900
-
 x * 52900, SDS-PAGE Pyrococcus horikoshii
5.3.1.8 52900
-
 x * 52900, SDS-PAGE Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.13 GTP + alpha-D-mannose 1-phosphate Pyrococcus horikoshii
-
 diphosphate + GDP-mannose
-
 ?
2.7.7.13 GTP + alpha-D-mannose 1-phosphate Pyrococcus horikoshii DSM 12428
-
 diphosphate + GDP-mannose
-
 ?
2.7.7.13 GTP + alpha-D-mannose 1-phosphate Pyrococcus horikoshii ATCC 700860
-
 diphosphate + GDP-mannose
-
 ?
2.7.7.13 additional information Pyrococcus horikoshii a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities ?
-
 ?
2.7.7.13 additional information Pyrococcus horikoshii DSM 12428 a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities ?
-
 ?
2.7.7.13 additional information Pyrococcus horikoshii ATCC 700860 a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities ?
-
 ?
2.7.7.34 additional information Pyrococcus horikoshii a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37 and EC 2.7.7.34, activities ?
-
 ?
2.7.7.37 GTP + alpha-D-mannose 1-phosphate Pyrococcus horikoshii
-
 diphosphate + GDP-mannose
-
 ?
2.7.7.37 additional information Pyrococcus horikoshii a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities. Substrate specificity of the sugar-1-P NTase activity of the PH0925 protein, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.13 Pyrococcus horikoshii O58649
-
-
2.7.7.13 Pyrococcus horikoshii O58649 bifunctional enzyme with phosphomannose isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
-
2.7.7.13 Pyrococcus horikoshii ATCC 700860 O58649
-
-
2.7.7.13 Pyrococcus horikoshii DSM 12428 O58649 bifunctional enzyme with phosphomannose isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
-
2.7.7.34 Pyrococcus horikoshii O58649
-
-
2.7.7.34 Pyrococcus horikoshii ATCC 700860 O58649
-
-
2.7.7.37 Pyrococcus horikoshii O58649
-
-
2.7.7.37 Pyrococcus horikoshii ATCC 700860 O58649
-
-
5.3.1.8 Pyrococcus horikoshii O58649 bifunctional enzyme with mannose-6-phosphate isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
-
5.3.1.8 Pyrococcus horikoshii DSM 12428 O58649 bifunctional enzyme with mannose-6-phosphate isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.13 recombinant His-tagged PH0925 protein from Escherichia coli strain BL21-Codon Plus(DE3)-RIL by nickel affinity chromatography Pyrococcus horikoshii
2.7.7.34 recombinant His-tagged PH0925 protein from Escherichia coli strain BL21-Codon Plus(DE3)-RIL by nickel affinity chromatography Pyrococcus horikoshii
2.7.7.37 recombinant His-tagged PH0925 protein from Escherichia coli strain BL21-Codon Plus(DE3)-RIL by nickel affinity chromatography Pyrococcus horikoshii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.7.13 0.8
-
 with ATP, CTP, or UTP and alpha-D-mannose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.13 7.3
-
 substrates GTP, alpha-D-glucosamine 1-phosphate, pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.13 8.2
-
 substrates dGTP, alpha-D-mannose 1-phosphate, pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.13 8.2
-
 with dGTP and alpha-D-mannose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.13 10.2
-
 substrates GTP, alpha-D-mannose 1-phosphate, pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.13 10.2
-
 with GTP and alpha-D-mannose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.34 0.2
-
 with dGTP and alpha-D-glucose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.34 0.5
-
 with dGTP and alpha-D-glucosamine 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.34 5.2
-
 with GTP and alpha-D-glucose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.34 7.3
-
 with GTP and alpha-D-glucosamine 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C Pyrococcus horikoshii
2.7.7.37 10.2
-
 with GTP and alpha-D-mannose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.13 ATP + alpha-D-mannose 1-phosphate about 8% of the activity with GTP Pyrococcus horikoshii diphosphate + ADP-mannose
-
 ?
2.7.7.13 CTP + alpha-D-mannose 1-phosphate about 8% of the activity with GTP Pyrococcus horikoshii diphosphate + CDP-mannose
-
 ?
2.7.7.13 dGTP + alpha-D-mannose 1-phosphate high activity Pyrococcus horikoshii diphosphate + dGDP-mannose
-
 ?
2.7.7.13 GTP + alpha-D-glucosamine 1-phosphate
-
 Pyrococcus horikoshii diphosphate + GDP-alpha-D-glucosamine
-
 ?
2.7.7.13 GTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus horikoshii diphosphate + GDP-mannose
-
 ?
2.7.7.13 GTP + alpha-D-mannose 1-phosphate best substrate Pyrococcus horikoshii diphosphate + GDP-mannose
-
 ?
2.7.7.13 GTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus horikoshii DSM 12428 diphosphate + GDP-mannose
-
 ?
2.7.7.13 GTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus horikoshii ATCC 700860 diphosphate + GDP-mannose
-
 ?
2.7.7.13 additional information enzyme can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase enzyme, e.g. PH0923. No substrates: fructose 1-phosphate, alpha-D-galactose 1-phosphate, N-acetyl-D-glucosamine 1-phosphate Pyrococcus horikoshii ?
-
 ?
2.7.7.13 additional information a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities Pyrococcus horikoshii ?
-
 ?
2.7.7.13 additional information no activity with dATP, dCTP, and dTTP, and no activity with fructose-1-phosphate, alpha-D-galactose-1-phosphate, and N-acetyl-D-glucosamine-1-phosphate Pyrococcus horikoshii ?
-
 ?
2.7.7.13 additional information enzyme can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase enzyme, e.g. PH0923. No substrates: fructose 1-phosphate, alpha-D-galactose 1-phosphate, N-acetyl-D-glucosamine 1-phosphate Pyrococcus horikoshii DSM 12428 ?
-
 ?
2.7.7.13 additional information a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities Pyrococcus horikoshii DSM 12428 ?
-
 ?
2.7.7.13 additional information no activity with dATP, dCTP, and dTTP, and no activity with fructose-1-phosphate, alpha-D-galactose-1-phosphate, and N-acetyl-D-glucosamine-1-phosphate Pyrococcus horikoshii DSM 12428 ?
-
 ?
2.7.7.13 additional information enzyme can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase enzyme, e.g. PH0923. No substrates: fructose 1-phosphate, alpha-D-galactose 1-phosphate, N-acetyl-D-glucosamine 1-phosphate Pyrococcus horikoshii ATCC 700860 ?
-
 ?
2.7.7.13 additional information a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities Pyrococcus horikoshii ATCC 700860 ?
-
 ?
2.7.7.13 additional information no activity with dATP, dCTP, and dTTP, and no activity with fructose-1-phosphate, alpha-D-galactose-1-phosphate, and N-acetyl-D-glucosamine-1-phosphate Pyrococcus horikoshii ATCC 700860 ?
-
 ?
2.7.7.13 UTP + alpha-D-mannose 1-phosphate about 8% of the activity with GTP Pyrococcus horikoshii diphosphate + UDP-mannose
-
 ?
2.7.7.34 dGTP + alpha-D-glucosamine 1-phosphate very low activity Pyrococcus horikoshii diphosphate + dGDP-glucosamine
-
 ?
2.7.7.34 dGTP + alpha-D-glucose 1-phosphate very low activity Pyrococcus horikoshii diphosphate + dGDP-glucose
-
 ?
2.7.7.34 GTP + alpha-D-glucosamine 1-phosphate best substrate Pyrococcus horikoshii diphosphate + GDP-glucosamine
-
 ?
2.7.7.34 GTP + alpha-D-glucose 1-phosphate
-
 Pyrococcus horikoshii diphosphate + GDP-glucose
-
 ?
2.7.7.34 additional information a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37 and EC 2.7.7.34, activities Pyrococcus horikoshii ?
-
 ?
2.7.7.34 additional information substrate specificity of the sugar-1-P NTase activity of the PH0925 protein, overview. No activity with fructose-1-phosphate, alpha-D-galactose-1-phosphate, and N-acetyl-D-glucosamine-1-phosphate and no activity with ATP, CTP, UTP, dATP, dCTP, and dTTP Pyrococcus horikoshii ?
-
 ?
2.7.7.37 GTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus horikoshii diphosphate + GDP-mannose
-
 ?
2.7.7.37 additional information a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities. Substrate specificity of the sugar-1-P NTase activity of the PH0925 protein, overview Pyrococcus horikoshii ?
-
 ?
2.7.7.37 additional information no activity with dATP, dCTP, and dTTP, and no activity with fructose-1-phosphate, alpha-D-galactose-1-phosphate, and N-acetyl-D-glucosamine-1-phosphate Pyrococcus horikoshii ?
-
 ?
5.3.1.8 beta-D-mannose 6-phosphate
-
 Pyrococcus horikoshii beta-D-fructose 6-phosphate
-
 ?
5.3.1.8 beta-D-mannose 6-phosphate
-
 Pyrococcus horikoshii DSM 12428 beta-D-fructose 6-phosphate
-
 ?
5.3.1.8 beta-D-mannose 6-phosphate
-
 Pyrococcus horikoshii ATCC 700860 beta-D-fructose 6-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.13 ? x * 52900, SDS-PAGE Pyrococcus horikoshii
2.7.7.13 More sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, and the C-terminal 114 residue region inhibits the Man-1-P guanylyltransferase activity. The N-terminal region plays an important role in the solubility of the entire protein and in the acquisition of the correct structure Pyrococcus horikoshii
5.3.1.8 ? x * 52900, SDS-PAGE Pyrococcus horikoshii
5.3.1.8 More mannose-6-phosphate isomerase activity is abolished by deletion of the C-terminal 14 residues. The N-terminal region plays an important role in the solubility of the entire protein and in the acquisition of the correct structure Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
2.7.7.13 Man-1-PGTase
-
 Pyrococcus horikoshii
2.7.7.13 mannose-1-phosphate guanylyltransferase
-
 Pyrococcus horikoshii
2.7.7.13 More cf. EC 2.7.7.37 and EC 2.7.7.34 Pyrococcus horikoshii
2.7.7.13 multiple sugar-1-P NTase
-
 Pyrococcus horikoshii
2.7.7.13 PH0925
-
 Pyrococcus horikoshii
2.7.7.13 PH0925 protein
-
 Pyrococcus horikoshii
2.7.7.34 Man-1-PGTase
-
 Pyrococcus horikoshii
2.7.7.34 mannose-1-phosphate guanylyltransferase
-
 Pyrococcus horikoshii
2.7.7.34 More cf. EC 2.7.7.37 and EC 2.7.7.13 Pyrococcus horikoshii
2.7.7.34 multiple sugar-1-P NTase
-
 Pyrococcus horikoshii
2.7.7.34 PH0925
-
 Pyrococcus horikoshii
2.7.7.34 PH0925 protein
-
 Pyrococcus horikoshii
2.7.7.37 More cf. EC 2.7.7.13 and EC 2.7.7.34 Pyrococcus horikoshii
2.7.7.37 multiple sugar-1-P NTase
-
 Pyrococcus horikoshii
2.7.7.37 multiple sugar-1-phosphate nucleotidylyltransferase
-
 Pyrococcus horikoshii
2.7.7.37 PH0925
-
 Pyrococcus horikoshii
2.7.7.37 PH0925 protein
-
 Pyrococcus horikoshii
2.7.7.37 sugar-1-phosphate nucleotidylyltransferase
-
 Pyrococcus horikoshii
5.3.1.8 PH0925
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.13 95
-
-
 Pyrococcus horikoshii
2.7.7.34 95
-
-
 Pyrococcus horikoshii
2.7.7.37 95
-
-
 Pyrococcus horikoshii
5.3.1.8 95
-
-
 Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.13 7.6
-
 assay at Pyrococcus horikoshii
2.7.7.34 7.6
-
 assay at Pyrococcus horikoshii
2.7.7.37 7.6
-
 assay at Pyrococcus horikoshii

General Information

EC Number General Information Comment Organism
2.7.7.13 evolution the enzyme belongs to the mannose-6-phosphate isomerase type 2 family Pyrococcus horikoshii
2.7.7.13 additional information the sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, the Man-1-P GTase activity is located in the C-terminal 114 residue region of the PH0925 protein, the phosphomannose isomerase requires the the C-terminal 14 residues Pyrococcus horikoshii
2.7.7.34 evolution the enzyme belongs to the mannose-6-phosphate isomerase type 2 family Pyrococcus horikoshii
2.7.7.34 additional information the sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, the Man-1-P GTase activity is located in the C-terminal 114 residue region of the PH0925 protein, the phosphomannose isomerase requires the the C-terminal 14 residues Pyrococcus horikoshii
2.7.7.37 evolution the enzyme belongs to the mannose-6-phosphate isomerase type 2 family Pyrococcus horikoshii
2.7.7.37 additional information the sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, the Man-1-P GTase activity is located in the C-terminal 114 residue region of the PH0925 protein, the phosphomannose isomerase requires the the C-terminal 14 residues Pyrococcus horikoshii