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Literature summary for 2.7.7.13 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
Search for more literature for 2.7.7.13

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
EDTA complete inhibition Pyrococcus horikoshii
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0026
-
 GTP pH 7.6, 85°C Pyrococcus horikoshii
0.0026
-
 GTP pH 7.6, 85°C, recombinant enzyme Pyrococcus horikoshii
0.0161
-
 alpha-D-mannose 1-phosphate pH 7.6, 85°C Pyrococcus horikoshii
0.0161
-
 alpha-D-mannose 1-phosphate pH 7.6, 85°C, recombinant enzyme Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Pyrococcus horikoshii
Ca2+ 2 mM, about 50% of the activity with Cu2+ Pyrococcus horikoshii
Co2+ activates Pyrococcus horikoshii
Cu2+ best activating metal ion Pyrococcus horikoshii
Cu2+ 2 mM, maximum activity Pyrococcus horikoshii
Mg2+ 2 mM, about 80% of the activity with Cu2+ Pyrococcus horikoshii
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
Mn2+ activates Pyrococcus horikoshii
additional information absolute requirement for divalent cation Pyrococcus horikoshii
additional information the metal cofactor requirements of the multifunctional enzyme differ with the substrates used, overview Pyrococcus horikoshii
Ni2+ activates slightly Pyrococcus horikoshii
Zn2+ highly activating Pyrococcus horikoshii
Zn2+ 2 mM, about 80% of the activity with Cu2+ Pyrococcus horikoshii

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + alpha-D-mannose 1-phosphate Pyrococcus horikoshii
-
 diphosphate + GDP-mannose
-
 ?
GTP + alpha-D-mannose 1-phosphate Pyrococcus horikoshii DSM 12428
-
 diphosphate + GDP-mannose
-
 ?
GTP + alpha-D-mannose 1-phosphate Pyrococcus horikoshii ATCC 700860
-
 diphosphate + GDP-mannose
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58649
-
-
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
-
Pyrococcus horikoshii ATCC 700860 O58649
-
-
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
-

Purification (Commentary)

Purification (Comment) Organism
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]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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
7.3
-
 substrates GTP, alpha-D-glucosamine 1-phosphate, pH 7.6, 85°C Pyrococcus horikoshii
8.2
-
 substrates dGTP, alpha-D-mannose 1-phosphate, pH 7.6, 85°C Pyrococcus horikoshii
8.2
-
 with dGTP and alpha-D-mannose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C Pyrococcus horikoshii
10.2
-
 substrates GTP, alpha-D-mannose 1-phosphate, pH 7.6, 85°C Pyrococcus horikoshii
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + alpha-D-mannose 1-phosphate about 8% of the activity with GTP Pyrococcus horikoshii diphosphate + ADP-mannose
-
 ?
CTP + alpha-D-mannose 1-phosphate about 8% of the activity with GTP Pyrococcus horikoshii diphosphate + CDP-mannose
-
 ?
dGTP + alpha-D-mannose 1-phosphate high activity Pyrococcus horikoshii diphosphate + dGDP-mannose
-
 ?
GTP + alpha-D-glucosamine 1-phosphate
-
 Pyrococcus horikoshii diphosphate + GDP-alpha-D-glucosamine
-
 ?
GTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus horikoshii diphosphate + GDP-mannose
-
 ?
GTP + alpha-D-mannose 1-phosphate best substrate Pyrococcus horikoshii diphosphate + GDP-mannose
-
 ?
GTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus horikoshii DSM 12428 diphosphate + GDP-mannose
-
 ?
GTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus horikoshii ATCC 700860 diphosphate + GDP-mannose
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
UTP + alpha-D-mannose 1-phosphate about 8% of the activity with GTP Pyrococcus horikoshii diphosphate + UDP-mannose
-
 ?

Subunits

Subunits Comment Organism
? x * 52900, SDS-PAGE Pyrococcus horikoshii
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

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
95
-
-
 Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Pyrococcus horikoshii

General Information

General Information Comment Organism
evolution the enzyme belongs to the mannose-6-phosphate isomerase type 2 family Pyrococcus horikoshii
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