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Literature summary for 2.7.7.37 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 2.7.7.37

Cloned(Commentary)

Cloned (Comment) Organism
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 phosphomannose isomerase 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, recombinant enzyme 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
Co2+ activates Pyrococcus horikoshii
Cu2+ best activating metal ion Pyrococcus horikoshii
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
Mn2+ activates 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

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
-
 ?
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

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

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
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.
GTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus horikoshii diphosphate + GDP-mannose
-
 ?
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 ?
-
 ?
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 ?
-
 ?

Synonyms

Synonyms Comment Organism
More cf. EC 2.7.7.13 and EC 2.7.7.34 Pyrococcus horikoshii
multiple sugar-1-P NTase
-
 Pyrococcus horikoshii
multiple sugar-1-phosphate nucleotidylyltransferase
-
 Pyrococcus horikoshii
PH0925
-
 Pyrococcus horikoshii
PH0925 protein
-
 Pyrococcus horikoshii
sugar-1-phosphate nucleotidylyltransferase
-
 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