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Literature summary extracted from

  • Borges, N.; Marugg, J.D.; Empadinhas, N.; da Costa, M.S.; Santos, H.
    Specialized roles of the two pathways for the synthesis of mannosylglycerate in osmoadaptation and thermoadaptation of Rhodothermus marinus (2004), J. Biol. Chem., 279, 9892-9898.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.217 additional information the isozyme involved in the two-step pathway is upregulated by osmotic stress, the isozyme involved in the one-step pathway is upregulated by heat stress Rhodothermus marinus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.217 gene mpgs, DNA and amino acid sequence determination and analysis of the 2 isozymes, expression in Escherichia coli strain BL21(DE) Rhodothermus marinus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.217 GDP 50% inhibition at 2.5 mM Rhodothermus marinus
2.4.1.217 KCl
-
 Rhodothermus marinus
2.4.1.217 additional information no inhibition by 2-(alpha-D-mannosyl)-3-phosphoglycerate or mannosylglycerate Rhodothermus marinus
2.4.1.217 NaCl
-
 Rhodothermus marinus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.217 Mg2+ required for activity Rhodothermus marinus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.217 45584
-
 x * 48795, isozyme 1, mass spectrometry, x * 45584, isozyme 2, mass spectrometry Rhodothermus marinus
2.4.1.217 48795
-
 x * 48795, isozyme 1, mass spectrometry, x * 45584, isozyme 2, mass spectrometry Rhodothermus marinus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.217 GDP-mannose + 3-phospho-D-glycerate Rhodothermus marinus 2 pathways for mannosylglycerate biosynthesis, a one-step and a two-step pathway, with specialized roles in osmoadaptation and thermoadaptation, the isozyme involved in the two-step pathway is upregulated by osmotic stress, the isozyme involved in the one-step pathway is upregulated by heat stress, regulatory mechanisms, overview GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
 ?
2.4.1.217 additional information Rhodothermus marinus the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.217 Rhodothermus marinus Q6WSQ4 gene mpgs, 2 isozymes
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.217 proteolytic modification the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide by intracellular proteases increases the activity by 10fold Rhodothermus marinus

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.217 native isozymes in a multistep procedure, recombinant isozymes from Escherichia coli by 3 chromatographic steps of cation exchange chromatography and gel filtration Rhodothermus marinus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.217 156
-
 purified enzyme lacking the 30 amino acids of the C-terminus Rhodothermus marinus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.217 GDP-mannose + 3-phospho-D-glycerate
-
 Rhodothermus marinus GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
 ?
2.4.1.217 GDP-mannose + 3-phospho-D-glycerate 2 pathways for mannosylglycerate biosynthesis, a one-step and a two-step pathway, with specialized roles in osmoadaptation and thermoadaptation, the isozyme involved in the two-step pathway is upregulated by osmotic stress, the isozyme involved in the one-step pathway is upregulated by heat stress, regulatory mechanisms, overview Rhodothermus marinus GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
 ?
2.4.1.217 additional information the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold Rhodothermus marinus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.217 ? x * 48795, isozyme 1, mass spectrometry, x * 45584, isozyme 2, mass spectrometry Rhodothermus marinus

Synonyms

EC Number Synonyms Comment Organism
2.4.1.217 MPGS
-
 Rhodothermus marinus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.217 80
-
-
 Rhodothermus marinus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.4.1.217 40 95 temperature-profile of full length and truncated enzyme Rhodothermus marinus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.217 80
-
 half-life truncated enzyme: 79 min, half-life full length enzyme: 40 min Rhodothermus marinus
2.4.1.217 100
-
 85% remaining activity of the truncated enzyme, the full length enzyme is inactive Rhodothermus marinus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.217 7.5
-
-
 Rhodothermus marinus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.217 5 10 pH-profile of full length and truncated enzyme Rhodothermus marinus