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Literature summary extracted from

  • Goncalves, S.; Borges, N.; Esteves, A.M.; Victor, B.L.; Soares, C.M.; Santos, H.; Matias, P.M.
    Structural analysis of Thermus thermophilus HB27 mannosyl-3-phosphoglycerate synthase provides evidence for a second catalytic metal ion and new insight into the retaining mechanism of glycosyltransferases (2010), J. Biol. Chem., 285, 17857-17868.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.217
-
 Thermus thermophilus HB27

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.217 the three-dimensional structure of mannosyl-3-phosphoglycerate synthase in its binary complex form, with GDP-alpha-D-mannose and Mg2+, shows a second metal binding site, about 6 A away from the mannose moiety, wild-type and H309A mutant Thermus thermophilus HB27

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.217 E251A site-directed mutagenesis, no specific activity detected Thermus thermophilus HB27
2.4.1.217 H309A site-directed mutagenesis with the absence of the metal site, negligible specific activity Thermus thermophilus HB27

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.217 Zn2+ measurement in the presence of Zn2+ (300 microM) instead Mg2+, the activity decreases about 100fold (0.4 micromol/min/mg), Zn2+ can displace Mg2+ at the second metal binding site Thermus thermophilus HB27

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.217 Mg2+ used as single metal cofactor at 20 mM, activity dependend on Thermus thermophilus HB27

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.217 Thermus thermophilus HB27 Q84B24
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.217
-
 Thermus thermophilus HB27

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 0.4
-
 with Zn2+ as a cofactor Thermus thermophilus HB27
2.4.1.217 5.3
-
 when 20 mM Mg2+ is added in combination with Zn2+ (300 microM), the MpgS specific activity recovered substantially Thermus thermophilus HB27
2.4.1.217 45
-
 with Mg2+ as a cofactor Thermus thermophilus HB27

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
-
 Thermus thermophilus HB27 GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.217 dimer
-
 Thermus thermophilus HB27

Synonyms

EC Number Synonyms Comment Organism
2.4.1.217 mannosyl-3-phosphoglycerate synthase
-
 Thermus thermophilus HB27
2.4.1.217 MPGS glycosyltransferase from the GT55 family Thermus thermophilus HB27

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.217 75
-
 assay at Thermus thermophilus HB27

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.217 7.6
-
 assay at Thermus thermophilus HB27