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Literature summary for 2.4.1.217 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)

Cloned (Comment) Organism
-
Thermus thermophilus HB27

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Inhibitors

Inhibitors Comment Organism Structure
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

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

Organism

Organism UniProt Comment Textmining
Thermus thermophilus HB27 Q84B24
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermus thermophilus HB27

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.4
-
with Zn2+ as a cofactor Thermus thermophilus HB27
5.3
-
when 20 mM Mg2+ is added in combination with Zn2+ (300 microM), the MpgS specific activity recovered substantially Thermus thermophilus HB27
45
-
with Mg2+ as a cofactor Thermus thermophilus HB27

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP-mannose + 3-phospho-D-glycerate
-
Thermus thermophilus HB27 GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
?

Subunits

Subunits Comment Organism
dimer
-
Thermus thermophilus HB27

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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