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Literature summary for 2.7.7.9 extracted from

  • Steiner, T.; Lamerz, A.C.; Hess, P.; Breithaupt, C.; Krapp, S.; Bourenkov, G.; Huber, R.; Gerardy-Schahn, R.; Jacob, U.
    Open and closed structures of the UDP-glucose pyrophosphorylase from Leishmania major (2007), J. Biol. Chem., 282, 13003-13010.
    View publication on PubMed
Search for more literature for 2.7.7.9

Crystallization (Commentary)

Crystallization (Comment) Organism
uncomplexed apo-protein with open conformation and in complex with UDP-glucose and closed conformation. the central catalyitc domain resembles a Rossman fold and contains key residues. The C-terminal domain forms a left-handed parallel beta-helix Leishmania major

Protein Variants

Protein Variants Comment Organism
H191L no residual activity Leishmania major
H191N 0.3% of wild-type activity Leishmania major
K380D no residual activity Leishmania major
K95A 0.5% of wild-type activity Leishmania major
L281D 16.3% of wild-type activity Leishmania major

Organism

Organism UniProt Comment Textmining
Leishmania major
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.7
-
 mutant H191N, pH 7.8, 25°C Leishmania major
7.8
-
 mutant K95A, pH 7.8, 25°C Leishmania major
240
-
 mutant L281D, pH 7.8, 25°C Leishmania major
1477
-
 wild-type, pH 7.8, 25°C Leishmania major

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UTP + alpha-D-glucose 1-phosphate
-
 Leishmania major diphosphate + UDP-glucose
-
 ?