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Literature summary extracted from

  • Dickmanns, A.; Damerow, S.; Neumann, P.; Schulz, E.C.; Lamerz, A.C.; Routier, F.H.; Ficner, R.
    Structural basis for the broad substrate range of the UDP-sugar pyrophosphorylase from Leishmania major (2011), J. Mol. Biol., 405, 461-478.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.64 expressed as a His-tagged fusion protein Leishmania major

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.64 crystal structures of a USP in the APO-, UTP-, and UDP-sugar-bound forms is presented. The overall structure of the enzyme exhibits a significant structural homology to other nucleotidyldiphosphate-glucose pyrophosphorylases. The broad substrate specificity is strongly correlated with the flexibility of the SB-loop and, in contrast to UDP-glucose pyrophosphorylase of Leishmania major, the spacious sugar binding cavity as well as the multiple conformations observed for the residues involved in sugar moiety binding Leishmania major

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.64 additional information Leishmania major the enzyme preferentially generates UDP-glucose and UDP-galactose, but it may also activate other hexose- or pentose-1-phosphates such as galacturonic acid-1-phosphate or arabinose-1-phosphate ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.64 Leishmania major D3G6S4
-
-
2.7.7.64 no activity in Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.64 using Ni-NTA chromatography Leishmania major

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.64 additional information the enzyme preferentially generates UDP-glucose and UDP-galactose, but it may also activate other hexose- or pentose-1-phosphates such as galacturonic acid-1-phosphate or arabinose-1-phosphate Leishmania major ?
-
 ?
2.7.7.64 additional information the Leishmania major UDP-sugar pyrophosphorylase exhibits a broad substrate specificity in vitro Leishmania major ?
-
 ?
2.7.7.64 UTP + alpha-D-galactose 1-phosphate
-
 Leishmania major diphosphate + UDP-D-galactose
-
 ?
2.7.7.64 UTP + alpha-D-galacturonate 1-phosphate
-
 Leishmania major diphosphate + UDP-D-galacturonate
-
 ?
2.7.7.64 UTP + alpha-D-glucose 1-phosphate
-
 Leishmania major diphosphate + UDP-D-glucose
-
 r
2.7.7.64 UTP + alpha-L-arabinose 1-phosphate
-
 Leishmania major diphosphate + UDP-L-arabinose
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.64 More overall structure of the enzyme, structure-function analysis, overview Leishmania major

Synonyms

EC Number Synonyms Comment Organism
2.7.7.64 UDP-sugar pyrophosphorylase
-
 Leishmania major
2.7.7.64 USP
-
 Leishmania major

General Information

EC Number General Information Comment Organism
2.7.7.64 metabolism the enzyme, likely involved in monosaccharide salvage, preferentially generates UDP-glucose and UDP-galactose, but it may also activate other hexose- or pentose-1-phosphates such as galacturonic acid-1-phosphate or arabinose-1-phosphate Leishmania major
2.7.7.64 additional information active site conformations of apoenzyme and ligand-bound enzyme, substrate binding structures, structure-function analysis, modeling, overview Leishmania major