Literature summary for 2.7.7.64 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.

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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

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

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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	?	-	?
additional information	the Leishmania major UDP-sugar pyrophosphorylase exhibits a broad substrate specificity in vitro	Leishmania major	?	-	?
UTP + alpha-D-galactose 1-phosphate	-	Leishmania major	diphosphate + UDP-D-galactose	-	?
UTP + alpha-D-galacturonate 1-phosphate	-	Leishmania major	diphosphate + UDP-D-galacturonate	-	?
UTP + alpha-D-glucose 1-phosphate	-	Leishmania major	diphosphate + UDP-D-glucose	-	r
UTP + alpha-L-arabinose 1-phosphate	-	Leishmania major	diphosphate + UDP-L-arabinose	-	?

Subunits

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

Synonyms

Synonyms	Comment	Organism
UDP-sugar pyrophosphorylase	-	Leishmania major
USP	-	Leishmania major

General Information

General Information	Comment	Organism
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
additional information	active site conformations of apoenzyme and ligand-bound enzyme, substrate binding structures, structure-function analysis, modeling, overview	Leishmania major