Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.64 extracted from

  • Wahl, C.; Spiertz, M.; Elling, L.
    Characterization of a new UDP-sugar pyrophosphorylase from Hordeum vulgare (barley) (2017), J. Biotechnol., 258, 51-55 .
    View publication on PubMed
Search for more literature for 2.7.7.64

Cloned(Commentary)

Cloned (Comment) Organism
gene hvusp, identified due to a BLAST search using the gene psusp from Pisum sativum as template, recombinant expression of C-terminally His-tagged enzyme best in Escherichia coli strain T7 Express, several Escherichia coli strains are tested Hordeum vulgare subsp. vulgare

Protein Variants

Protein Variants Comment Organism
additional information UDP-sugar pyrophosphorylase from Hordeum vulgare, with favorable biochemical properties like broad pH and temperature tolerances as well as a broad substrate spectrum and high synthesis stability, is used for efficient synthesis of nucleotide sugars under conditions optimized by high-through-put multiplexed capillary electrophoresis analysis in combination with a galactokinase UDP-alpha-D-galactose (UDP-Gal). Assay optimization, overview Hordeum vulgare subsp. vulgare

Inhibitors

Inhibitors Comment Organism Structure
ADP at higher concentrations above 6 mM Hordeum vulgare subsp. vulgare
ATP
-
 Hordeum vulgare subsp. vulgare
diphosphate
-
 Hordeum vulgare subsp. vulgare
EDTA complete inhibition Hordeum vulgare subsp. vulgare

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Hordeum vulgare subsp. vulgare
0.3
-
 alpha-D-galactose 1-phosphate pH 7.5, 37°C, recombinant enzyme Hordeum vulgare subsp. vulgare

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates Hordeum vulgare subsp. vulgare
Mg2+ required, activates, preferred cation Hordeum vulgare subsp. vulgare
Mn2+ activates Hordeum vulgare subsp. vulgare
additional information the enzyme requires bivalent cations for activity. HvUSP accepts other bivalent cation such as Co2+, Ni2+, Mn2+ and Zn2+, but prefers Mg2+ Hordeum vulgare subsp. vulgare
Ni2+ activates Hordeum vulgare subsp. vulgare
Zn2+ activates Hordeum vulgare subsp. vulgare

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UTP + alpha-D-galactose 1-phosphate Hordeum vulgare subsp. vulgare
-
 diphosphate + UDP-alpha-D-galactose
-
 r
UTP + alpha-D-glucose 1-phosphate Hordeum vulgare subsp. vulgare
-
 diphosphate + UDP-alpha-D-glucose
-
 r
UTP + alpha-D-glucuronate 1-phosphate Hordeum vulgare subsp. vulgare
-
 diphosphate + UDP-alpha-D-glucuronate
-
 r
UTP + D-xylose 1-phosphate Hordeum vulgare subsp. vulgare
-
 diphosphate + UDP-D-xylose
-
 ir

Organism

Organism UniProt Comment Textmining
Hordeum vulgare subsp. vulgare F2DQG9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain T7 Express by nickel affinity chromatography and ultrafiltration Hordeum vulgare subsp. vulgare

Storage Stability

Storage Stability Organism
4°C, purified recombinant His-taged enzyme, HvUSP shows a high storage stability over 31 days Hordeum vulgare subsp. vulgare

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme HvUSP has a promiscuous substrate spectrum. It is not active with ATP, CTP, GTP or dTTP, and in combination with UTP HvUSP shows conversion in decreasing order of Gal-1-P, Glc-1-P, GlcA-1-P and Xyl-1-P. No activity with mannose-1phosphate, N-acetyl-glucosamine-1-phosphate, glucosamine-1-phosphate, or fucose-1-phosphate Hordeum vulgare subsp. vulgare ?
-
-
UTP + alpha-D-galactose 1-phosphate
-
 Hordeum vulgare subsp. vulgare diphosphate + UDP-alpha-D-galactose
-
 r
UTP + alpha-D-galactose 1-phosphate preferred substrates Hordeum vulgare subsp. vulgare diphosphate + UDP-alpha-D-galactose
-
 r
UTP + alpha-D-glucose 1-phosphate
-
 Hordeum vulgare subsp. vulgare diphosphate + UDP-alpha-D-glucose
-
 r
UTP + alpha-D-glucuronate 1-phosphate
-
 Hordeum vulgare subsp. vulgare diphosphate + UDP-alpha-D-glucuronate
-
 r
UTP + D-xylose 1-phosphate
-
 Hordeum vulgare subsp. vulgare diphosphate + UDP-D-xylose
-
 ir

Subunits

Subunits Comment Organism
? x * 68700, about, sequence calculation Hordeum vulgare subsp. vulgare

Synonyms

Synonyms Comment Organism
HvUSP
-
 Hordeum vulgare subsp. vulgare
UDP-sugar pyrophosphorylase
-
 Hordeum vulgare subsp. vulgare

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Hordeum vulgare subsp. vulgare

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
35 60 50% of maximal activity within this range Hordeum vulgare subsp. vulgare

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
 purified recombinant His-taged enzyme, residual activity of HvUSP after 88 h is 46% Hordeum vulgare subsp. vulgare

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Hordeum vulgare subsp. vulgare

pH Range

pH Minimum pH Maximum Comment Organism
7 9.5 50% of maximal activity within this range Hordeum vulgare subsp. vulgare

pI Value

Organism Comment pI Value Maximum pI Value
Hordeum vulgare subsp. vulgare sequence calculation
-
 6.44

General Information

General Information Comment Organism
metabolism UDP-sugar pyrophosphorylases are involved in the plant salvage pathways Hordeum vulgare subsp. vulgare