This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Carbohydrates Biosynthesis → Sugars Biosynthesis → Sugar Nucleotides Biosynthesis → GDP-sugar Biosynthesis|
About 50 different nucleoside diphosphate sugars have been isolated, and many of these have been shown to be intermediates in the biosynthesis of various types of complex carbohydrates [Ning00]. These substances and the enzymes involved in their synthesis, i.e., the nueleoside diphosphate sugar pyrophosphorylases, have been found in many organisms, including microorganisms, plants and animals [Danishefsky67, Nikaido68, Hassid69].
The biological synthesis of GDP-α-D-glucose was first described in 1961 in bovine mammary gland [Carlson62]. The authors found that it was synthesized from GTP and α-D-glucose 1-phosphate by the enzyme glucose-1-phosphate guanylyltransferase, which they partially purified. A similar enzyme was partially purified from human mast cell tumors [Danishefsky67]. That enzyme also had GDP-D-mannose pyrophosphorylase activity. Surprisingly, no further work has focused on this enzyme since the 1967 publication.
A dimeric GDP-D-mannose pyrophosphorylase (EC 184.108.40.206) has been purified from pig liver, and was shown to have higher activity with GDP-α-D-glucose (assayed in the reverse direction) than with GDP-α-D-mannose [Szumilo93]. The purified small subunit from that enzyme was able to catalyze the GDP-D-mannose pyrophosphorylase activity on its own, but had no activity with α-D-glucose 1-phosphate, prompting the authors to suggest that the (uncharacterized) large subunit may be responsible for the GDP-D-glucose pyrophosphorylase activity. This hypothesis has not been tested yet [Ning00].
Ning00: Ning B, Elbein AD (2000). "Cloning, expression and characterization of the pig liver GDP-mannose pyrophosphorylase. Evidence that GDP-mannose and GDP-Glc pyrophosphorylases are different proteins." Eur J Biochem 267(23);6866-74. PMID: 11082198
Szumilo93: Szumilo T, Drake RR, York JL, Elbein AD (1993). "GDP-mannose pyrophosphorylase. Purification to homogeneity, properties, and utilization to prepare photoaffinity analogs." J Biol Chem 268(24);17943-50. PMID: 7688733
Accorsi89: Accorsi A, Piatti E, Piacentini MP, Gini S, Fazi A (1989). "Isoenzymes of phosphoglucomutase from human red blood cells: isolation and kinetic properties." Prep Biochem 19(3);251-71. PMID: 2533352
Csutora05: Csutora P, Strassz A, Boldizsar F, Nemeth P, Sipos K, Aiello DP, Bedwell DM, Miseta A (2005). "Inhibition of phosphoglucomutase activity by lithium alters cellular calcium homeostasis and signaling in Saccharomyces cerevisiae." Am J Physiol Cell Physiol 289(1);C58-67. PMID: 15703203
Fu95: Fu L, Bounelis P, Dey N, Browne BL, Marchase RB, Bedwell DM (1995). "The posttranslational modification of phosphoglucomutase is regulated by galactose induction and glucose repression in Saccharomyces cerevisiae." J Bacteriol 177(11);3087-94. PMID: 7768805
Graille06: Graille M, Baltaze JP, Leulliot N, Liger D, Quevillon-Cheruel S, van Tilbeurgh H (2006). "Structure-based functional annotation: yeast ymr099c codes for a D-hexose-6-phosphate mutarotase." J Biol Chem 281(40);30175-85. PMID: 16857670
Hansen03: Hansen T, Schonheit P (2003). "ATP-dependent glucokinase from the hyperthermophilic bacterium Thermotoga maritima represents an extremely thermophilic ROK glucokinase with high substrate specificity." FEMS Microbiol Lett 226(2);405-11. PMID: 14553940
Kofler00: Kofler H, Hausler RE, Schulz B, Groner F, Flugge UI, Weber A (2000). "Molecular characterisation of a new mutant allele of the plastid phosphoglucomutase in Arabidopsis, and complementation of the mutant with the wild-type cDNA." Mol Gen Genet 263(6);978-86. PMID: 10954083
Labes07: Labes A, Schonheit P (2007). "Unusual starch degradation pathway via cyclodextrins in the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324." J Bacteriol 189(24);8901-13. PMID: 17921308
Lazarevic05: Lazarevic V, Soldo B, Medico N, Pooley H, Bron S, Karamata D (2005). "Bacillus subtilis alpha-phosphoglucomutase is required for normal cell morphology and biofilm formation." Appl Environ Microbiol 71(1);39-45. PMID: 15640167
Parche06: Parche S, Beleut M, Rezzonico E, Jacobs D, Arigoni F, Titgemeyer F, Jankovic I (2006). "Lactose-over-glucose preference in Bifidobacterium longum NCC2705: glcP, encoding a glucose transporter, is subject to lactose repression." J Bacteriol 188(4);1260-5. PMID: 16452407
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