Note: a dashed line (without arrowheads) between two compound names is meant to imply that the two names are just different instantiations of the same compound -- i.e. one may be a specific name and the other a general name, or they may both represent the same compound in different stages of a polymerization-type pathway. 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-glucopyranose 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-glucopyranose 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
Aleshin98: Aleshin AE, Zeng C, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB (1998). "The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate." Structure 6(1);39-50. PMID: 9493266
Cao02: Cao H, Shorey S, Robinson J, Metzger DL, Stewart L, Cummings E, Hegele RA (2002). "GCK and HNF1A mutations in Canadian families with maturity onset diabetes of the young (MODY)." Hum Mutat 20(6);478-9. PMID: 12442280
Colosimo96: Colosimo A, Calabrese G, Gennarelli M, Ruzzo AM, Sangiuolo F, Magnani M, Palka G, Novelli G, Dallapiccola B (1996). "Assignment of the hexokinase type 3 gene (HK3) to human chromosome band 5q35.3 by somatic cell hybrids and in situ hybridization." Cytogenet Cell Genet 74(3);187-8. PMID: 8941369
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
Fazi90: Fazi A, Piacentini MP, Piatti E, Accorsi A (1990). "Purification and partial characterization of the phosphoglucomutase isozymes from human placenta." Prep Biochem 20(3-4);219-40. PMID: 2149596
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
Furuta96: Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI (1996). "Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization." Genomics 36(1);206-9. PMID: 8812439
Glaser98: Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC (1998). "Familial hyperinsulinism caused by an activating glucokinase mutation." N Engl J Med 338(4);226-30. PMID: 9435328
Harndahl06: Harndahl L, Schmoll D, Herling AW, Agius L (2006). "The role of glucose 6-phosphate in mediating the effects of glucokinase overexpression on hepatic glucose metabolism." FEBS J 273(2);336-46. PMID: 16403021
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
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