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 → Amines and Polyamines Biosynthesis → UDP-N-acetyl-D-galactosamine Biosynthesis|
|Biosynthesis → Cell Structures Biosynthesis → Cell Wall Biosynthesis|
Some taxa known to possess this pathway include : Giardia intestinalis
Expected Taxonomic Range: Giardiinae
The protozoan parasite Giardia intestinalis (synonyms Giardia lamblia, Giardia duodenalis) is a common cause of enteric disease (giardiasis) in humans and other mammals, worldwide. Its life cycle consists of two stages, a flagellated trophozoite that replicates in the host, and a dormant cyst stage in which the organism is transmitted. Encystment is induced in response to bile in the gastrointestinal tract.
The outer cyst wall is rich in a homopolymer of (β1->3)-N-acetyl-D-galactosamine residues that is biosynthesized from a UDP-N-acetyl-D-galactosamine precursor. This pathway describes the biosynthesis of this precursor, which is derived from endogenous glucose that is converted to fructose-6-phosphate by glycolytic enzymes.
UDP-N-acetyl-D-galactosamine is converted to the homopolymer by cyst wall synthase [Karr04]. The last five enzymes of the pathway are transcriptionally activated when trophozoites are induced to encyst. Their activities greatly increase during encystment. In [Lopez07, Mok05, Mok05a, Sener04, Lopez03b, Bulik00].
Bulik00: Bulik DA, van Ophem P, Manning JM, Shen Z, Newburg DS, Jarroll EL (2000). "UDP-N-acetylglucosamine pyrophosphorylase, a key enzyme in encysting Giardia, is allosterically regulated." J Biol Chem 275(19);14722-8. PMID: 10799561
Jarroll01: Jarroll EL, Macechko PT, Steimle PA, Bulik D, Karr CD, van Keulen H, Paget TA, Gerwig G, Kamerling J, Vliegenthart J, Erlandsen S (2001). "Regulation of carbohydrate metabolism during Giardia encystment." J Eukaryot Microbiol 48(1);22-6. PMID: 11249189
Karr04: Karr CD, Jarroll EL (2004). "Cyst wall synthase: N-acetylgalactosaminyltransferase activity is induced to form the novel N-acetylgalactosamine polysaccharide in the Giardia cyst wall." Microbiology 150(Pt 5);1237-43. PMID: 15133086
Lopez03b: Lopez AB, Sener K, Jarroll EL, van Keulen H (2003). "Transcription regulation is demonstrated for five key enzymes in Giardia intestinalis cyst wall polysaccharide biosynthesis." Mol Biochem Parasitol 128(1);51-7. PMID: 12706796
Lopez07: Lopez AB, Sener K, Trosien J, Jarroll EL, VAN Keulen H (2007). "UDP-N-Acetylglucosamine 4'-Epimerase from the Intestinal Protozoan Giardia Intestinalis Lacks UDP-Glucose 4'-Epimerase Activity." J Eukaryot Microbiol 54(2);154-60. PMID: 17403156
Macechko92: Macechko PT, Steimle PA, Lindmark DG, Erlandsen SL, Jarroll EL (1992). "Galactosamine-synthesizing enzymes are induced when Giardia encyst." Mol Biochem Parasitol 56(2);301-9. PMID: 1484552
Mok05: Mok MT, Edwards MR (2005). "Kinetic and physical characterization of the inducible UDP-N-acetylglucosamine pyrophosphorylase from Giardia intestinalis." J Biol Chem 280(47);39363-72. PMID: 16169849
Mok05a: Mok MT, Tay E, Sekyere E, Glenn WK, Bagnara AS, Edwards MR (2005). "Giardia intestinalis: molecular characterization of UDP-N-acetylglucosamine pyrophosphorylase." Gene 357(1);73-82. PMID: 15951138
Altamirano87: Altamirano MM, Mulliert G, Calcagno M (1987). "Sulfhydryl groups of glucosamine-6-phosphate isomerase deaminase from Escherichia coli." Arch Biochem Biophys 1987;258(1);95-100. PMID: 2821923
Altamirano90: Altamirano MM, Calcagno M (1990). "Zinc binding and its trapping by allosteric transition in glucosamine-6-phosphate deaminase from Escherichia coli." Biochim Biophys Acta 1038(3);291-4. PMID: 2111170
Altamirano92: Altamirano MM, Plumbridge JA, Calcagno ML (1992). "Identification of two cysteine residues forming a pair of vicinal thiols in glucosamine-6-phosphate deaminase from Escherichia coli and a study of their functional role by site-directed mutagenesis." Biochemistry 31(4);1153-8. PMID: 1734962
Altamirano93: Altamirano MM, Plumbridge JA, Barba HA, Calcagno ML (1993). "Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides." Biochem J 295 ( Pt 3);645-8. PMID: 8240271
Altamirano94: Altamirano MM, Hernandez-Arana A, Tello-Solis S, Calcagno ML (1994). "Spectrochemical evidence for the presence of a tyrosine residue in the allosteric site of glucosamine-6-phosphate deaminase from Escherichia coli." Eur J Biochem 1994;220(2);409-13. PMID: 8125098
Altamirano95: Altamirano MM, Plumbridge JA, Horjales E, Calcagno ML (1995). "Asymmetric allosteric activation of Escherichia coli glucosamine-6-phosphate deaminase produced by replacements of Tyr 121." Biochemistry 34(18);6074-82. PMID: 7742311
Bassler91: Bassler BL, Yu C, Lee YC, Roseman S (1991). "Chitin utilization by marine bacteria. Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii." J Biol Chem 266(36);24276-86. PMID: 1761533
Baveja86: Baveja UK, Jyoti AS, Kaur M, Agarwal DS, Anand BS, Nanda R (1986). "Isoenzyme studies of Giardia lamblia isolated from symptomatic cases." Aust J Exp Biol Med Sci 64 ( Pt 2);119-26. PMID: 2943257
Bernatchez05: Bernatchez S, Szymanski CM, Ishiyama N, Li J, Jarrell HC, Lau PC, Berghuis AM, Young NM, Wakarchuk WW (2005). "A single bifunctional UDP-GlcNAc/Glc 4-epimerase supports the synthesis of three cell surface glycoconjugates in Campylobacter jejuni." J Biol Chem 280(6);4792-802. PMID: 15509570
Boehmelt00: Boehmelt G, Fialka I, Brothers G, McGinley MD, Patterson SD, Mo R, Hui CC, Chung S, Huber LA, Mak TW, Iscove NN (2000). "Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association." J Biol Chem 275(17);12821-32. PMID: 10777580
Brown99: Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y (1999). "Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily." EMBO J 18(15);4096-107. PMID: 10428949
Bulik98: Bulik DA, Lindmark DG, Jarroll EL (1998). "Purification and characterization of UDP-N-acetylglucosamine pyrophosphorylase from encysting Giardia." Mol Biochem Parasitol 95(1);135-9. PMID: 9763295
BustosJaimes01: Bustos-Jaimes I, Calcagno ML (2001). "Allosteric transition and substrate binding are entropy-driven in glucosamine-6-phosphate deaminase from Escherichia coli." Arch Biochem Biophys 394(2);156-60. PMID: 11594728
BustosJaimes02: Bustos-Jaimes I, Sosa-Peinado A, Rudino-Pinera E, Horjales E, Calcagno ML (2002). "On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase." J Mol Biol 319(1);183-9. PMID: 12051945
BustosJaimes05: Bustos-Jaimes I, Ramirez-Costa M, De Anda-Aguilar L, Hinojosa-Ocana P, Calcagno ML (2005). "Evidence for two different mechanisms triggering the change in quaternary structure of the allosteric enzyme, glucosamine-6-phosphate deaminase." Biochemistry 44(4);1127-35. PMID: 15667206
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