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:||Degradation/Utilization/Assimilation → Amines and Polyamines Degradation → N-acetylglucosamine degradation|
|Degradation/Utilization/Assimilation → Secondary Metabolites Degradation → Sugar Derivatives Degradation → N-acetylglucosamine degradation|
N-acetyl-β-D-glucosamine, which is relatively abundant in nature, being a constituent of chitosan, chitin, the cell walls of fungi as well as the cell walls, capsular polysaccharides, and outer membranes of bacteria, is an excellent total source of carbon, energy and nitrogen.
In some organisms N-acetyl-β-D-glucosamine is transported into the cell by a PTS system which phosphoylates it to N-acetyl-D-glucosamine 6-phosphate (see N-acetylglucosamine degradation I). In other organisms the compound is transported by different types of transporters, without being phosphorylated. In these cases phosphorylation occurs intracellularly by the enzyme N-acetyl-D-glucosamine kinase. Following the sequential removal of its acetyl and amino groups, it enters glycolysis as β-D-fructofuranose 6-phosphate and hence flows through the pathways of central metabolism to satisfy the cell's need for precursor metabolites, reducing power, and metabolic energy [Boulanger10].
Subpathways: N-acetylglucosamine degradation I
Boulanger10: Boulanger A, Dejean G, Lautier M, Glories M, Zischek C, Arlat M, Lauber E (2010). "Identification and regulation of the N-acetylglucosamine utilization pathway of the plant pathogenic bacterium Xanthomonas campestris pv. campestris." J Bacteriol 192(6);1487-97. PMID: 20081036
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
AlvarezAnorve05: Alvarez-Anorve LI, Calcagno ML, Plumbridge J (2005). "Why does Escherichia coli grow more slowly on glucosamine than on N-acetylglucosamine? Effects of enzyme levels and allosteric activation of GlcN6P deaminase (NagB) on growth rates." J Bacteriol 187(9);2974-82. PMID: 15838023
AlvarezAnorve09: Alvarez-Anorve LI, Bustos-Jaimes I, Calcagno ML, Plumbridge J (2009). "Allosteric regulation of glucosamine-6-phosphate deaminase (NagB) and growth of Escherichia coli on glucosamine." J Bacteriol 191(20);6401-7. PMID: 19700525
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
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
Calcagno84: Calcagno M, Campos PJ, Mulliert G, Suastegui J (1984). "Purification, molecular and kinetic properties of glucosamine-6-phosphate isomerase (deaminase) from Escherichia coli." Biochim Biophys Acta 1984;787(2);165-73. PMID: 6375729
CastanoCerezo11: Castano-Cerezo S, Bernal V, Blanco-Catala J, Iborra JL, Canovas M (2011). "cAMP-CRP co-ordinates the expression of the protein acetylation pathway with central metabolism in Escherichia coli." Mol Microbiol 82(5);1110-28. PMID: 22059728
Cisneros04: Cisneros DA, Montero-Moran GM, Lara-Gonzalez S, Calcagno ML (2004). "Inversion of the allosteric response of Escherichia coli glucosamine-6-P deaminase to N-acetylglucosamine 6-P, by single amino acid replacements." Arch Biochem Biophys 421(1);77-84. PMID: 14678787
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
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