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Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 Å resolution
  • Universidade de São Paulo (USP)
  • Univ. Nac. Auton. de México
  • Universidade Estadual Paulista (UNESP)
Background: Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and is activated by N-acetyl-D-glucosamine 6-phosphate. Mechanistically, it belongs to the group of aldose-ketose isomerases, but its reaction also accomplishes a simultaneous amination/deamination. The determination of the structure of this protein provides fundamental knowledge for understanding its mode of action and the nature of allosteric conformational changes that regulate its function. Results: The crystal structure of glucosamine 6-phosphate deaminase with bound phosphate ions is presented at 2.1 Å resolution together with the refined structures of the enzyme in complexes with its allosteric activator and with a competitive inhibitor. The protein fold can be described as a modified NAD-binding domain. Conclusions: From the similarities between the three presented structures, it is concluded that these represent the enzymatically active R state conformer. A mechanism for the deaminase reaction is proposed. It comprises steps to open the pyranose ring of the substrate and a sequence of general base-catalyzed reactions to bring about isomerization and deamination, with Asp72 playing a key role as a proton exchanger.
Issue Date: 
Structure, v. 3, n. 12, p. 1323-1332, 1995.
Time Duration: 
  • α/β open structure
  • Aldose-ketose isomerase
  • Allosteric enzyme
  • NAD-binding domain
  • 2 deoxy 2 aminoglucitol 6 phosphate
  • 2-deoxy-2-aminoglucitol-6-phosphate
  • bacterial protein
  • drug derivative
  • enzyme inhibitor
  • epimerase
  • fructose 6 phosphate
  • fructose phosphate
  • fructose-6-phosphate
  • glucosamine
  • glucosamine 6 phosphate
  • glucosamine 6 phosphate isomerase
  • glucosamine 6-phosphate
  • glucosamine-6-phosphate isomerase
  • glucose 6 phosphate
  • glucose phosphate
  • isomerase
  • nicotinamide adenine dinucleotide
  • phosphate
  • sorbitol
  • sugar phosphate
  • allosterism
  • binding site
  • biosynthesis
  • catalysis
  • chemical structure
  • chemistry
  • drug antagonism
  • enzymology
  • Escherichia coli
  • macromolecule
  • metabolism
  • protein conformation
  • X ray crystallography
  • Aldose-Ketose Isomerases
  • Allosteric Regulation
  • Bacterial Proteins
  • Binding Sites
  • Carbohydrate Epimerases
  • Catalysis
  • Crystallography, X-Ray
  • Enzyme Inhibitors
  • Fructosephosphates
  • Glucosamine
  • Glucose-6-Phosphate
  • Glucosephosphates
  • Macromolecular Substances
  • Models, Molecular
  • NAD
  • Phosphates
  • Protein Conformation
  • Sorbitol
  • Sugar Phosphates
  • Bacteria (microorganisms)
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Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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