Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 Å resolution

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorOliva, Glaucius
dc.creatorFontes, Marcos R.M.
dc.creatorGarratt, Richard C.
dc.creatorAltamirano, Myriam M.
dc.creatorCalcagno, Mario L.
dc.creatorHorjales, Eduardo
dc.date2014-05-27T11:18:02Z
dc.date2016-10-25T18:13:37Z
dc.date2014-05-27T11:18:02Z
dc.date2016-10-25T18:13:37Z
dc.date1995-12-01
dc.date.accessioned2017-04-06T00:46:28Z
dc.date.available2017-04-06T00:46:28Z
dc.identifierStructure, v. 3, n. 12, p. 1323-1332, 1995.
dc.identifier0969-2126
dc.identifierhttp://hdl.handle.net/11449/64662
dc.identifierhttp://acervodigital.unesp.br/handle/11449/64662
dc.identifier10.1016/S0969-2126(01)00270-2
dc.identifier2-s2.0-0029646095.pdf
dc.identifier2-s2.0-0029646095
dc.identifierhttp://dx.doi.org/10.1016/S0969-2126(01)00270-2
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/886464
dc.descriptionBackground: 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.
dc.languageeng
dc.relationStructure
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectα/β open structure
dc.subjectAldose-ketose isomerase
dc.subjectAllosteric enzyme
dc.subjectNAD-binding domain
dc.subject2 deoxy 2 aminoglucitol 6 phosphate
dc.subject2-deoxy-2-aminoglucitol-6-phosphate
dc.subjectbacterial protein
dc.subjectdrug derivative
dc.subjectenzyme inhibitor
dc.subjectepimerase
dc.subjectfructose 6 phosphate
dc.subjectfructose phosphate
dc.subjectfructose-6-phosphate
dc.subjectglucosamine
dc.subjectglucosamine 6 phosphate
dc.subjectglucosamine 6 phosphate isomerase
dc.subjectglucosamine 6-phosphate
dc.subjectglucosamine-6-phosphate isomerase
dc.subjectglucose 6 phosphate
dc.subjectglucose phosphate
dc.subjectisomerase
dc.subjectnicotinamide adenine dinucleotide
dc.subjectphosphate
dc.subjectsorbitol
dc.subjectsugar phosphate
dc.subjectallosterism
dc.subjectbinding site
dc.subjectbiosynthesis
dc.subjectcatalysis
dc.subjectchemical structure
dc.subjectchemistry
dc.subjectdrug antagonism
dc.subjectenzymology
dc.subjectEscherichia coli
dc.subjectmacromolecule
dc.subjectmetabolism
dc.subjectprotein conformation
dc.subjectX ray crystallography
dc.subjectAldose-Ketose Isomerases
dc.subjectAllosteric Regulation
dc.subjectBacterial Proteins
dc.subjectBinding Sites
dc.subjectCarbohydrate Epimerases
dc.subjectCatalysis
dc.subjectCrystallography, X-Ray
dc.subjectEnzyme Inhibitors
dc.subjectFructosephosphates
dc.subjectGlucosamine
dc.subjectGlucose-6-Phosphate
dc.subjectGlucosephosphates
dc.subjectMacromolecular Substances
dc.subjectModels, Molecular
dc.subjectNAD
dc.subjectPhosphates
dc.subjectProtein Conformation
dc.subjectSorbitol
dc.subjectSugar Phosphates
dc.subjectBacteria (microorganisms)
dc.titleStructure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 Å resolution
dc.typeOtro


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