Thermodynamic Studies of Aminoglycoside Antibiotic-Enzyme Interactions

In this manuscrip ipt, we describe thermodynamic properties of complexes formed between aminoglycoside antibiotics and the enzymes that modify these antibiotics and render them useless against infectious bacteria. Studies with three different enzymes that represent three different catalytic modifica...

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Autores principales:	Engin H. Serpersu, Can Özen, Edward Wright1
Formato:	article
Lenguaje:	EN
Publicado:	De Gruyter 2006
Materias:	Aminoglycosides Aminoglycoside-Modifying Enzymes Thermodynamics E Enzyme–Aminoglycoside C e Complexes Biochemistry QD415-436
Acceso en línea:	https://doaj.org/article/4de79093d4d84ed2b439ad76ec715b55
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id	oai:doaj.org-article:4de79093d4d84ed2b439ad76ec715b55
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spelling	oai:doaj.org-article:4de79093d4d84ed2b439ad76ec715b552021-12-02T13:03:22ZThermodynamic Studies of Aminoglycoside Antibiotic-Enzyme Interactions0250-46851303-829Xhttps://doaj.org/article/4de79093d4d84ed2b439ad76ec715b552006-06-01T00:00:00Zhttp://www.turkjbiochem.com/2006/079_085.pdfhttps://doaj.org/toc/0250-4685https://doaj.org/toc/1303-829XIn this manuscrip ipt, we describe thermodynamic properties of complexes formed between aminoglycoside antibiotics and the enzymes that modify these antibiotics and render them useless against infectious bacteria. Studies with three different enzymes that represent three different catalytic modification reactions for theseantibiotics are described. These studies revealed certain general properties of these complexes. Formation of the binary enzyme –AG complexes enthalp lpically favored and entropically disfavored. However, large exothermic enthalp lpy compensates theunfavorable entropy yielding a favorable free energy (ΔG) of binding in all cases.The presence of co-substrate increases the affinity of AGs to enzymes. A general selectivity pattern for aminoglycosides were also revealed from these studies such that the aminoglycosides with 2’-NH2 and 6’-NH2 bind to enzymes with higher affinity when compared to those with – OH at these positions.Binding-linked protonation is also observed in the formation of binary enzyme– aminoglycoside and ternary enzyme–co-substrate–AG complexes. Multiple amino groups of aminoglycosides show up-shifted pKas in enzyme–aminoglycoside complexes compared to free aminoglycosides. Determined intrinsic enthalp lpy(ΔHint) suggested that, at high pH, protonation of amino groups was the major contributor to ΔHint, however, at neutral pH contributions from protonation/ deprotonation of other functional groups were also involved. Engin H. SerpersuCan Özen,Edward Wright1De GruyterarticleAminoglycosidesAminoglycoside-Modifying EnzymesThermodynamicsEEnzyme–Aminoglycoside C e ComplexesBiochemistryQD415-436ENTürk Biyokimya Dergisi, Vol 31, Iss 2, Pp 79-85 (2006)
institution	DOAJ
collection	DOAJ
language	EN
topic	Aminoglycosides Aminoglycoside-Modifying Enzymes Thermodynamics E Enzyme–Aminoglycoside C e Complexes Biochemistry QD415-436
spellingShingle	Aminoglycosides Aminoglycoside-Modifying Enzymes Thermodynamics E Enzyme–Aminoglycoside C e Complexes Biochemistry QD415-436 Engin H. Serpersu Can Özen, Edward Wright1 Thermodynamic Studies of Aminoglycoside Antibiotic-Enzyme Interactions
description	In this manuscrip ipt, we describe thermodynamic properties of complexes formed between aminoglycoside antibiotics and the enzymes that modify these antibiotics and render them useless against infectious bacteria. Studies with three different enzymes that represent three different catalytic modification reactions for theseantibiotics are described. These studies revealed certain general properties of these complexes. Formation of the binary enzyme –AG complexes enthalp lpically favored and entropically disfavored. However, large exothermic enthalp lpy compensates theunfavorable entropy yielding a favorable free energy (ΔG) of binding in all cases.The presence of co-substrate increases the affinity of AGs to enzymes. A general selectivity pattern for aminoglycosides were also revealed from these studies such that the aminoglycosides with 2’-NH2 and 6’-NH2 bind to enzymes with higher affinity when compared to those with – OH at these positions.Binding-linked protonation is also observed in the formation of binary enzyme– aminoglycoside and ternary enzyme–co-substrate–AG complexes. Multiple amino groups of aminoglycosides show up-shifted pKas in enzyme–aminoglycoside complexes compared to free aminoglycosides. Determined intrinsic enthalp lpy(ΔHint) suggested that, at high pH, protonation of amino groups was the major contributor to ΔHint, however, at neutral pH contributions from protonation/ deprotonation of other functional groups were also involved.
format	article
author	Engin H. Serpersu Can Özen, Edward Wright1
author_facet	Engin H. Serpersu Can Özen, Edward Wright1
author_sort	Engin H. Serpersu
title	Thermodynamic Studies of Aminoglycoside Antibiotic-Enzyme Interactions
title_short	Thermodynamic Studies of Aminoglycoside Antibiotic-Enzyme Interactions
title_full	Thermodynamic Studies of Aminoglycoside Antibiotic-Enzyme Interactions
title_fullStr	Thermodynamic Studies of Aminoglycoside Antibiotic-Enzyme Interactions
title_full_unstemmed	Thermodynamic Studies of Aminoglycoside Antibiotic-Enzyme Interactions
title_sort	thermodynamic studies of aminoglycoside antibiotic-enzyme interactions
publisher	De Gruyter
publishDate	2006
url	https://doaj.org/article/4de79093d4d84ed2b439ad76ec715b55
work_keys_str_mv	AT enginhserpersu thermodynamicstudiesofaminoglycosideantibioticenzymeinteractions AT canozen thermodynamicstudiesofaminoglycosideantibioticenzymeinteractions AT edwardwright1 thermodynamicstudiesofaminoglycosideantibioticenzymeinteractions
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Thermodynamic Studies of Aminoglycoside Antibiotic-Enzyme Interactions

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