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- W2010796770 abstract "The zinc complex Tp∗ZnOH (1:Tp∗ = hydrotris-(3-cumyl,5-methyl-pyrazolyl)borate) which is a model of hydrolytic zinc enzymes was reacted with hydroxamic acids and hydroxyketones. Two hydroxamates Tp∗Zn-Hya (2: Hya = acetohydroxamate, 3: Hya = 2-hydroxamato-4-methylpentanoyl-alanyl-glycylamide) and two ketoalcoholates Tp∗Zn-Kea (4: Kea = hydroxyacetonate, 5: Kea = cumoylacetonate) were obtained. Crystal structure determinations of 2, 3 and 5 have revealed distorted ZnN3O2 coordinations in each case. The immediate environment of the zinc ion in the hydroxamates closely resembles that in enzyme-(hydroxamate)inhibitor complexes of zinc-containing metalloproteases like collagenases and thermolysin or of class II aldolases like fuculose-1-phoshate aldolase. Like in the enzymes the hydroxamates and the ketoalcoholates can serve as transition state analogues of the enzyme-catalysed reactions." @default.
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- W2010796770 date "1996-09-01" @default.
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- W2010796770 title "Modelling transition state analogues and enzyme-inhibitor complexes of zinc-containing class II aldolases and metalloproteases" @default.
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- W2010796770 doi "https://doi.org/10.1016/s0020-1693(96)05236-x" @default.
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