Dynamics and Function Relationships of Hydrolases in Organic Solvents
Dynamics and Function Relationships of Hydrolases in Organic Solvents
批准号:
7598951
负责人:
GABRIEL Luis BARLETTA
金额:
$12.54万
依托单位国家:
美国
项目类别:
财政年份:
--
资助国家:
美国
项目状态:
未结题
起止时间:
至
关键词:
AcetonitrilesAcidityActive SitesAdoptedAffectAlcoholsBindingBiologicalCatalysisComplementComputer SimulationConditionCrown EthersDataDependenceEnzyme KineticsEnzymesEstersFluorescence SpectroscopyGoalsGrantHistidineHydrolaseIncubatedKineticsLinkMeasurementMeasuresMethodsOrganic solvent productOutcomePersonal SatisfactionPlant RootsPliabilityPreparationPropertyReactionRecyclingReportingRoleScreening procedureShapesSolventsSpecificitySpectroscopy, Fourier Transform InfraredStructureSubstrate InteractionSubtilisinSubtilisinsSubtilopeptidase ASystemTechniquesThinkingTriad Acrylic Resinaqueouscatalystchemical propertydesigndesireenzyme activityenzyme mechanismenzyme structureesteraseionizationmolecular modelingpreferenceresearch studysuccesstetrahydrofuran
中文摘要
在规划生物活性有机分子的合成时越来越重要的考虑因素
是手性的引入。实现这一点的一种方法是使用手性催化剂,例如酶,
它们是高度对映性和特异性的,这一特征有助于制备靶手性手性化合物
具有药理活性的化合物。还有一个特性使这些生物催化剂对
有机化学家认为,它们的性质,如对映体选择性、前手性选择性和特异性是
由有机溶剂控制(当用作反应介质时)。奥索,酶很便宜,他们
可以“回收”,并且无毒。
不幸的是,有一些缺点限制了它们的应用和潜力。问题的根源
酶在非水介质中的催化机理还不是很清楚,
因此,通常需要一种试错法来寻找最佳的培养基、酶和条件。
本研究的目的是阐明有机溶剂影响酶的机制。
立体选择性、活性和稳定性,从而使立体选择性系统的合理设计成为可能
利用底物和溶剂的物理化学性质,以及酶的结构。我们
建议使用实验和理论相结合的方法(酶动力学,复杂
分子模拟和核磁共振方法)以了解介质在形成生物催化剂中的作用
结构、活性和立体选择性。
英文摘要
An increasingly important consideration when planning the synthesis of biological active organic molecules
is the introduction of chirality. One method to achieve this is to use a chiral catalyst, such as an enzyme,
which are highly enantiose/ective and specific, a feature that facilitates the preparation of target chirat
pharmacologically active compounds. An additional property that makes these biocatalysts attractive to the
organic chemist, is that their properties, such as enantioselectivity, prochiral selectivity and specificity are
controlled by organic solvents (when used as the reaction medium). Olso, enzymes are inexpensive, they
can be "recycled" and are non toxic.
Unfortunately there are some drawbacks that limit their applications and potential. The root of the problem
is that the mechanism of enzymatic catalysis in non-aqueous media is still not well understood, and
consequently a trial and error approach is usually needed to find the best medium, enzymes and conditions.
The goal of this study is to elucidate the mechanism by which organic solvents influence enzymatic
stereoselectivity, activity and stability, and thereby enable the rational design of stereoselective systems
using the physicochemical properties of the substrate and solvents, together with the enzyme structure. We
propose to use a combination of experimental and theoretical methods (enzyme kinetics, sophisticated
molecular-modeling and NMR methods) to understand the role of the medium in shaping a biocatalyst
structure, activity and stereoselectivity.
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负责人:GABRIEL Luis BARLETTA
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依托单位:
ACTIVITY, STABILITY, MECHANISM OF HYDROLASES
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批准号:6972463
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资助金额:$5.72万
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负责人:GABRIEL Luis BARLETTA
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依托单位:
SOLVENT DEPENDENCE OF ENZYME ENANTIOSELECTIVITY
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批准号:6579936
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项目类别:
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资助金额:$7.38万
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财政年份:2002
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依托单位:
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项目类别:
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资助金额:$25.93万
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依托单位:
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项目类别:
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资助金额:$17.0万
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财政年份:2000
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依托单位:
SOLVENT DEPENDENCE OF ENZYME ENANTIOSELECTIVITY
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批准号:6107319
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项目类别:
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资助金额:$17.0万
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财政年份:1999
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负责人:GABRIEL Luis BARLETTA
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依托单位:
IMPROVING THE USE OF ENZYMES FOR SYNTHESIS
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批准号:2024445
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项目类别:
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资助金额:$10.98万
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财政年份:1997
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负责人:GABRIEL Luis BARLETTA
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依托单位:
Dynamics and Function Relationships of Hydrolases in Organic Solvents
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批准号:7793570
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项目类别:
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资助金额:$12.88万
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财政年份:--
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负责人:GABRIEL Luis BARLETTA
-
依托单位:
Dynamics and Function Relationships of Hydrolases in Organic Solvents
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批准号:8039128
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项目类别:
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资助金额:$12.68万
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依托单位:
海外基金