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,
就是引入手性。实现这一点的一种方法是使用手性催化剂,如酶,
其是高度对映体/有效的和特异的,这一特征有利于目标手性化合物的制备,
生物活性化合物。使这些生物催化剂对生物催化剂有吸引力的另一个特性是,
有机化学家,是他们的性质,如对映选择性,前手性选择性和特异性,
由有机溶剂控制(当用作反应介质时)。另外,酶很便宜,
可以被“回收”并且无毒。
然而,它的一些缺点限制了它的应用和潜力。问题的根源
在非水介质中酶催化的机制仍然没有很好地理解,
因此,通常需要试错法来找到最佳培养基、酶和条件。
本研究的目的是阐明有机溶剂影响酶促反应的机制,
立体选择性,活性和稳定性,从而能够合理设计立体选择性系统
使用底物和溶剂的物理化学性质以及酶结构。我们
建议使用实验和理论方法(酶动力学,复杂的
分子建模和NMR方法)来理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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批准号:7610156
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批准号:7170784
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资助金额:$21.35万
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财政年份:2005
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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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项目类别:
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资助金额:$5.72万
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财政年份:2004
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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
-
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:
SOLVENT DEPENDENCE OF ENZYME ENANTIOSELECTIVITY
-
批准号:6437020
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项目类别:
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资助金额:$25.93万
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财政年份:2001
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负责人:GABRIEL Luis BARLETTA
-
依托单位:
SOLVENT DEPENDENCE OF ENZYME ENANTIOSELECTIVITY
-
批准号:6301710
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项目类别:
-
资助金额:$17.0万
-
财政年份:2000
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负责人:GABRIEL Luis BARLETTA
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依托单位:
SOLVENT DEPENDENCE OF ENZYME ENANTIOSELECTIVITY
-
批准号:6107319
-
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:
-
资助金额:$12.88万
-
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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财政年份:--
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负责人:GABRIEL Luis BARLETTA
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依托单位:
海外基金