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BioAssay: AID 287198

Inhibition of Saccharomyces cerevisiae homoisocitrate dehydrogenase expressed in Escherichia coli Rosetta cells above 10 mM

Homoisocitrate dehydrogenase is involved in the alpha-aminoadipate pathway of biosynthesis of l-lysine in fungi, yeast, some prokaryotic bacteria, and archaea. This enzyme catalyzes the oxidative decarboxylation of (2R,3S)-homoisocitrate into 2-oxoadipate using NAD(+) as a coenzyme. Substrate specificity of two homoisocitrate dehydrogenases derived from Deinococcus radiodurans and Saccharomyces more ..
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 Tested Compounds
 Tested Compounds
All(5)
 
 
Inconclusive(1)
 
 
Unspecified(4)
 
 
 Tested Substances
 Tested Substances
All(5)
 
 
Inconclusive(1)
 
 
Unspecified(4)
 
 
 Related BioAssays
 Related BioAssays
AID: 287198
Data Source: ChEMBL (435224)
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2010-05-25
Modify Date: 2013-11-19

Data Table ( Complete ):           All
Target
Sequence: RecName: Full=Homoisocitrate dehydrogenase, mitochondrial; Short=HIcDH; Flags: Precursor
Description ..   
Protein Family: LeuB
Comment ..   

Gene:LYS12     Related Protein 3D Structures     More BioActivity Data..
Tested Compounds:
Description:
Title: Substrate specificity analysis and inhibitor design of homoisocitrate dehydrogenase.

Abstract: Homoisocitrate dehydrogenase is involved in the alpha-aminoadipate pathway of biosynthesis of l-lysine in fungi, yeast, some prokaryotic bacteria, and archaea. This enzyme catalyzes the oxidative decarboxylation of (2R,3S)-homoisocitrate into 2-oxoadipate using NAD(+) as a coenzyme. Substrate specificity of two homoisocitrate dehydrogenases derived from Deinococcus radiodurans and Saccharomyces cerevisiae was analyzed using a series of synthetic substrate analogs, which indicated a relatively broad substrate specificity of these enzymes. Based on the substrate specificity, 3-hydroxyalkylidene- and 3-carboxyalkylidenemalate derivatives were designed as a specific inhibitor for homoisocitrate dehydrogenase. The synthetic inhibitors showed a moderate competitive inhibitory activity and (R,Z)-3-carboxypropylidenemalate was the most inhibitory among the synthesized inhibitors. Therefore, homoisocitrate dehydrogenase appeared to recognize preferentially an extended conformation of homoisocitrate.
(PMID: 17116397)
Categorized Comment
ChEMBL Assay Type: Binding

ChEMBL Assay Data Source: Scientific Literature

ChEMBL Target ID: 102958

ChEMBL Target Type: Target is a single protein chain

Result Definitions
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TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Ki*Ki PubChem standard valueFloatμM
2BEIBinding Efficiency Index(nM)Float
3SEISurface Efficiency Index(nM)Float
4LELigand EfficiencyFloat
5LLELipophilic Ligand EfficiencyFloat
6Ki activity commentKi activity commentString
7Ki standard flagKi standard flagInteger
8Ki qualifierKi qualifierString
9Ki published valueKi published valueFloatμM
10Ki standard valueKi standard valueFloatnM
11Ki data validityKi data validityString

* Activity Concentration.

Data Table (Concise)
Classification
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