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BioAssay: AID 287194

Activity of recombinant Saccharomyces cerevisiae homoisocitrate dehydrogenase expressed in Escherichia coli Rosetta cells

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(13)
 
 
Active(2)
 
 
Unspecified(11)
 
 
 Tested Substances
 Tested Substances
All(13)
 
 
Active(2)
 
 
Unspecified(11)
 
 
AID: 287194
Data Source: ChEMBL (435220)
BioAssay Type: Confirmatory, Concentration-Response Relationship Observed
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2010-05-25
Modify Date: 2014-05-23

Data Table ( Complete ):           View Active Data    View All Data
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..
BioActive Compounds: 2
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)
Comment
Compounds with activity <= 50uM or explicitly reported as active by ChEMBL are flagged as active in this PubChem assay presentation.

Categorized Comment
Assay Type: Binding

Assay Data Source: Scientific Literature

Assay Test Type: In vitro

BAO: Assay Format: cell-based format

Target Type: Target is a single protein chain

Result Definitions
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TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Km*Km PubChem standard valueFloatμM
2Kcat activity commentKcat activity commentString
3Kcat standard flagKcat standard flagInteger
4Kcat qualifierKcat qualifierString
5Kcat published valueKcat published valueFloat/s
6Kcat standard valueKcat standard valueFloats-1
7Km activity commentKm activity commentString
8Km standard flagKm standard flagInteger
9Km qualifierKm qualifierString
10Km published valueKm published valueFloatμM
11Km standard valueKm standard valueFloatnM

* Activity Concentration.

Data Table (Concise)
Data Table ( Complete ):     View Active Data    View All Data
Classification
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