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BioAssay: AID 287200

Ratio of kcat/km of recombinant 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(13)
 
 
Unspecified(13)
 
 
 Tested Substances
 Tested Substances
All(13)
 
 
Unspecified(13)
 
 
 Related BioAssays
 Related BioAssays
AID: 287200
Data Source: ChEMBL (435226)
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
TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Kcat/Km activity commentKcat/Km activity commentString
2Kcat/Km standard flagKcat/Km standard flagInteger
3Kcat/Km qualifierKcat/Km qualifierString
4Kcat/Km published valueKcat/Km published valueFloat/s/microM
5Kcat/Km standard valueKcat/Km standard valueFloatuM-1 s-1

Data Table (Concise)
Classification
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