dihydroxy-acid dehydratase (2,3-dihydroxy-3-methylbutanoate, 2,3-dihydroxy-3-methylpentanoate)
function
biosynthesis of branched-chain amino acids
product
dihydroxy-acid dehydratase
(2,3-dihydroxy-3-methylbutanoate,
2,3-dihydroxy-3-methylpentanoate)
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.3|Amino acid/ nitrogen metabolism] → [category|SW 2.3.1|Biosynthesis/ acquisition of amino acids] → [category|SW 2.3.1.12|Biosynthesis/ acquisition of branched-chain amino acids][SW|Categories] containing this gene/protein
[SW|biosynthesis/ acquisition of amino acids], [SW|most abundant proteins]This gene is a member of the following [SW|regulons]
[SW|CodY regulon]Gene
Coordinates on the chromosome (coding sequence)
2,300,762 -> 2,302,438
The protein
Catalyzed reaction/ biological activity
2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate H2O (according to Swiss-Prot) Structure
[PDB|2GP4] (apo form of 6-phosphogluconate dehydratase from ''Shewanella oneidensis'', 33% identity)Expression and Regulation
Operon
''[protein|search|ilvD]'' [Pubmed|15060025]Regulation
repressed by casamino acids [Pubmed|12107147]repressed during growth in the presence of branched chain amino acids ([protein|search|CodY]) [Pubmed|12618455]Regulatory mechanism
[protein|search|CodY]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed1] [http://www.ncbi.nlm.nih.gov/sites/entrez/18083814 PubMed2]Additional information
belongs to the 100 [[most abundant proteins]] [PubMed|15378759]the terminator is inhibited by [protein|search|NusA] [ http://www.nature.com/articles/nmicrobiol20157 Reference]Biological materials
lacZ fusion
pGP522 (in [protein|search|pAC5]), pGP235 (in [protein|search|pAC5]), both available in [SW|Jörg Stülke]'s lab; a series of promoter deletions in [protein|search|pAC6] is available in [SW|Jörg Stülke]'s labReferences
18083814,12618455,15060025,12107147,24163341,15378759,26220295 
