Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Analysis of the DNA sequence upstream of the previously isolated Enterobacter cloacae UW4 ACC deaminase gene (Shah et al. 1998) suggests that this segment contains several features that are thought to be involved in the transcriptional regulation of this gene. These features include half of a CRP (cAMP receptor protein) binding site, an FNR (fumarate-nitrate reduction) regulatory protein binding site, an LRP (leucine responsive regulatory protein) binding site, and an LRP-like protein coding region. ACC deaminase activity was measured following growth of either various Escherichia coli strains carrying a plasmid that contained the Enterobacter cloacae UW4 ACC deaminase gene, or of Enterobacter cloacae UW4. Variables that were compared include aerobic versus anaerobic conditions, the presence and absence of ACC in the growth medium, addition of leucine to the medium, and bacterial strains that did or did not contain either lrp or fnr genes. The data reported are consistent with the involvement of most, if not all, of the above mentioned potential regulatory regions in the expression of ACC deaminase.
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PMID:Identification of DNA sequences that regulate the expression of the Enterobacter cloacae UW4 1-aminocyclopropane-1-carboxylic acid deaminase gene. 1114 8

The phytostimulatory alphaproteobacterium Azospirillum lipoferum 4B exhibits the plant-beneficial gene acdS, which enables deamination of the ethylene precursor 1-aminocyclopropane-1-carboxylic acid (ACC). Here, we show that acdS is in the vicinity of acdR, a homolog to leucine-responsive regulator lrp, in A. lipoferum 4B and most other acdS+ Proteobacteria. Unlike in Beta- and Gammaproteobacteria, acdS (and acdR) is preferentially located on symbiotic islands and plasmids in Alphaproteobacteria. In A. lipoferum 4B, acdS was mapped on a 750-kb plasmid that is lost during phenotypic variation, whereas other phytobeneficial genes such as nifH (associative nitrogen fixation) are maintained. In Proteobacteria, the phylogenies of acdR and acdS were largely but not totally congruent, despite physical proximity of the genes, regardless of whether DNA or deduced protein sequences were used. Potential Lrp, cAMP receptor protein (CRP) and fumarate-nitrate reduction regulator (FNR) binding sites were evidenced in the acdS promoter regions of strain 4B and most of 46 other acdS+ Proteobacteria. Indeed, transcriptional and enzymatic analyses done in vitro pointed to the involvement of Lrp- and FNR-like transcriptional up-regulation of ACC deaminase activity in A. lipoferum 4B. This is the first synteny, phylogenetic, and functional analysis of factors modulating acdS expression in Azospirillum plant growth-promoting rhizobacterium.
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PMID:Physical organization and phylogenetic analysis of acdR as leucine-responsive regulator of the 1-aminocyclopropane-1-carboxylate deaminase gene acdS in phytobeneficial Azospirillum lipoferum 4B and other Proteobacteria. 1840 7