Metabolism of
            <scp>d</scp>
            -Serine in
            <i>Escherichia coli</i>
            K-12: Mechanism of Growth Inhibition

Cosloy, Sharon D.; McFall, Elizabeth

doi:10.1128/jb.114.2.685-694.1973

Cited by 72 publications

(45 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These enzymes often exhibit a broad specificity and can attack a number of D-amino acids, although with variable efficiency (2, 4, 8 -14). There also occur specific enzymes, such as the D-serine deaminase, which protects numerous organisms against the toxicity of D-serine (15,16).…”

mentioning

confidence: 99%

d-Tyrosyl-tRNATyr Metabolism inSaccharomyces cerevisiae

Soutourina

Blanquet

Plateau

2000

Journal of Biological Chemistry

View full text Add to dashboard Cite

The Saccharomyces cerevisiae YDL219w (DTD1) gene, which codes for an amino acid sequence sharing 34% identity with the Escherichia coli D-Tyr-tRNA(Tyr) deacylase, was cloned, and its product was functionally characterized. Overexpression in the yeast of the DTD1 gene from a multicopy plasmid increased D-Tyr-tRNA(Tyr) deacylase activity in crude extracts by two orders of magnitude. Upon disruption of the chromosomal gene, deacylase activity was decreased by more than 90%, and the sensitivity to D-tyrosine of the growth of S. cerevisiae was exacerbated. The toxicity of D-tyrosine was also enhanced under conditions of nitrogen starvation, which stimulate the uptake of D-amino acids. In relation with these behaviors, the capacity of purified S. cerevisiae tyrosyl-tRNA synthetase to produce D-Tyr-tRNA(Tyr) could be shown. Finally, the phylogenetic distribution of genes homologous to DTD1 was examined in connection with L-tyrosine prototrophy or auxotrophy. In the auxotrophs, DTD1-like genes are systematically absent. In the prototrophs, the putative occurrence of a deacylase is variable. It possibly depends on the L-tyrosine anabolic pathway adopted by the cell.

show abstract

mentioning

confidence: 99%

d-Tyrosyl-tRNATyr Metabolism inSaccharomyces cerevisiae

Soutourina

Blanquet

Plateau

2000

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…When we analyzed the sequenced genomes of staphylococci, we found that only S. saprophyticus ATCC15305 contains a homologue (SSP0432, 433 amino acids) of the D-serine deaminase DsdA of Escherichia coli (identity 54%; Metzler & Snell, 1952;McFall, 1967;Kuroda et al, 2005). DsdA is a pyridoxal phosphate-dependent enzyme (Cosloy & McFall, 1973) that degrades D-serine to ammonia and pyruvate (Dowhan & Snell, 1970), and E. coli may use D-serine as an energy source (Bloom & McFall, 1975). With concentrations of 3-115 mg mL À1 , D-serine is one of the most prevalent amino acids in mammalian urine (Huang et al, 1998) and can be found in mammalian blood as well (Pätzold et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

“…In high concentrations, it is toxic to many living organisms (Maas et al, 1995). In bacteria that do not express a D-serine deaminase, this amino acid may inhibit L-serine metabolism and synthesis of pantothenate, thereby inhibiting multiplication (Cosloy & McFall, 1973). The significance of D-serine catabolism during human uropathogenic E. coli (UPEC) infection was demonstrated by Roos & Klemm (2006).…”

Section: Introductionmentioning

confidence: 99%

The uropathogenic speciesStaphylococcus saprophyticustolerates a high concentration of d-serine

Sakιnç¹,

Michalski

Kleine

et al. 2009

FEMS Microbiology Letters

View full text Add to dashboard Cite

Human urine contains a relatively high concentration of d-serine, which is toxic to several nonuropathogenic bacteria, but can be utilized or detoxified by uropathogenic Escherichia coli (UPEC). The sequenced genome of uropathogenic Staphylococcus saprophyticus contains a gene with homology to the d-serine deaminase gene (dsdA) of UPEC. We found the gene in several clinical isolates of S. saprophyticus; however, the gene was absent in Staphylococcus xylosus and Staphylococcus cohnii, phylogenetically close relatives of S. saprophyticus, and could also not be detected in isolates of Staphylococcus aureus, Staphylococcus epidermidis and 13 other staphylococcal species. In addition, the genomes of other sequenced staphylococci do not harbor homologues of this operon. Interestingly, S. saprophyticus could grow in media supplemented with relatively high concentrations of d-serine, whereas S. aureus, S. epidermidis and other staphylococcal species could not. The association of the dsdA gene with growth in media including d-serine was proved by introducing the gene into S. aureus Newman. Given the fact that UPEC and S. saprophyticus tolerate this compound, d-serine utilization and detoxification may be a general property of uropathogenic bacteria.

show abstract

“…D-Serine deaminase (Dsdase) functions primarily as a detoxifying enzyme in Escherichia coli K-12 as the inducer. D-Serine (DS) is toxic at concentrations greater than 25 Ag/ml (3,7).Dsdase converts DS to pyruvate and NH3, allowing DS to serve as the sole source of carbon and nitrogen. Dsdase thus functions secondarily as a catabolic enzyme.…”

mentioning

confidence: 99%

“…D-Serine deaminase (Dsdase) functions primarily as a detoxifying enzyme in Escherichia coli K-12 as the inducer. D-Serine (DS) is toxic at concentrations greater than 25 Ag/ml (3,7).…”

mentioning

confidence: 99%

Isolation and characterization of D-serine deaminase constitutive mutants by utilization of D-serine as sole carbon or nitrogen source

Bloom¹,

McFall²

1975

J Bacteriol

View full text Add to dashboard Cite

Mutants constitutive for p-serine deaminase (Dsdase) synthesis were isolated by utilizing D-serine as sole nitrogen or carbon source in the chemostat. This method generated only regulatory constitutive (dsdC) mutants. The altered dsdC gene product in these strains is apparently able to bind D-serine more efficiently than the wild-type dsdC+ gene product-a selective advantage. Constitutive synthesis of Dsdase in all of these dsdC mutants is extremely sensitive to catabolite repression, and catabolite repression is reversed by the addition of D-serine. Of the 15 mutants generated by this method, none are suppressible by supD, supE, or supF. Mutations to a low level of constitutivity (maximal specific activity of 9) occur much more frequently than mutations to a high level (maximal specific activity of 79). High level constitutive synthesis of Dsdase results from the synthesis of an altered dsdC gene productnot from loss of ability to form the dsdC product. Dsdase synthesis is not regulated by the nitrogen supply in the medium, as nitrogen starvation does not result in the derepression of Dsdase synthesis. D-Serine deaminase (Dsdase) functions primarily as a detoxifying enzyme in Escherichia coli K-12 as the inducer. D-Serine (DS) is toxic at concentrations greater than 25 Ag/ml (3,7).Dsdase converts DS to pyruvate and NH3, allowing DS to serve as the sole source of carbon and nitrogen. Dsdase thus functions secondarily as a catabolic enzyme. The induced synthesis of Dsdase is subject to catabolite repression (CR); efficient induction requires cyclic adenosine 5'-monophosphate (cAMP) and the cAMP binding protein (CAP factor) as well as DS (11). The DS-dsdC regulatory gene product complex can partially replace the cAMP-CAP factor complex in promoting Dsdase synthesis (11).Six mutants constitutive for Dsdase synthesis were isolated from a dsdC+ strain by utilization of DS as sole carbon source limiting growth in the chemostat and by alternate subculture in media with DS or NH3 as sole nitrogen source. These were mapped in two regions, dsdC and dsdO, close to the structural gene for Dsdase (dsdA) (7,12). Previously isolated dsdC mutants (two) synthesize Dsdase at a low constitutive rate (7). Constitutive Dsdase synthesis is extremely sensitive to CR in these mutants and is hyperinducible in one (8) but not the other. ' Present address:

show abstract

Metabolism of d -Serine in Escherichia coli K-12: Mechanism of Growth Inhibition

Cited by 72 publications

References 18 publications

d-Tyrosyl-tRNATyr Metabolism inSaccharomyces cerevisiae

d-Tyrosyl-tRNATyr Metabolism inSaccharomyces cerevisiae

The uropathogenic speciesStaphylococcus saprophyticustolerates a high concentration of d-serine

Isolation and characterization of D-serine deaminase constitutive mutants by utilization of D-serine as sole carbon or nitrogen source

Contact Info

Product

Resources

About