Synthesis Of Cystathionine And Its Control In Salmonella Typhimurium

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Surface-exposed Tryptophan Residues Are Essential for O

tryptophan synthase, cystathionine -synthase, and threonine dehydratase. Depending on the subcellular compartment and on the growth conditions, many isoforms of OASS have been described (1, 2). In Salmonella typhimurium, the OASS-A iso-form is responsible for the synthesis of L-cysteine from sulfide and O-acetylserine (OAS). Catalysis follows a

Methionine Synthesis in Lemnal - JSTOR Home

tathionine y-synthase of Salmonella typhimurium (7). Datko and Mudd (5) recently demonstrated that PAG can inhibit the growth of Lemna paucicostata, with concomitant cessation of the flux of radioactive sulfur from cysteine into cystathionine and its sulfur-containing products. The growth inhibition could be prevented by methionine.

Methionine production by fermentation

control mechanisms for methionine biosynthesis are examined. The importance of fermentation media composition and culture conditions for methionine production is assessed and methods for


Salmonella typhimurium (13). Inhibition of the growth of the latter organism is overcome by addition to the medium of methionine or homocysteine, but not of serine, homoserine, or cystathionine. Available evidence (1) indicates that Salmonella 1 Present address: South Carolina State College, Post Office Box 1706, Orangeburg, S. C. 29115.

min, Ap - PNAS

the regulation of methionine biosynthesis in S. typhimurium (5). Tofurther investigate whether cystathionine is required for induction of cystathionase or SAMsynthetase, a strain which is unable to make cystathionine but has the wild typemetJallelewasused.Enzymeactivitiesweremeasuredin HfrC (metB-metJ+)whichhadbeengrownonmediasupple-

Regulation of Branched Biosynthetic Pathways in Bacteria

cystathionine. Hydrolysis of the thio-ether linkage of cystathionine and sub-sequent methylation of the sulfhydryl group yields methionine. It should be pointed out that cysteine per se is not a direct intermediate in bacterial me-thionine biosynthesis, but rather is the terminal metabolite of a separate bio-synthetic pathway; cysteine donates its

Small RNAs of Pathogenic Bacteria: Not Small Enough to be

18 RNAs of Pathogenic Bacteria Mol Cell Pharmacol 2012;4(1):17-30. 80-100 sRNA species have been reported in Escherichia coli genome. Other species of bacteria seem to possess more number of sRNAs.

Biosynthesis of the Branched-Chain Amino Acids

bonds would occur in the cell, it may be that the enzyme was oxidized during its purification. That this problem has not arisen with the enzyme from the K-12 strain of E. coli may be because 1 of the 30 amino acid differences between the two enzymes is the presence of an extra cysteine residue in the S. typhimurium enzyme (118).

Role of Homocysteine metR-Mediated Activation metE and metH

metHGenes in Salmonella typhimurium andEscherichia coli MARKL. URBANOWSKIANDGEORGEV. STAUFFER* Department ofMicrobiology, University ofIowa, Iowa City, Iowa52242 Received 3 January 1989/Accepted 14 March 1989 The metR-mediated activation of the Salmonella typhimurium metE and metH genes was shown to be

Influence Methionine Biosynthesis Serine

and methionine synthesis in Salmonella typhimurium appears to be due to either analtered S-adenosylmethionine synthetase or alteredS-adenosylme-thionine pools. The pathways for glycine and methionine synthesisareconnected,withthemethylgroup for methionine synthesis coming from serine

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serine by cell -free extracts of Escherichia and Salmonella typhimurium has been found which condenses with cysteine to form cystathionine. Feedback inhibition and repression by methionine has been demonstrated for some of the enzymes responsible for this synthesis (Rowbury, 1962b, 1964a; Rowbury and Woods, 1964b).


3.1 Synthesis of Cysteine from Sulfide or Thiosulfate teine to cysteine via a cystathionine intermediate. Homocysteine is synthe- Salmonella typhimurium. This sulfate transporter consists

Bacterial Pathogens Hijack the Innate Immune Response by

phage response and function is unknown. We show that the enzyme cystathionine-lyase (CTH) is induced in macrophages infected with pathogenic bacteria through signaling involving phosphatidylinositol 3-kinase (PI3K)/MTOR and the transcription factor SP1. This results in the synthesis of cystathionine, which facilitates the survival

Identification and Functional Analysis of Escherichia coli

as Salmonella enterica serovar Typhimurium (6, 17) and E. coli (2, 11). In E. coli, cystathionine lyase (CBL) (17) encoded by metC, which catalyzes mainly the conversion of cystathionine to homocysteine, pyruvate, and ammonia (9), as well as tryp-tophanase (TNase) encoded by tnaA, which primarily degrades

Homocysteine Biosynthesis in Green Plants

tivity of cystathionine y-synthase with various substrates were extended to a number of lower organisms. The pat- terns of substrate activity with crude extracts of a blue-green alga and Escherichia coli are very similar, and resemble the pattern for cystathionine y-synthase of Salmonella typh-