Suicide substrates for the alanine racemase of Escherichia coli B

Wang, Elizabeth; Walsh, Christopher T.

doi:10.1021/bi00600a028

Cited by 177 publications

(128 citation statements)

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“…With late-stationary-phase cells grown on alanine a high level of racemase activity and a normal level of ligase activity were still present (data not shown). A molecular mass of 53-56 kDa was estimated for the inducible racemase from cells grown on L-alanine and should be compared to the values of 98 kDa and 103 kDa determined in the case of E. coli strains W and B respectively (Lambert & Neuhaus, 1972a;Wang & Walsh, 1978). The enzyme from E .…”

Section: Variations Of the Pool Levels Of Alanine D-alanyl-d-alaninementioning

confidence: 99%

“…The enzyme from E . coli B is a dimer composed of identical subunits each carrying one active site and one pyridoxal phosphate molecule (Wang & Walsh, 1978). The molecular mass of the partially purified ligase activity from cells grown in minimal or rich medium was estimated as 56-60 kDa.…”

Section: Variations Of the Pool Levels Of Alanine D-alanyl-d-alaninementioning

confidence: 99%

“…In uitro, D-cycloserine is an effective inhibitor of both the L-alanine racernase and D-alanine : D-alanine ligase activities of E. coli (Lambert & Neuhaus, 19723;Lugtenberg, 1972;Lugtenberg & van Schijndel-van Dam, 1973;Wang & Walsh, 1978). As expected, the treatment of exponential-phase cells with D-cycloserine led to a strong depletion of the D-alanyl-D-alanine pool (Table 3) , 1980).…”

Section: Eflects Of D-cycloserine and Chlorarnphenicolmentioning

confidence: 99%

“…The predominant racemase, coded by the dadX gene, is inducible by alanine and repressible by glucose (Wild et al, 1985). Homogeneous preparations of this activity were obtained from two strains of E. coli (Lambert & Neuhaus, 19723;Wang & Walsh, 1978). The other racemase, which is probably the product of the alr gene, is constitutive in respect of both alanine and * Author for correspondence.…”

Section: Introductionmentioning

confidence: 99%

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Peptidoglycan biosynthesis in Escherichia coli: variations in the metabolism of alanine and D-alanyl-D-alanine

Roubin

Mengin‐Lecreulx²,

Heijenoort³

1992

Journal of General Microbiology

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~The in uivo functioning of the alanine/D-alanyl-D-alanine pathway of Escherichia cofi was investigated by determining precursor pool levels and specific enzyme activities under various growth conditions. Cells grown on D-or L-alanine showed several remarkable features compared with cells grown on other carbon sources: 10-fold higher values of the D-alanyl-D-alanine and the UDP-MurNAc-pentapeptide pools, a 240-fold increase of the alanine racemase activity, and the absence of bacteriolysis after treatment with D-cycloserine at high concentrations (50 pg m1-l). In cells grown on glucose, D-cycloserine (1 pg ml-l) led to depletion of the D-alanyl-D-alanine pool and to lysis, which was efficiently antagonized by chloramphenicol. A threefold increase of the dipeptide pool was observed when cells were treated with chloramphenicol alone. The alanine racemase activity was lowest in glucose-grown cells and the D-alanine : D-alanine ligase and D-alanyl-D-alanhe-adding activities were the same whatever the carbon source. Molecular masses of 53-56 kDa and 5 6 4 8 kDa were estimated for the partially purified inducible alanine racemase and D-alanine: D-alanine ligase respectively.

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Section: Variations Of the Pool Levels Of Alanine D-alanyl-d-alaninementioning

confidence: 99%

Section: Variations Of the Pool Levels Of Alanine D-alanyl-d-alaninementioning

confidence: 99%

Section: Eflects Of D-cycloserine and Chlorarnphenicolmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Peptidoglycan biosynthesis in Escherichia coli: variations in the metabolism of alanine and D-alanyl-D-alanine

Roubin

Mengin‐Lecreulx²,

Heijenoort³

1992

Journal of General Microbiology

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“…6 ) They demonstrated that the antibacterial action of 3-chloroalanine was caused by the inactivation of both n-amino acid transaminase and alanine racemase. The physiological effects of both isomers of this amino acid have been investigated and demonstrated as a suicide substrate 7 ) or an inhibitor of an active transport system. 8 ) Pseudomonas putida CRI-I, which is resistant to 3-chloro-D-alanine, produces an enzyme which catalyzes an a,f1-elimination reaction of 3-chloro-D-alanine.…”

mentioning

confidence: 99%