2001
DOI: 10.1128/jb.183.7.2226-2233.2001
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Functional Characterization of Alanine Racemase from Schizosaccharomyces pombe : a Eucaryotic Counterpart to Bacterial Alanine Racemase

Abstract: Schizosaccharomyces pombe has an open reading frame, which we named alr1؉ , encoding a putative protein similar to bacterial alanine racemase. We cloned the alr1 ؉ gene in Escherichia coli and purified the gene product (

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Cited by 67 publications
(46 citation statements)
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“…ArgR is thought to be translocated via the Sec pathway by cleavage of an N-terminal signal peptide. According to the physiological role of alanine racemase [31] it is assumed that also amino acid racemase plays an important role for the synthesis of d-alanine and d-glutamate in the murein layer.…”
Section: Resultsmentioning
confidence: 99%
“…ArgR is thought to be translocated via the Sec pathway by cleavage of an N-terminal signal peptide. According to the physiological role of alanine racemase [31] it is assumed that also amino acid racemase plays an important role for the synthesis of d-alanine and d-glutamate in the murein layer.…”
Section: Resultsmentioning
confidence: 99%
“…The enzyme occurs widely in bacteria and is essential in synthesis of peptidoglycan of bacterial cell walls by providing the D-enantiomer. There are some exceptions that some eukaryotes have the enzyme for biosynthesis of D-alanine-containing peptides in fungi (1,2), D-alanine metabolism in yeast (3), and osmotic regulation in a crayfish (4) and a bivalve mollusc (5). However, the peptidoglycan biosynthesis is unique to bacteria, and therefore the enzyme has been a target of antibacterial drugs (6 -10).…”
mentioning
confidence: 97%
“…Alanine racemase is ubiquitous among bacteria, but is generally absent in higher eukaryotes with some exceptions: enzymes for D-alanine metabolism in yeast (7), the muscle of black tiger prawn (8) and alfalfa seedlings (9). Structure and properties such as amino acid sequence, quaternary structure, pH-dependency and kinetic parameters of eukaryotic enzymes seem to be distinct from those of bacterial alanine racemases.…”
mentioning
confidence: 99%