Crosslinking of peptidoglycan by l,d‐transpeptidases allows bacteria to bypass the antibacterial activity of many betalactams as well as vancomycin. NMR studies of the Enterococcus faeciuml,d‐transpeptidase have identified the binding sites for the acyl donor and the acyl acceptor of the peptidoglycan cross‐linking reaction. For details, see the article by Triboulet et al. on pp. 90–100 of this issue.

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MOLECULAR MICROBIOLOGY, Vol. 950-382X, Iss. 1, 2015-10 ,pp. : i-i

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Acyl acceptor recognition by Enterococcus faeciuml,d‐transpeptidase Ldtfm

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MOLECULAR MICROBIOLOGY, Vol. 98, Iss. 1, 2015-10 ,pp. : 90-100

John Wiley & Sons Inc

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Gut bacteria recognize glycan substrates using cell surface glycoside hydrolases containing multiple carbohydrate binding modules (CBMs). Cockburn et al. characterized the five CBMs of a surface anchored, starch‐degrading α‐amylase of Eubacterium rectale (Amy13K) that displays high affinity for amylose corn starch as well as amylopectin and maltooligosaccharides, but little affinity for potato starch. For details, see the article by Cockburn et al. on pp. 249‐264 of this issue.

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MOLECULAR MICROBIOLOGY, Vol. 107, Iss. 2, 2018-01 ,pp. : i-i

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Time‐dependent changes in gene expression, particularly for those genes involved in adhesion and metabolism, are at the core of biofilm development. Detailed transcriptomic studies combined with a transcription factor deletion mutant library have identified several new regulators critical for Candida albicans biofilm formation. For details, see the article by Fox et al. on pp. 1226–1239 of this issue.

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MOLECULAR MICROBIOLOGY, Vol. 96, Iss. 6, 2015-06 ,pp. : i-i

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The type‐II NADH:quinone oxidoreductase (NDH‐2) from Staphylococcus aureus has been recognized as a potential target for antimicrobial therapy. Structural and biochemical studies reveal that NDH‐2 is a dimeric protein with distinct binding sites for the two substrates (NADH and quinones). Kinetic studies identify quinone reduction as the rate limiting step. For details, see the article by Sena et al. on pp. 272–288 of this issue.

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MOLECULAR MICROBIOLOGY, Vol. 950-382X, Iss. 2, 2015-10 ,pp. : i-i

John Wiley & Sons Inc

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