Covering up to February 2015 Phenylglycine-type amino acids occur in a wide variety of
peptide natural products, including glycopeptide antibiotics and biologically active linear …

Tyrosine sulfation, a post-translational modification, can determine and often enhance
protein–protein interaction specificity. Sulfotyrosyl residues (sTyrs) are formed by the …

The metabolic differences between B-NHL and primary human B cells are poorly
understood. Among human B-cell non-Hodgkin lymphomas (B-NHL), primary effusion …

Glycopeptide antibiotics have long served as drugs of last resort for the treatment of
antibiotic-resistant Gram-positive bacterial infections. Resistance to the clinically relevant …

Sulfotransferases and sulfatases are the major enzymes responsible for sulfate transfer
processes. The past two years have seen the elucidation of new functions for these …

Synthetic biology offers a new path for the exploitation and improvement of natural products
to address the growing crisis in antibiotic resistance. All antibiotics in clinical use are facing …

The luciferin sulfokinase (coelenterazine sulfotransferase) of Renilla was previously
reported to activate the storage form, luciferyl sulfate (coelenterazine sulfate) to luciferin …

There is a considerable interest in the modification of existing antibiotics to generate new
antimicrobials. Glycopeptide antibiotics (GPAs) are effective against serious Gram-positive …

Sulfotransferases are involved in a variety of physiological processes and typically use 3′-
phosphoadenosine 5′-phosphosulfate (PAPS) as the sulfate donor substrate. In contrast …

Nearly 50 naturally occurring carbapenem β‐lactam antibiotics, most produced by
Streptomyces, have been identified. The structural diversity of these compounds is limited to …