Sulfatases: structure, mechanism, biological activity, inhibition, and synthetic utility

SR Hanson, MD Best, CH Wong - … Chemie International Edition, 2004 - Wiley Online Library
Sulfatases, which cleave sulfate esters in biological systems, play a key role in regulating
the sulfation states that determine the function of many physiological molecules. Sulfatase …

Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications

MJ Appel, CR Bertozzi - ACS chemical biology, 2015 - ACS Publications
Formylglycine (fGly) is a catalytically essential residue found almost exclusively in the active
sites of type I sulfatases. Formed by post-translational oxidation of cysteine or serine side …

Meta-analysis of heavy metal effects on soil enzyme activities

H Aponte, P Meli, B Butler, J Paolini, F Matus… - Science of the Total …, 2020 - Elsevier
Enzyme activities (EAs) respond to contamination in several ways depending on the
chemical form and content of heavy metals and metalloids (HMs) and their interactions with …

One in a million: flow cytometric sorting of single cell-lysate assays in monodisperse picolitre double emulsion droplets for directed evolution

A Zinchenko, SRA Devenish, B Kintses… - Analytical …, 2014 - ACS Publications
Directed evolution relies on iterative cycles of randomization and selection. The outcome of
an artificial evolution experiment is crucially dependent on (i) the numbers of variants that …

[HTML][HTML] Multiple sulfatase deficiency is caused by mutations in the gene encoding the human Cα-formylglycine generating enzyme

T Dierks, B Schmidt, LV Borissenko, J Peng… - Cell, 2003 - cell.com
C α-formylglycine (FGly) is the catalytic residue in the active site of eukaryotic sulfatases. It is
posttranslationally generated from a cysteine in the endoplasmic reticulum. The genetic …

Picoliter cell lysate assays in microfluidic droplet compartments for directed enzyme evolution

B Kintses, C Hein, MF Mohamed, M Fischlechner… - Chemistry & Biology, 2012 - cell.com
We demonstrate the utility of a microfluidic platform in which water-in-oil droplet
compartments serve to miniaturize cell lysate assays by a million-fold for directed enzyme …

Matching the diversity of sulfated biomolecules: creation of a classification database for sulfatases reflecting their substrate specificity

T Barbeyron, L Brillet-Guéguen, W Carré, C Carrière… - PloS one, 2016 - journals.plos.org
Sulfatases cleave sulfate groups from various molecules and constitute a biologically and
industrially important group of enzymes. However, the number of sulfatases whose substrate …

What makes an enzyme promiscuous?

A Babtie, N Tokuriki, F Hollfelder - Current opinion in chemical biology, 2010 - Elsevier
Kinetic analyses of promiscuous enzymes reveal rate accelerations,(kcat/KM)/k2, of up to
1018 for their secondary activities. Such large values suggest that binding and catalysis can …

Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding

A Anandan, GL Evans… - Proceedings of the …, 2017 - National Acad Sciences
Multidrug-resistant (MDR) gram-negative bacteria have increased the prevalence of fatal
sepsis in modern times. Colistin is a cationic antimicrobial peptide (CAMP) antibiotic that …

[HTML][HTML] The crystal structure of the human polo‐like kinase‐1 polo box domain and its phospho‐peptide complex

KY Cheng, ED Lowe, J Sinclair, EA Nigg… - The EMBO …, 2003 - embopress.org
Human polo‐like kinase Plk1 localizes to the centrosomes, kinetochores and central spindle
structures during mitosis. It plays an essential role in promoting mitosis and cytokinesis …