The catalytic mechanisms of binuclear metallohydrolases
Binuclear metallohydrolases are a structurally diverse group of enzymes that use binuclear
metal ion centers to catalyze the hydrolysis of amides and esters of carboxylic and …
metal ion centers to catalyze the hydrolysis of amides and esters of carboxylic and …
The Mre11/Rad50/Nbs1 complex: recent insights into catalytic activities and ATP-driven conformational changes
TT Paull, RA Deshpande - Experimental cell research, 2014 - Elsevier
DNA double-strand breaks (DSBs) can arise from internal or external sources of damage,
and the rapid detection, processing, and repair of this damage is important for cell viability …
and the rapid detection, processing, and repair of this damage is important for cell viability …
Catalytic and noncatalytic roles of the CtIP endonuclease in double-strand break end resection
N Makharashvili, AT Tubbs, SH Yang, H Wang… - Molecular cell, 2014 - cell.com
The carboxy-terminal binding protein (CtBP)-interacting protein (CtIP) is known to function in
5′ strand resection during homologous recombination, similar to the budding yeast Sae2 …
5′ strand resection during homologous recombination, similar to the budding yeast Sae2 …
Enhanced access to the human phosphoproteome with genetically encoded phosphothreonine
Protein phosphorylation is a ubiquitous post-translational modification used to regulate
cellular processes and proteome architecture by modulating protein-protein interactions …
cellular processes and proteome architecture by modulating protein-protein interactions …
Cellular and Biophysical Applications of Genetic Code Expansion
HB Yi, S Lee, K Seo, H Kim, M Kim, HS Lee - Chemical Reviews, 2024 - ACS Publications
Despite their diverse functions, proteins are inherently constructed from a limited set of
building blocks. These compositional constraints pose significant challenges to protein …
building blocks. These compositional constraints pose significant challenges to protein …
Substrate-promoted formation of a catalytically competent binuclear center and regulation of reactivity in a glycerophosphodiesterase from Enterobacter aerogenes
KS Hadler, EA Tanifum, SHC Yip, N Mitic… - Journal of the …, 2008 - ACS Publications
The glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes is a promiscuous
binuclear metallohydrolase that catalyzes the hydrolysis of mono-, di-, and triester …
binuclear metallohydrolase that catalyzes the hydrolysis of mono-, di-, and triester …
[PDF][PDF] Metallophosphoesterases: structural fidelity with functional promiscuity.
N Matange, M Podobnik, SS Visweswariah - Biochemical journal, 2015 - researchgate.net
Calcineurin-like metallophosphoesterases (MPEs) form a large superfamily of binuclear
metal-ion-centre-containing enzymes that hydrolyse phosphomono-, phosphodi-or …
metal-ion-centre-containing enzymes that hydrolyse phosphomono-, phosphodi-or …
The structure and function of a novel glycerophosphodiesterase from Enterobacter aerogenes
CJ Jackson, PD Carr, JW Liu, SJ Watt, JL Beck… - Journal of molecular …, 2007 - Elsevier
The structure of the glycerophosphodiesterase (GDPD) from Enterobacter aerogenes,
GpdQ, has been solved by SAD phasing from the active site metal ions. Structural analysis …
GpdQ, has been solved by SAD phasing from the active site metal ions. Structural analysis …
Structural flexibility enhances the reactivity of the bioremediator glycerophosphodiesterase by fine-tuning its mechanism of hydrolysis
KS Hadler, N Mitic, F Ely, GR Hanson… - Journal of the …, 2009 - ACS Publications
The glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) belongs to the family
of binuclear metallohydrolases and has attracted recent attention due to its potential in …
of binuclear metallohydrolases and has attracted recent attention due to its potential in …
A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2′, 3′-cyclic nucleotide phosphodiesterase activity
N Keppetipola, S Shuman - Journal of Biological Chemistry, 2008 - ASBMB
Binuclear metallophosphoesterases are an enzyme superfamily defined by a shared fold
and a conserved active site. Although many family members have been characterized …
and a conserved active site. Although many family members have been characterized …