Results 61 to 70 of about 810,832 (336)

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

FEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang, Naoki Sunagawa, Toma Kashima, Kiyohiko Igarashi, Akimasa Miyanaga, Shinya Fushinobu   +5 more
wiley   +1 more source

Directed enzyme evolution: climbing fitness peaks one amino acid at a time [PDF]

, 2009
Directed evolution can generate a remarkable range of new enzyme properties. Alternate substrate specificities and reaction selectivities are readily accessible in enzymes from families that are naturally functionally diverse.
Arnold, Frances H., Tracewell, Cara A.
core   +2 more sources

The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity

FEBS Letters, EarlyView.
The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley   +1 more source

Substrate specificity of branched chain amino acid aminotransferases: The substitution of glycine to serine in the active site determines the substrate specificity for α-ketoglutarate

Frontiers in Catalysis, 2022
A branched chain aminotransferase from Thermoproteus tenax has been identified, cloned, over-expressed and biochemically characterised. A molecular modelling approach has been used to predict the 3D structure allowing its comparison with other related ...
Jan-Moritz Sutter, Daniel E. Mitchell, Marcel Schmidt, Michail N. Isupov, Jennifer A. Littlechild, Peter Schönheit   +5 more
doaj   +1 more source

A P-type ATPase importer that discriminates between essential and toxic transition metals [PDF]

, 2009
Transition metals, although being essential cofactors in many physiological processes, are toxic at elevated concentrations. Among the membrane-embedded transport proteins that maintain appropriate intracellular levels of transition metals are ATP-driven
A. T. Lee, Agranoff, Arguello, Arg  ello, Axelsen, Bal, Bull, D. C. Rees, Finney, Francis, Grass, Johnson, Krogh, Legatzki, Lewinson, Melchers, Nies, O. Lewinson, Papp-Wallace, Phung, Rensing, Schafer, Sharma, Thompson, Trenor, Vulpe   +25 more
core   +2 more sources

Substrate specificity of haloalkane dehalogenases [PDF]

Biochemical Journal, 2011
An enzyme's substrate specificity is one of its most important characteristics. The quantitative comparison of broad-specificity enzymes requires the selection of a homogenous set of substrates for experimental testing, determination of substrate-specificity data and analysis using multivariate statistics.
Tana, Koudelakova, Eva, Chovancova, Jan, Brezovsky, Marta, Monincova, Andrea, Fortova, Jiri, Jarkovsky, Jiri, Damborsky   +6 more
openaire   +2 more sources

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

FEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang, Satoshi Hashimoto, Sota Ito, Chisato Kikuguchi, Miho Hoshi, Kiyoshi Yamaguchi, Yoichi Furukawa, Toru Suzuki, Toshifumi Inada   +8 more
wiley   +1 more source

Fine-tuning of substrate preferences of the Src-family kinase Lck revealed through a high-throughput specificity screen

eLife, 2018
The specificity of tyrosine kinases is attributed predominantly to localization effects dictated by non-catalytic domains. We developed a method to profile the specificities of tyrosine kinases by combining bacterial surface-display of peptide libraries ...
Neel H Shah, Mark Löbel, Arthur Weiss, John Kuriyan   +3 more
doaj   +1 more source

Combining structure and sequence information allows automated prediction of substrate specificities within enzyme families. [PDF]

PLoS Computational Biology, 2010
An important aspect of the functional annotation of enzymes is not only the type of reaction catalysed by an enzyme, but also the substrate specificity, which can vary widely within the same family. In many cases, prediction of family membership and even
Marc Röttig, Christian Rausch, Oliver Kohlbacher   +2 more
doaj   +1 more source