Results 101 to 110 of about 5,034,587 (402)

Thermostable neutral metalloprotease from Geobacillus sp. EA1 does not share thermolysin's preference for substrates with leucine at the P1′ position

FEBS Letters, EarlyView.
Knowing how proteases recognise preferred substrates facilitates matching proteases to applications. The S1′ pocket of protease EA1 directs cleavage to the N‐terminal side of hydrophobic residues, particularly leucine. The S1′ pocket of thermolysin differs from EA's at only one position (leucine in place of phenylalanine), which decreases cleavage ...
Grant R. Broomfield, Torsten Kleffmann, David J. Saul, Sigurd M. Wilbanks   +3 more
wiley   +1 more source

Influence of enzymatic cow milk hydrolysates on IgA and IgG response of Balb/c mice organism

Czech Journal of Food Sciences, 2005
The manuscript presents the application of an animal model, Balb/c mice, in studies aimed at identifying among enzymatic hydrolysates of sodium caseinate and whey proteins the product with the most beneficial impact on the animal organism.
Barbara Wróblewska, Lucjan Jędrychowski   +1 more
doaj   +1 more source

Digging for biosynthetic dark matter. [PDF]

, 2015
An analysis of bacterial communities in soil samples from around the world reveals unexplored diversity in biosynthetic ...
Moore, Bradley S, Zhang, Jia Jia
core   +2 more sources

Redox‐dependent binding and conformational equilibria govern the fluorescence decay of NAD(P)H in living cells

FEBS Letters, EarlyView.
In this work, we reveal how different enzyme binding configurations influence the fluorescence decay of NAD(P)H in live cells using time‐resolved anisotropy imaging and fluorescence lifetime imaging microscopy (FLIM). Mathematical modelling shows that the redox states of the NAD and NADP pools govern these configurations, shaping their fluorescence ...
Thomas S. Blacker, Nimit Mistry, Nicoletta Plotegher, Elizabeth R. Westbrook, Michael D. E. Sewell, John Carroll, Gyorgy Szabadkai, Angus J. Bain, Michael R. Duchen   +8 more
wiley   +1 more source

Deubiquitylating enzymes and drug discovery: emerging opportunities

Nature reviews. Drug discovery, 2017
More than a decade after a Nobel Prize was awarded for the discovery of the ubiquitin–proteasome system and clinical approval of proteasome and ubiquitin E3 ligase inhibitors, first-generation deubiquitylating enzyme (DUB) inhibitors are now approaching ...
J. Harrigan, X. Jacq, N. Martin, S. Jackson   +3 more
semanticscholar   +1 more source

Neutrophil deficiency increases T cell numbers at the site of tissue injury in mice

FEBS Letters, EarlyView.
In wild‐type mice, injury or acute inflammation induces neutrophil influx followed by macrophage accumulation. Mcl1ΔMyelo (neutrophil‐deficient) mice lack neutrophils, and in response to muscle injury show fewer macrophages and exhibit strikingly elevated T‐cell numbers, primarily non‐conventional “double‐negative” (DN) αβ and γδ T cells.
Hajnalka Halász, Albert Bálint Papp, Lukács Sándor Lesinszki, Attila Mócsai, Tamás Varga, László Nagy, Péter Gogolák   +6 more
wiley   +1 more source

Elucidation of the noncovalent interactions driving enzyme activity guides branching enzyme engineering for α-glucan modification

Nature Communications
Branching enzymes (BEs) confer to α-glucans, the primary energy-storage reservoir in nature, a variety of features, like slow digestion. The full catalytic cycle of BEs can be divided in six steps, namely two covalent catalytic steps involving ...
Zhiyou Zong, Xuewen Zhang, Peng Chen, Zhuoyue Fu, Yan Zeng, Qian Wang, Christophe Chipot, Leila Lo Leggio, Yuanxia Sun   +8 more
doaj   +1 more source

Lysine Biosynthesis in Bacteria: A Metallodesuccinylase as a Potential Antimicrobial Target [PDF]

, 2012
In this review, we summarize the recent literature on dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase (DapE) enzymes, with an emphasis on structure–function studies that provide insight into the catalytic mechanism.
Becker, Daniel P., Gillner, Danuta, Holz, Richard C.   +2 more
core   +2 more sources

An enzyme in disguise [PDF]

IUCrJ, 2020
The enzyme carbonic anhydrase binds its zinc ion by three histidine residues in a similar manner to the way copper is bound to nitrite reductase. This remote similarity has now been shown to be real [Andring et al. (2020). IUCrJ, 7, 287-293]. A carbonic anhydrase with two bound copper ions is also a nitrite reductase.
openaire   +4 more sources

Mechanisms and kinetic assays of aminoacyl‐tRNA synthetases

FEBS Letters, EarlyView.
Igor Zivkovic, Morana Dulic, Ita Gruic‐Sovulj   +2 more
wiley   +1 more source