Results 31 to 40 of about 10,376,430 (391)

Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding [PDF]

, 2003
Two mutant forms of penicillin acylase from Escherichia coli strains, selected using directed evolution for the ability to use glutaryl-L-leucine for growth [Forney, Wong and Ferber (1989) Appl. Environ. Microbiol.
Brannigan, J A, Forney, L J, Ladurner, A G, McVey, C E, Morillas, M, Virden, R   +5 more
core   +2 more sources

Proteomics profiling of arginine methylation defines PRMT5 substrate specificity

Science Signaling, 2019
Proteomics identifies target sites and substrates of the arginine methyltransferase PRMT5. Profiling PRMT5 The enzyme PRMT5 methylates arginine residues in target proteins to modify their function.
D. Musiani, Jabez Bok, Enrico Massignani, Liling Wu, Tommaso Tabaglio, M. Ippolito, A. Cuomo, U. Ozbek, Habiba Zorgati, Umesh Ghoshdastider, R. Robinson, E. Guccione, T. Bonaldi   +12 more
semanticscholar   +1 more source

Substrate specificity and the effect of calcium on Trypanosomabrucei metacaspase 2 [PDF]

, 2013
Metacaspases are cysteine peptidases found only in yeast, plants and lower eukaryotes, including the protozoa. To investigate the extended substrate specificity and effects of Ca²⁺ on the activation of these enzymes, detailed ...
Juliano, L., Juliano, M.A., Machado, M.K.M, Marcondes, M.F., McLuskey, K., Moss, C.X., Mottram, J.C., Oliveira, V.   +7 more
core   +1 more source

Substrate specificity of human MCPIP1 endoribonuclease

Scientific Reports, 2018
MCPIP1, also known as Regnase-1, is a ribonuclease crucial for regulation of stability of transcripts related to inflammatory processes. Here, we report that MCPIP1 acts as an endonuclease by degrading several stem-loop RNA structures and single-stranded
Mateusz Wilamowski, Andrzej Gorecki, Marta Dziedzicka-Wasylewska, Jolanta Jura   +3 more
doaj   +1 more source

Bacillus anthracis edema factor substrate specificity: evidence for new modes of action [PDF]

, 2012
Since the isolation of Bacillus anthracis exotoxins in the 1960s, the detrimental activity of edema factor (EF) was considered as adenylyl cyclase activity only.
Agrawal, Altaweel, Basler, Bauche, Bell, Benson, Beste, Bock, Bond, Boyd, Bradley, Brown, Burhenne, Carbonetti, Carbonetti, Carson-Walter, Casteel, Christensen, Christensen, Confer, Copsel, Crawford, Crowe, Cunningham, Dalkas, Defer, Deuquet, Ding, Drum, Duesbery, Feld, Firoved, Friedlander, Fu, Fukuhara, Gaion, Gille, Gordon, Göttle, Hammerschmidt, He, Helfman, Hong, Ivarsson, Jernigan, Johnson, Katayama, Katayama, Kaupp, Kintzer, Klimpel, Laine, Larabee, Larabee, Leppla, Liu, Martin Göttle, McDonough, Milne, Mogridge, Mogridge, Newton, Newton, Newton, Newton, Newton, Oncu, O´Brien, Park, Petosa, Pezard, Postea, Puhar, Roland Seifert, Santelli, Scobie, Scobie, Scorpio, Shapiro, Shen, Shirshev, Soelaiman, Stefan Dove, Sun, Tamayo, Taylor, Taylor, Tesmer, Thomas, Tournier, Vitale, Vitale, Vojtova, Yeager, Zong   +94 more
core   +2 more sources

Crystal Structure and Substrate Specificity of PTPN12

Cell Reports, 2016
PTPN12 is an important tumor suppressor that plays critical roles in various physiological processes. However, the molecular basis underlying the substrate specificity of PTPN12 remains uncertain.
Hui Li, Fan Yang, Chunhua Liu, Peng Xiao, Yunfei Xu, Zonglai Liang, Chuan Liu, Hongmei Wang, Wenjun Wang, Wenshuai Zheng, Wei Zhang, Xiaoyun Ma, Dongfang He, Xiaoyuan Song, Fuai Cui, Zhigang Xu, Fan Yi, Jin-Peng Sun, Xiao Yu   +18 more
doaj   +1 more source

Error thresholds for self- and cross-specific enzymatic replication [PDF]

, 2010
The information content of a non-enzymatic self-replicator is limited by Eigen's error threshold. Presumably, enzymatic replication can maintain higher complexity, but in a competitive environment such a replicator is faced with two problems related to ...
Acevedo, Alves, Baake, Benedikt Obermayer, Blythe, Campos, Cech, de Oliveira, Doudna, Eigen, Eigen, Erwin Frey, Fernando, Fontanari, Galluccio, Gerland, Gilbert, Hermisson, Huynen, Johnston, Joyce, Komarova, Kun, Leuthäusser, Lilley, Lincoln, Lässig, Maynard Smith, Michod, Nowak, Obermayer, Orgel, Orgel, Pace, Peliti, Rajamani, Rawlings, Saakian, Saakian, Schuster, Stadler, Stadler, Summers, Swetina, Szathmáry, Szostak, Takeuchi, Takeuchi, von Kiedrowski, Wagner, Weiner, Wiehe, Wilke, Wilke, Woodcock, Wu, Zaher   +56 more
core   +4 more sources

Substrate Specificity in Thiol Dioxygenases.

Biochemistry, 2019
Thiol dioxygenases make up a class of ferrous iron-dependent enzymes that oxidize thiols to their corresponding sulfinates. X-ray diffraction structures of cysteine-bound cysteine dioxygenase show how cysteine is coordinated via its thiolate and amine to
Sekotilani Aloi, Casey G. Davies, P. Karplus, S. Wilbanks, Guy N. L. Jameson   +4 more
semanticscholar   +1 more source

Insights into a Cancer-Target Demethylase: Substrate Prediction through Systematic Specificity Analysis for KDM3A

Biomolecules, 2022
Jumonji C (JmjC) lysine demethylases (KDMs) catalyze the removal of methyl (-CH3) groups from modified lysyl residues. Several JmjC KDMs promote cancerous properties and these findings have primarily been in relation to histone demethylation.
Anand Chopra, William G. Willmore, Kyle K. Biggar   +2 more
doaj   +1 more source

Evolution of substrate specificity in a retained enzyme driven by gene loss. [PDF]

, 2017
The connection between gene loss and the functional adaptation of retained proteins is still poorly understood. We apply phylogenomics and metabolic modeling to detect bacterial species that are evolving by gene loss, with the finding that ...
Babnigg, Gyorgy, Barona-Gómez, Francisco, Carrillo-Tripp, Mauricio, Edirisinghe, Janaka N, Endres, Michael, Henry, Christopher S, Joachimiak, Andrzej, Juárez-Vázquez, Ana Lilia, Medina-Ruíz, Sofía, Michalska, Karolina, Noda-García, Lianet, Santoyo-Flores, Julián, Ton-That, Hung, Verduzco-Castro, Ernesto A, Wu, Chenggang   +14 more
core   +1 more source