Results 41 to 50 of about 134,814 (288)

Modelling Reactions Catalysed by Carbohydrate-Active Enzymes [PDF]

, 2014
Abstract Carbohydrate polymers are ubiquitous in biological systems and their roles are highly diverse, ranging from energy storage over mechanical stabilisation to mediating cell-cell or cell-protein interactions. The functional diversity is mirrored by a chemical diversity that results from the high flexibility of how different sugar ...
Kartal, Önder, Ebenhöh, Oliver
openaire   +1 more source

Active-Site Engineering Switches Carbohydrate Regiospecificity in a Fungal Copper Radical Oxidase

, 2022
Copper radical oxidases (CROs) from Auxiliary Activity Family 5, Subfamily 2 (AA5_2), are organic cofactor-free biocatalysts for the selective oxidation of alcohols to the corresponding aldehydes.
Yann Mathieu (487812), Maria E. Cleveland (13204967), Harry Brumer (811100)   +2 more
core   +1 more source

Metagenomics approach to identify lignocellulose-degrading enzymes in the gut microbiota of the Chinese bamboo rat cecum

Electronic Journal of Biotechnology, 2021
Background: Lignocellulose is considered a renewable organic material, but the industrial production of biofuel from lignocellulose is challenging because of the lack of highly active hydrolytic enzymes.
Ding-Ping Bai, Xin-Yu Lin, Yu-Qiong Hu, Zhen-Zhen Chen, Lu Chen, Yi-Fan Huang, Xiao-Hong Huang, Jian Li   +7 more
doaj   +1 more source

High-quality draft genome sequence of Aquidulcibacter paucihalophilus TH1–2T isolated from cyanobacterial aggregates in a eutrophic lake

Standards in Genomic Sciences, 2017
Aquidulcibacter paucihalophilus TH1–2T is a member of the family Caulobacteraceae within Alphaproteobacteria isolated from cyanobacterial aggregates in a eutrophic lake. The draft genome comprises 3,711,627 bp and 3489 predicted protein-coding genes. The
Haiyuan Cai, Yonghui Zeng
doaj   +1 more source

Structure and function of the transketolase from Mycobacterium tuberculosis and comparison with the human enzyme [PDF]

, 2012
The transketolase (TKT) enzyme in Mycobacterium tuberculosis represents a novel drug target for tuberculosis treatment and has low homology with the orthologous human enzyme.
Jones, T. Alwyn, Elizabeth Fullam, Cole, Stewart T., Stewart T. Cole, Jones, T Alwyn, Florence Pojer, Fullam, Elizabeth, Pojer, Florence, Bergfors, Terese, Fullam, E., Cole, Stewart T, Bergfors, T., T. Alwyn Jones, Jones, T. A., Terese Bergfors, Pojer, F., Cole, S. T., Jones, T. Alwyn,, Bergfors, Terese,   +18 more
core   +1 more source

Systems approaches to predict the functions of glycoside hydrolases during the life cycle of Aspergillus niger using developmental mutants ∆brlA and ∆flbA.

PLoS ONE, 2015
BackgroundThe filamentous fungus Aspergillus niger encounters carbon starvation in nature as well as during industrial fermentations. In response, regulatory networks initiate and control autolysis and sporulation.
Jolanda M van Munster, Benjamin M Nitsche, Michiel Akeroyd, Lubbert Dijkhuizen, Marc J E C van der Maarel, Arthur F J Ram   +5 more
doaj   +1 more source

Cazypedia : carbohydrate-active enzymes, an introduction [PDF]

Glycobiology, 2011
CAZypedia is an online, community-driven effort to assemble a comprehensive encyclopedia of the enzymes and binding proteins involved in the synthesis and degradation of complex carbohydrates. An evolving encyclopedia of carbohydrate-active enzymes – ”CAZymes” CAZypedia is inspired by, and closely connected with, the actively curated CAZy Database (www.
Abbott Wade, Alber Orly, Bayer Ed, Berrin JeanGuy, Boraston Alisdair, Brumer Harry, Brzezinski Ryszard, Clarke Anthony, CobucciPonzano Beatrice, Cockburn Darrell, Coutinho Pedro, Czjzek Mirjam, Dassa Bareket, Davies Gideon John, Eijsink Vincent, Eklof Jens, Felice Alfons, FickoBlean Elizabeth, Pincher Geoff, Fontaine Thierry, Fujimoto Zui, Fujita Kiyotaka, Fushinobu Shinya, Gilbert Harry, Gloster Tracey, GoddardBorger Ethan, Greig Ian, Hehemann JanHendrik, Hemsworth Glyn, Henrissat Bernard, Hidaka Masafumi, HurtadoGuerrero Ramon, Igarashi Kiyohiko, Ishida Takuya, Janecek Stefan, Jongkees Seino, Juge Nathalie, Kaneko Satoshi, Katayama Takane, Kitaoka Motomitsu, Konno Naotake, Kracher Daniel, Kulminskaya Anna, van Bueren Alicia Lammerts, Larsen Sine, Lee Junho, Linder Markus, LoLeggio Leila, Ludwig Roland, Luis Ana, Maksimainen Mirko, Mark Brian, McLean Richard, Michel Gurvan, Michel Gurvan, Montanier Cedric, Moracci Marco, Mori Haruhide, Nakai Hiroyuki, Nerinckx Wim, Ohnuma Takayuki, Pickersgill Richard, Piens Kathleen, Pons Tirso, Rebuffet Etienne, Reilly Peter, RemaudSimeon Magali, Rempel Brian, Robinson Kyle, Rose David, Rouvinen Juha, Saburi Wataru, Sakamoto Yuichi, Sandgren Mats, Shaikh Fathima, Shoham Yuval, St John Franz, Stahlberg Jerry, Suits Michael, Sulzenbacher Gerlind, Sumida Tomomi, Suzuki Ryuichiro, Svensson Birte, Taira Toki, Taylor Ed, Tonozuka Takashi, Urbanowicz Breeanna, VaajeKolstad Gustav, Van den Ende Wim, Varrot Annabelle, Versluys Maxime, Vincent Florence, Vocadlo David, Wakarchuk Warren, Wennekes Tom, Williams Rohan, Williams Spencer, Wilson David, Withers Stephen, Yaoi Katsuro, Yip Vivian, Zhang Ran   +101 more
openaire   +9 more sources

Carbohydrate active enzyme domains in Chalara fraxinea

, 2013
Carbohydrate active enzyme domain analysis in Chalara fraxinea draft ...
Dan MacLean (415236)
core   +1 more source

The (Glg)ABCs of cyanobacteria: modelling of glycogen synthesis and functional divergence of glycogen synthases in Synechocystis sp. PCC 6803

FEBS Letters, EarlyView.
We reconstituted Synechocystis glycogen synthesis in vitro from purified enzymes and showed that two GlgA isoenzymes produce glycogen with different architectures: GlgA1 yields denser, highly branched glycogen, whereas GlgA2 synthesizes longer, less‐branched chains.
Kenric Lee, Dimitrios Bekiari, Sofia Doello, Karl Forchhammer   +3 more
wiley   +1 more source

Structural insights into an engineered feruloyl esterase with improved MHET degrading properties

FEBS Letters, EarlyView.
A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa, Konstantinos Makryniotis, Theofani‐Iosifina Sousani, Evangelos Topakas, Vangelis Daskalakis, Maria Dimarogona   +5 more
wiley   +1 more source