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Thematische Bibliographien / GH ENZYMES

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Auswahl der wissenschaftlichen Literatur zum Thema „GH ENZYMES“

Autor: Grafiati

Veröffentlicht am 11. September 2023

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Zeitschriftenartikel zum Thema "GH ENZYMES"

1

Malgas, Samkelo, Mpho S. Mafa, Brian N. Mathibe, and Brett I. Pletschke. "Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation." Molecules 26, no. 22 (2021): 6770. http://dx.doi.org/10.3390/molecules26226770.

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Enzymes classified with the same Enzyme Commission (EC) that are allotted in different glycoside hydrolase (GH) families can display different mechanisms of action and substrate specificities. Therefore, the combination of different enzyme classes may not yield synergism during biomass hydrolysis, as the GH family allocation of the enzymes influences their behavior. As a result, it is important to understand which GH family combinations are compatible to gain knowledge on how to efficiently depolymerize biomass into fermentable sugars. We evaluated GH10 (Xyn10D and XT6) and GH11 (XynA and Xyn2

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2

Vucinic, Jelena, Gleb Novikov, Cédric Montanier, Claire Dumon, Thomas Schiex, and Sophie Barbe. "A Comparative Study to Decipher the Structural and Dynamics Determinants Underlying the Activity and Thermal Stability of GH-11 Xylanases." International Journal of Molecular Sciences 22, no. 11 (2021): 5961. http://dx.doi.org/10.3390/ijms22115961.

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With the growing need for renewable sources of energy, the interest for enzymes capable of biomass degradation has been increasing. In this paper, we consider two different xylanases from the GH-11 family: the particularly active GH-11 xylanase from Neocallimastix patriciarum, NpXyn11A, and the hyper-thermostable mutant of the environmentally isolated GH-11 xylanase, EvXyn11TS. Our aim is to identify the molecular determinants underlying the enhanced capacities of these two enzymes to ultimately graft the abilities of one on the other. Molecular dynamics simulations of the respective free-enzy

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3

Angelov, Angel, Christoph Loderer, Susanne Pompei, and Wolfgang Liebl. "Novel Family of Carbohydrate-Binding Modules Revealed by the Genome Sequence of Spirochaeta thermophila DSM 6192." Applied and Environmental Microbiology 77, no. 15 (2011): 5483–89. http://dx.doi.org/10.1128/aem.00523-11.

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ABSTRACTSpirochaeta thermophilais a thermophilic, free-living, and cellulolytic anaerobe. The genome sequence data for this organism have revealed a high density of genes encoding enzymes from more than 30 glycoside hydrolase (GH) families and a noncellulosomal enzyme system for (hemi)cellulose degradation. Functional screening of a fosmid library whose inserts were mapped on theS. thermophilagenome sequence allowed the functional annotation of numerous GH open reading frames (ORFs). Seven different GH ORFs from theS. thermophilaDSM 6192 genome, all putative β-glycanase ORFs according to seque

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4

Iakiviak, Michael, Roderick I. Mackie, and Isaac K. O. Cann. "Functional Analyses of Multiple Lichenin-Degrading Enzymes from the Rumen Bacterium Ruminococcus albus 8." Applied and Environmental Microbiology 77, no. 21 (2011): 7541–50. http://dx.doi.org/10.1128/aem.06088-11.

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ABSTRACTRuminococcus albus8 is a fibrolytic ruminal bacterium capable of utilization of various plant cell wall polysaccharides. A bioinformatic analysis of a partial genome sequence ofR. albusrevealed several putative enzymes likely to hydrolyze glucans, including lichenin, a mixed-linkage polysaccharide of glucose linked together in β-1,3 and β-1,4 glycosidic bonds. In the present study, we demonstrate the capacity of four glycoside hydrolases (GHs), derived fromR. albus, to hydrolyze lichenin. Two of the genes encoded GH family 5 enzymes (Ra0453 and Ra2830), one gene encoded a GH family 16

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5

Abe, Koichi, Masahiro Nakajima, Tetsuro Yamashita та ін. "Biochemical and structural analyses of a bacterial endo-β-1,2-glucanase reveal a new glycoside hydrolase family". Journal of Biological Chemistry 292, № 18 (2017): 7487–506. http://dx.doi.org/10.1074/jbc.m116.762724.

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β-1,2-Glucan is an extracellular cyclic or linear polysaccharide from Gram-negative bacteria, with important roles in infection and symbiosis. Despite β-1,2-glucan's importance in bacterial persistence and pathogenesis, only a few reports exist on enzymes acting on both cyclic and linear β-1,2-glucan. To this end, we purified an endo-β-1,2-glucanase to homogeneity from cell extracts of the environmental species Chitinophaga arvensicola, and an endo-β-1,2-glucanase candidate gene (Cpin_6279) was cloned from the related species Chitinophaga pinensis. The Cpin_6279 protein specifically hydrolyzed

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6

Christensen, Stefan Jarl, Silke Flindt Badino, Ana Mafalda Cavaleiro, Kim Borch, and Peter Westh. "Functional analysis of chimeric TrCel6A enzymes with different carbohydrate binding modules." Protein Engineering, Design and Selection 32, no. 9 (2019): 401–9. http://dx.doi.org/10.1093/protein/gzaa003.

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Abstract The glycoside hydrolase (GH) family 6 is an important group of enzymes that constitute an essential part of industrial enzyme cocktails used to convert lignocellulose into fermentable sugars. In nature, enzymes from this family often have a carbohydrate binding module (CBM) from the CBM family 1. These modules are known to promote adsorption to the cellulose surface and influence enzymatic activity. Here, we have investigated the functional diversity of CBMs found within the GH6 family. This was done by constructing five chimeric enzymes based on the model enzyme, TrCel6A, from the so

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7

Ramirez, María Cecilia, Guillermina María Luque, Ana María Ornstein, and Damasia Becu-Villalobos. "Differential neonatal testosterone imprinting of GH-dependent liver proteins and genes in female mice." Journal of Endocrinology 207, no. 3 (2010): 301–8. http://dx.doi.org/10.1677/joe-10-0276.

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Abnormal exposure to steroid hormones within a critical developmental period elicits permanent alterations in female reproductive physiology in rodents, but the impact on the female GH axis and the underlying sexual differences in hepatic enzymes have not been described in detail. We have investigated the effect of neonatal androgenization of female mice (achieved by s.c. injection of 100 μg testosterone propionate (TP) on the day of birth: TP females) on the GHRH–somatostatin–GH axis and downstream GH targets, which included female and male predominant liver enzymes and secreted proteins. At

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8

Grøfte, Thorbjørn, Dorthe Svenstrup Jensen, Henning Grønbæk, et al. "Effects of growth hormone on steroid-induced increase in ability of urea synthesis and urea enzyme mRNA levels." American Journal of Physiology-Endocrinology and Metabolism 275, no. 1 (1998): E79—E86. http://dx.doi.org/10.1152/ajpendo.1998.275.1.e79.

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Growth hormone (GH) reduces the catabolic side effects of steroid treatment due to its effects on tissue protein synthesis/degradation. Little attention is focused on hepatic amino acid degradation and urea synthesis. Five groups of rats were given 1) placebo, 2) prednisolone, 3) placebo, pair fed to the steroid group, 4) GH, and 5) prednisolone and GH. After 7 days, the in vivo capacity of urea N synthesis (CUNS) was determined by saturating alanine infusion, in parallel with measurements of liver mRNA levels of urea cycle enzymes, N contents of organs, N balance, and hormones. Prednisolone i

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9

Janeček, Štefan, та Birte Svensson. "How many α-amylase GH families are there in the CAZy database?" Amylase 6, № 1 (2022): 1–10. http://dx.doi.org/10.1515/amylase-2022-0001.

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Abstract The CAZy database is a web-server for sequence-based classification of carbohydrate-active enzymes that has become the worldwide and indispensable tool for scientists engaged in this research field. It was originally created in 1991 as a classification of glycoside hydrolases (GH) and currently, this section of CAZy represents its largest part counting 172 GH families. The present Opinion paper is devoted to the specificity of α-amylase (EC 3.2.1.1) and its occurrence in the CAZy database. Among the 172 defined GH families, four, i.e. GH13, GH57, GH119 and GH126, may be considered as

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10

Olsson, Bob, Mohammad Bohlooly-Y, Ola Brusehed, et al. "Bovine growth hormone-transgenic mice have major alterations in hepatic expression of metabolic genes." American Journal of Physiology-Endocrinology and Metabolism 285, no. 3 (2003): E504—E511. http://dx.doi.org/10.1152/ajpendo.00444.2002.

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Transgenic mice overexpressing growth hormone (GH) have been extensively used to study the chronic effects of elevated serum levels of GH. GH is known to have many acute effects in the liver, but little is known about the chronic effects of GH overexpression on hepatic gene expression. Therefore, we used DNA microarray to compare gene expression in livers from bovine GH (bGH)-transgenic mice and littermates. Hepatic expression of peroxisome proliferator-activated receptor-α (PPARα) and genes involved in fatty acid activation, peroxisomal and mitochondrial β-oxidation, and production of ketone

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