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Relevant bibliographies by topics / GH13_18

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Journal articles

Academic literature on the topic 'GH13_18'

Author: Grafiati

Published: 4 June 2025

Last updated: 1 August 2025

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Journal articles on the topic "GH13_18"

1

Janíčková, Zuzana, та Štefan Janeček. "In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites". Molecules 26, № 18 (2021): 5704. http://dx.doi.org/10.3390/molecules26185704.

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This study brings a detailed bioinformatics analysis of fungal and chloride-dependent α-amylases from the family GH13. Overall, 268 α-amylase sequences were retrieved from subfamilies GH13_1 (39 sequences), GH13_5 (35 sequences), GH13_15 (28 sequences), GH13_24 (23 sequences), GH13_32 (140 sequences) and GH13_42 (3 sequences). Eight conserved sequence regions (CSRs) characteristic for the family GH13 were identified in all sequences and respective sequence logos were analysed in an effort to identify unique sequence features of each subfamily. The main emphasis was given on the subfamily GH13_

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2

Franceus, Jorick, and Tom Desmet. "A GH13 glycoside phosphorylase with unknown substrate specificity from Corallococcus coralloides." Amylase 3, no. 1 (2019): 32–40. http://dx.doi.org/10.1515/amylase-2019-0003.

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Abstract Glycoside phosphorylases in subfamily GH13_18 of the carbohydrate-active enzyme database CAZy catalyse the reversible phosphorolysis of α-glycosidic bonds. They contribute to a more energy-efficient metabolism in vivo, and can be applied for the synthesis of valuable glucosides, sugars or sugar phosphates in vitro. Continuing our efforts to uncover new phosphorylase specificities, we identified an enzyme from the myxobacterium Corallococcus coralloides DSM 2259 that does not feature the signature sequence patterns of previously characterised phosphorylases. The enzyme was recombinantl

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3

Franceus, Jorick, Nikolas Capra, Tom Desmet, and Andy-Mark W. H. Thunnissen. "Structural Comparison of a Promiscuous and a Highly Specific Sucrose 6F-Phosphate Phosphorylase." International Journal of Molecular Sciences 20, no. 16 (2019): 3906. http://dx.doi.org/10.3390/ijms20163906.

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In family GH13 of the carbohydrate-active enzyme database, subfamily 18 contains glycoside phosphorylases that act on α-sugars and glucosides. Because their phosphorolysis reactions are effectively reversible, these enzymes are of interest for the biocatalytic synthesis of various glycosidic compounds. Sucrose 6F-phosphate phosphorylases (SPPs) constitute one of the known substrate specificities. Here, we report the characterization of an SPP from Ilumatobacter coccineus with a far stricter specificity than the previously described promiscuous SPP from Thermoanaerobacterium thermosaccharolytic

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4

Desiderato, Andrea, Marcos Barbeitos, Clément Gilbert, and Jean-Luc Da Lage. "Horizontal Transfer and Gene Loss Shaped the Evolution of Alpha-Amylases in Bilaterians." G3: Genes|Genomes|Genetics 10, no. 2 (2019): 709–19. http://dx.doi.org/10.1534/g3.119.400826.

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The subfamily GH13_1 of alpha-amylases is typical of Fungi, but it is also found in some unicellular eukaryotes (e.g., Amoebozoa, choanoflagellates) and non-bilaterian Metazoa. Since a previous study in 2007, GH13_1 amylases were considered ancestral to the Unikonts, including animals, except Bilateria, such that it was thought to have been lost in the ancestor of this clade. The only alpha-amylases known to be present in Bilateria so far belong to the GH13_15 and 24 subfamilies (commonly called bilaterian alpha-amylases) and were likely acquired by horizontal transfer from a proteobacterium.

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5

Mareček, Filip, та Štefan Janeček. "A Novel Subfamily GH13_46 of the α-Amylase Family GH13 Represented by the Cyclomaltodextrinase from Flavobacterium sp. No. 92". Molecules 27, № 24 (2022): 8735. http://dx.doi.org/10.3390/molecules27248735.

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In the CAZy database, the α-amylase family GH13 has already been divided into 45 subfamilies, with additional subfamilies still emerging. The presented in silico study was undertaken in an effort to propose a novel GH13 subfamily represented by the experimentally characterized cyclomaltodxtrinase from Flavobacterium sp. No. 92. Although most cyclomaltodextrinases have been classified in the subfamily GH13_20. This one has not been assigned any GH13 subfamily as yet. It possesses a non-specified immunoglobulin-like domain at its N-terminus mimicking a starch-binding domain (SBD) and the segment

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6

Conchou, Léa, Juliette Martin, Isabelle R. Gonçalves, et al. "The Candida glabrata glycogen branching enzyme structure reveals unique features of branching enzymes of the Saccharomycetaceae phylum." Glycobiology 32, no. 4 (2021): 343–55. http://dx.doi.org/10.1093/glycob/cwab110.

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Abstract Branching enzymes (BE) are responsible for the formation of branching points at the 1,6 position in glycogen and starch, by catalyzing the cleavage of α-1,4-linkages and the subsequent transfer by introducing α-1,6-linked glucose branched points. BEs are found in the large GH13 family, eukaryotic BEs being mainly classified in the GH13_8 subfamily, GH13_9 grouping almost exclusively prokaryotic enzymes. With the aim of contributing to the understanding of the mode of recognition and action of the enzymes belonging to GH13_8, and to the understanding of features distinguishing these en

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7

Franceus, Jorik, and Tom Desmet. "Sucrose Phosphorylase and Related Enzymes in Glycoside Hydrolase Family 13: Discovery, Application and Engineering." International Journal of Molecular Sciences 21, no. 7 (2020): 2526. https://doi.org/10.3390/ijms21072526.

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<strong>Abstract</strong> Sucrose phosphorylases are carbohydrate-active enzymes with outstanding potential for the biocatalytic conversion of common table sugar into products with attractive properties. They belong to the glycoside hydrolase family GH13, where they are found in subfamily 18. In bacteria, these enzymes catalyse the phosphorolysis of sucrose to yield alpha-glucose 1-phosphate and fructose. However, sucrose phosphorylases can also be applied as versatile transglucosylases for the synthesis of valuable glycosides and sugars because their broad promiscuity allo

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8

Miyazaki, Takatsugu, та Enoch Y. Park. "Structure–function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17 exo-α-glucosidases". Journal of Biological Chemistry 295, № 26 (2020): 8784–97. http://dx.doi.org/10.1074/jbc.ra120.013595.

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The domestic silkworm Bombyx mori expresses two sucrose-hydrolyzing enzymes, BmSUH and BmSUC1, belonging to glycoside hydrolase family 13 subfamily 17 (GH13_17) and GH32, respectively. BmSUH has little activity on maltooligosaccharides, whereas other insect GH13_17 α-glucosidases are active on sucrose and maltooligosaccharides. Little is currently known about the structural mechanisms and substrate specificity of GH13_17 enzymes. In this study, we examined the crystal structures of BmSUH without ligands; in complexes with substrates, products, and inhibitors; and complexed with its covalent in

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9

Saka, Naoki, Dominggus Malle, Hiroyuki Iwamoto, Nobuyuki Takahashi, Kimihiko Mizutani, and Bunzo Mikami. "Relationship between the induced-fit loop and the activity of Klebsiella pneumoniae pullulanase." Acta Crystallographica Section D Structural Biology 75, no. 9 (2019): 792–803. http://dx.doi.org/10.1107/s2059798319010660.

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Klebsiella pneumoniae pullulanase (KPP) belongs to glycoside hydrolase family 13 subfamily 13 (GH13_13) and is the only enzyme that is reported to perform an induced-fit motion of the active-site loop (residues 706–710). Comparison of pullulanase structures indicated that only KPP has Leu680 present behind the loop, in contrast to the glycine found in other GH13_13 members. Analysis of the structure and activity of recombinant pullulanase from K. pneumoniae ATCC 9621 (rKPP) and its mutant (rKPP-G680L) indicated that the side chain of residue 680 is important for the induced-fit motion of the l

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10

Bharanidharan, Rajaraman, Jun Suk Byun, and Kyoung Hoon Kim. "PSVIII-16 Metagenomic Analyses of Microbial and Carbohydrate-Active Enzymes in the Rumen of Holstein Steers Supplemented with Seeds of Pharbitis nil." Journal of Animal Science 100, Supplement_3 (2022): 398–99. http://dx.doi.org/10.1093/jas/skac247.729.

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Abstract Our previous research revealed the effects of dietary supplementation of Pharbitis nil seeds (PA) in improving the ruminal methane reduction and digestibility in Hanwoo steers. The objective of this study was to further investigate the effects of PA supplementation on rumen microbial taxonomy, Kyoto Encyclopedia of Genes and Genomes (KEGG) Orthology functional categories and the diversity of carbohydrate-active enzymes (CAZymes). Five rumen cannulated Holstein steers (744 ± 35 kg) were fed either basal diet (Control) or basal diet supplemented with PA at 5% dry matter intake (PA5) for

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