The structure of the AliC GH13 α-amylase from Alicyclobacillus sp. reveals the accommodation of starch branching points in the α-amylase family

Autor: Jon Agirre, Olga Moroz, Sebastian Meier, Jesper Brask, Astrid Munch, Tine Hoff, Carsten Andersen, Keith S. Wilson, Gideon J. Davies

Publikováno v: Agirre, J, Moroz, O V, Meier, S, Braak, J, Munch, A, Hoff, T, Anderson, C, Wilson, K S & Davies, G J 2019, ' Structure of the AliC GH13 α−amylase from Alicyclobacillus sp, reveals accommodation of starch branching points in the α−amylase family ', Acta crystallographica Section D: Structural biology, vol. 75, no. 1, pp. 1-7 . https://doi.org/10.1107/S2059798318014900
Acta Crystallographica. Section D, Structural Biology

In the light of NMR data on product profiles, the structure of an Alicyclobacillus sp. CAZy family GH13 α-amylase highlights the accommodation of branch points in the α-amylase active centre.
α-Amylases are glycoside hydrolases that break the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb1beb76e85d03223d7bbfd1383d0873
https://eprints.whiterose.ac.uk/141278/1/dw5192.pdf

Action of different types of endoxylanases on eucalyptus xylan in situ

Autor: Vladimír Puchart, Peter Biely, Kristian B. R. M. Krogh, Tine Hoff, Lucia Fraňová

Publikováno v: Applied microbiology and biotechnology. 102(4)

Most studies of the mode of action of industrially important endoxylanases have been done on alkali extracted-plant xylan. In just few cases, the native form of the polysaccharide, acetylated xylan, was used as a substrate. In this work action of xyl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3515053373670316039844deb994b8d
https://pubmed.ncbi.nlm.nih.gov/29302718

Development of new α-amylases for raw starch hydrolysis

Autor: Carsten Andersen, Tine Hoff, Anders Viksø-Nielsen, Sven Pedersen

Publikováno v: Biocatalysis and Biotransformation. 24:121-127

This paper describes the discovery of a new 4 domain α-amylase from Anoxybacillus contaminans which very efficiently hydrolyses raw starch granules. Compared to traditional starch liquefying α-amylases, this new 4 domain α-amylase contains a starc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::15f598897dd89b00ecfb162092244d23
https://doi.org/10.1080/10242420500519191

Biochemical and genetic characterization of three molybdenum cofactor hydroxylases in Arabidopsis thaliana

Autor: Tine Hoff, Anne Rocher, Gitte I. Frandsen, John Mundy

Publikováno v: Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1398:397-402

Aldehyde oxidases and xanthine dehydrogenases/oxidases belong to the molybdenum cofactor dependent hydroxylase class of enzymes. Zymograms show that Arabidopsis thaliana has at least three different aldehyde oxidases and one xanthine oxidase. Three d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6da2a1aadaa6a0b8fa78b99883c0044
https://doi.org/10.1016/s0167-4781(98)00085-2

Structural basis for substrate recognition by Erwinia chrysanthemi GH30 glucuronoxylanase

Autor: Lubica, Urbániková, Mária, Vršanská, Kristian B R, Mørkeberg Krogh, Tine, Hoff, Peter, Biely

Publikováno v: The FEBS journal. 278(12)

Xylanase A from the phytopathogenic bacterium Erwinia chrysanthemi is classified as a glycoside hydrolase family 30 enzyme (previously in family 5) and is specialized for degradation of glucuronoxylan. The recombinant enzyme was crystallized with the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b87d73534404a6d4383f1828c12bc7b9
https://pubmed.ncbi.nlm.nih.gov/21501386